Journal articles: 'Osteopontiini'

1

Choi, K. W., D. W. Kim, and S. W. Lee. "Purification and Properties of Osteopontin from Bovine Milk." Journal of Animal Science and Technology 45, no. 3 (June 30, 2003): 491–98. http://dx.doi.org/10.5187/jast.2003.45.3.491.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Chiu, Tai-Jan, Hung-I. Lu, Chang-Han Chen, Wan-Ting Huang, Yu-Ming Wang, Wei-Che Lin, and Shau-Hsuan Li. "Osteopontin Expression Is Associated with the Poor Prognosis in Patients with Locally Advanced Esophageal Squamous Cell Carcinoma Receiving Preoperative Chemoradiotherapy." BioMed Research International 2018 (2018): 1–9. http://dx.doi.org/10.1155/2018/9098215.

Full text

Abstract:

Background. The osteopontin has been involved in therapeutic resistance in a variety of cancers. But, the significance of osteopontin expression on the prognosis of patients with locally advanced esophageal squamous cell carcinoma (ESCC) receiving chemoradiotherapy is unclear.Methods.In 80 patients with locally advanced ESCC receiving preoperative chemoradiotherapy between 1999 and 2012, osteopontin expression was evaluated by immunohistochemistry and correlated with treatment outcome. The functional role of osteopontin in ESCC cell lines was determined by osteopontin-mediated siRNA.Results. Osteopontin expression and clinical T4 classification were significantly associated with poor pathological complete response. Univariate analyses demonstrated that osteopontin overexpression and clinical T classification, T4, were significantly associated with worse overall survival and disease-free survival. In multivariate comparison, osteopontin overexpression and clinical T classification, T4, represented the independent adverse prognosticator. In ESCC cell lines, endogenous osteopontin depletion by osteopontin-mediated siRNA increased sensitivity to cisplatin. Osteopontin expression is independently correlated with the response of chemoradiotherapy and prognosis of patients with locally advanced ESCC receiving preoperative chemoradiotherapy.Conclusions. Our results suggest that osteopontin may be a potential therapeutic target for patients with ESCC treated with preoperative chemoradiotherapy.

APA, Harvard, Vancouver, ISO, and other styles

3

Crivello, Joseph F., and E. Delvin. "Isolation and characterization of a cDNA for osteopontin-k: A kidney cell adhesion molecule with high homology to osteopontins." Journal of Bone and Mineral Research 7, no. 6 (December 3, 2009): 693–99. http://dx.doi.org/10.1002/jbmr.5650070614.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Sodek, J., B. Ganss, and M. D. McKee. "Osteopontin." Critical Reviews in Oral Biology & Medicine 11, no. 3 (July 2000): 279–303. http://dx.doi.org/10.1177/10454411000110030101.

Full text

Abstract:

Osteopontin (OPN) is a highly phosphorylated sialoprotein that is a prominent component of the mineralized extracellular matrices of bones and teeth. OPN is characterized by the presence of a polyaspartic acid sequence and sites of Ser/Thr phosphorylation that mediate hydroxyapatite binding, and a highly conserved RGD motif that mediates cell attachment/signaling. Expression of OPN in a variety of tissues indicates a multiplicity of functions that involve one or more of these conserved motifs. While the lack of a clear phenotype in OPN "knockout" mice has not established a definitive role for OPN in any tissue, recent studies have provided some novel and intriguing insights into the versatility of this enigmatic protein in diverse biological events, including developmental processes, wound healing, immunological responses, tumorigenesis, bone resorption, and calcification. The ability of OPN to stimulate cell activity through multiple receptors linked to several interactive signaling pathways can account for much of the functional diversity. In this review, we discuss the structural features of OPN I hat relate to its function in the formation, remodeling, and maintenance of bones and teeth.

APA, Harvard, Vancouver, ISO, and other styles

5

Scatena, Marta, Lucy Liaw, and Cecilia M. Giachelli. "Osteopontin." Arteriosclerosis, Thrombosis, and Vascular Biology 27, no. 11 (November 2007): 2302–9. http://dx.doi.org/10.1161/atvbaha.107.144824.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Szalay, Gudrun, Martina Sauter, Michael Haberland, Ulrich Zuegel, Andreas Steinmeyer, Reinhard Kandolf, and Karin Klingel. "Osteopontin." Circulation Research 104, no. 7 (April 10, 2009): 851–59. http://dx.doi.org/10.1161/circresaha.109.193805.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Shaheen, Mazen, and Neal L. Weintraub. "Osteopontin." Arteriosclerosis, Thrombosis, and Vascular Biology 27, no. 3 (March 2007): 439–41. http://dx.doi.org/10.1161/01.atv.0000258640.30287.7b.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Demer, Linda L., and Yin Tintut. "Osteopontin." Circulation Research 84, no. 2 (February 5, 1999): 250–52. http://dx.doi.org/10.1161/01.res.84.2.250.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Chellaiah, M. A., and K. A. Hruska. "Osteopontin." Drug News & Perspectives 11, no. 6 (1998): 350. http://dx.doi.org/10.1358/dnp.1998.11.6.863656.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Vogt, Mario HJ, Joop ten Kate, Roosmarie JM Drent, Chris H. Polman, and Raymond Hupperts. "Increased osteopontin plasma levels in multiple sclerosis patients correlate with bone-specific markers." Multiple Sclerosis Journal 16, no. 4 (January 19, 2010): 443–49. http://dx.doi.org/10.1177/1352458509359723.

Full text

Abstract:

The pro-inflammatory cytokine osteopontin has been found to be highly expressed in multiple sclerosis lesions and plasma levels are increased during relapses in relapse-onset multiple sclerosis patients. The objective was to determine the relationship between osteopontin plasma and cerebrospinal fluid levels in relation to the immunoglobulin G index. In addition, osteopontin plasma levels were compared with osteopontin mRNA levels in peripheral blood mononuclear cells and bone-specific markers to analyse whether osteopontin may be peripherally produced. Osteopontin and bone-specific markers were determined in paired plasma—cerebrospinal fluid samples and serum samples of relapse-onset multiple sclerosis patients ( n = 36), respectively. Osteopontin mRNA levels were determined by quantitative polymerase chain reaction analysis. Compared to healthy controls ( n = 20), plasma osteopontin levels were significantly increased in relapsing-remitting multiple sclerosis patients and correlated ( r = 0.43, p = 0.013) with the immunoglobulin G index. In contrast, cerebrospinal fluid osteopontin levels correlated neither with plasma osteopontin in paired samples nor with the immunoglobulin G index. Since osteopontin mRNA levels in peripheral blood mononuclear cells of relapsing-remitting multiple sclerosis patients did not correlate with osteopontin plasma levels, peripheral blood mononuclear cells might not be the major source for the increased osteopontin plasma levels. Osteopontin plasma levels correlated ( r = 0.42, p = 0.035) with the bone-specific degradation product C-telopeptide of type-1 collagen. In addition, another immunomodulatory molecule involved in bone metabolism, 25-OH vitamin D, correlated negatively ( r = —0.359, p = 0.048) with the immunoglobulin G index. This study suggests that bone-related molecules like osteopontin and vitamin D with important immunomodulatory functions are related to the immunoglobulin G index in relapsing-remitting multiple sclerosis patients.

APA, Harvard, Vancouver, ISO, and other styles

11

Feldreich, Tobias, Axel C. Carlsson, Johanna Helmersson-Karlqvist, Ulf Risérus, Anders Larsson, Lars Lind, and Johan Ärnlöv. "Urinary Osteopontin Predicts Incident Chronic Kidney Disease, while Plasma Osteopontin Predicts Cardiovascular Death in Elderly Men." Cardiorenal Medicine 7, no. 3 (2017): 245–54. http://dx.doi.org/10.1159/000476001.

Full text

Abstract:

Background and Objectives: The matricellular protein osteopontin is involved in the pathogenesis of both kidney and cardiovascular disease. However, whether circulating and urinary osteopontin levels are associated with the risk of these diseases is less studied. Design, Setting, Participants, and Measurements: A community-based cohort of elderly men (Uppsala Longitudinal Study of Adult Men [ULSAM]; n = 741; mean age: 77 years) was used to study the associations between plasma and urinary osteopontin, incident chronic kidney disease, and the risk of cardiovascular death during a median of 8 years of follow-up. Results: There was no significant cross-sectional correlation between plasma and urinary osteopontin (Spearman ρ = 0.07, p = 0.13). Higher urinary osteopontin, but not plasma osteopontin, was associated with incident chronic kidney disease in multivariable models adjusted for age, cardiovascular risk factors, baseline glomerular filtration rate, urinary albumin/creatinine ratio, and the inflammatory markers interleukin 6 and high-sensitivity C-reactive protein (odds ratio for 1 standard deviation [SD] of urinary osteopontin, 1.42, 95% CI 1.00-2.02, p = 0.048). Conversely, plasma osteopontin, but not urinary osteopontin, was independently associated with cardiovascular death (multivariable hazard ratio per SD increase, 1.35, 95% CI 1.14-1.58, p < 0.001, and 1.00, 95% CI 0.79-1.26, p = 0.99, respectively). The addition of plasma osteopontin to a model with established cardiovascular risk factors significantly increased the C-statistics for the prediction of cardiovascular death (p < 0.002). Conclusions: Higher urinary osteopontin specifically predicts incident chronic kidney disease, while plasma osteopontin specifically predicts cardiovascular death. Our data put forward osteopontin as an important factor in the detrimental interplay between the kidney and the cardiovascular system. The clinical implications, and why plasma and urinary osteopontin mirror different pathologies, remain to be established.

APA, Harvard, Vancouver, ISO, and other styles

12

Merry, K., R. Dodds, A. Littlewood, and M. Gowen. "Expression of osteopontin mRNA by osteoclasts and osteoblasts in modelling adult human bone." Journal of Cell Science 104, no. 4 (April 1, 1993): 1013–20. http://dx.doi.org/10.1242/jcs.104.4.1013.

Full text

Abstract:

Over recent years several non-collagenous matrix proteins of bone have been isolated and characterized. One of these proteins, osteopontin, has been shown to be synthesized by osteoblasts and deposited in the bone matrix where it is thought to bind to hydroxyapatite. However much of the functional evidence is circumstantial, and the precise function of osteopontin has not been fully elucidated. We have used in situ hybridization techniques to investigate the expression of osteopontin mRNA in a variety of human bone tissues. Cryostat sections of human osteophyte and osteoclastoma tissue were hybridized with an antisense RNA probe for osteopontin. Sense transcripts were used as a negative control to assess non-specific binding. There was a very distinct pattern of osteopontin mRNA expression in these tissues. Plump osteoblasts adjacent to the osteoid matrix expressed high levels of osteopontin mRNA, whilst flattened osteoblasts demonstrated weaker expression. The most striking feature of osteopontin mRNA expression was the high levels detected in osteoclasts. Osteoclasts in resorption lacunae and those distant from resorption sites both expressed osteopontin mRNA, suggesting that attachment was not a prerequisite for osteopontin expression. A population of mononuclear cells in resorption lacunae was also observed to express high levels of osteopontin mRNA. The whole population of osteoclasts in the osteoclastoma tissue expressed high levels of osteopontin mRNA, indicating that expression is not restricted to osteoclasts involved in bone resorption. This study confirms that human osteoblasts are capable of synthesizing osteopontin.(ABSTRACT TRUNCATED AT 250 WORDS)

APA, Harvard, Vancouver, ISO, and other styles

13

Berman, Jeffrey S., David Serlin, Xinfang Li, Geoffrey Whitley, John Hayes, David C. Rishikof, Dennis A. Ricupero, Lucy Liaw, Margaret Goetschkes, and Anthony W. O'Regan. "Altered bleomycin-induced lung fibrosis in osteopontin-deficient mice." American Journal of Physiology-Lung Cellular and Molecular Physiology 286, no. 6 (June 2004): L1311—L1318. http://dx.doi.org/10.1152/ajplung.00394.2003.

Full text

Abstract:

Osteopontin is a multifunctional matricellular protein abundantly expressed during inflammation and repair. Osteopontin deficiency is associated with abnormal wound repair characterized by aberrant collagen fibrillogenesis in the heart and skin. Recent gene microarray studies found that osteopontin is abundantly expressed in both human and mouse lung fibrosis. Macrophages and T cells are known to be major sources of osteopontin. During lung fibrosis, however, osteopontin expression continues to increase when inflammation has receded, suggesting alternative sources of ostepontin during this response. In this study, we demonstrate immunoreactivity for osteopontin in lung epithelial and inflammatory cells in human usual interstitial pneumonitis and murine bleomycin-induced lung fibrosis. After treatment with bleomycin, osteopontin-null mice develop lung fibrosis characterized by dilated distal air spaces and reduced type I collagen expression compared with wild-type controls. There is also a significant decrease in levels of active transforming growth factor-β1 and matrix metalloproteinase-2 in osteopontin null mice. Type III collagen expression and total collagenase activity are similar in both groups. These results demonstrate that osteopontin expression is associated with important fibrogenic signals in the lung and that the epithelium may be an important source of osteopontin during lung fibrosis.

APA, Harvard, Vancouver, ISO, and other styles

14

Brown, L. F., B. Berse, L. Van de Water, A. Papadopoulos-Sergiou, C. A. Perruzzi, E. J. Manseau, H. F. Dvorak, and D. R. Senger. "Expression and distribution of osteopontin in human tissues: widespread association with luminal epithelial surfaces." Molecular Biology of the Cell 3, no. 10 (October 1992): 1169–80. http://dx.doi.org/10.1091/mbc.3.10.1169.

Full text

Abstract:

Osteopontin, a glycoprotein with a glycine-arginine-glycine-aspartate-serine (GRGDS) cell-binding domain, has been described in bone and is also known to be expressed in other organs, particularly kidney. The goal of the present work was to define the distribution of osteopontin synthesis and deposition in a wide variety of normal adult human tissues using a multifaceted approach that included immunohistochemistry, in situ hybridization, and Northern analysis. Immunohistochemical studies have revealed the unexpected finding that osteopontin is deposited as a prominent layer at the luminal surfaces of specific populations of epithelial cells of the gastrointestinal tract, gall bladder, pancreas, urinary and reproductive tracts, lung, breast, salivary glands, and sweat glands. Northern analyses identified gallbladder as a major site of osteopontin gene transcription comparable in magnitude with that of kidney, and immunoblotting identified osteopontin in bile. In situ hybridization localized osteopontin gene transcripts predominantly to the epithelium of a variety of organs as well as to ganglion cells of bowel wall. Osteopontin of epithelial cell origin, like bone-derived osteopontin, promoted GRGDS-dependent cell spreading in attachment assays. We postulate that osteopontin secreted by epithelium binds integrins on luminal surfaces. Collectively, these findings suggest an important role for osteopontin on many luminal epithelial surfaces communicating with the external environment.

APA, Harvard, Vancouver, ISO, and other styles

15

HUDKINS, KELLY L., CECILIA M. GIACHELLI, YAN CUI, WILLIAM G. COUSER, RICHARD J. JOHNSON, and CHARLES E. ALPERS. "Osteopontin Expression in Fetal and Mature Human Kidney." Journal of the American Society of Nephrology 10, no. 3 (March 1999): 444–57. http://dx.doi.org/10.1681/asn.v103444.

Full text

Abstract:

Abstract. Osteopontin is a secreted phosphoprotein that is expressed by normal kidney, and has been associated with a number of functions including cell adhesion, migration, signaling, and biomineralization. Although there is a vast literature detailing osteopontin localization in various rodent models of both development and disease, this article presents the first comprehensive description of osteopontin localization in human kidney. In this study, immunohistochemistry, immunoelectron microscopy,in situhybridization, and Northern blotting are used to analyze osteopontin protein and mRNA expression in human fetal and normal mature renal tissue. Osteopontin is expressed in the human embryonic renal tubular epithelium beginning on approximately day 75 to 80 of gestation. In the fetal kidney, osteopontin can also be seen occasionally expressed in the ureteric buds and in some interstitial cells. As localized at the protein and mRNA level, the tubular expression of osteopontin increases with increasing gestational age and persists into adulthood. In the normal adult kidney, osteopontin is localized primarily to the distal nephron and is strongly expressed by the thick ascending limb of the loops of Henle. Osteopontin expression can also be observed in some collecting duct epithelium. In cases that exhibit foci of interstitial fibrosis and an associated influx of interstitial macrophages, osteopontin expression is significantly upregulated in all tubular segments, including proximal tubules.

APA, Harvard, Vancouver, ISO, and other styles

16

Marques, Durval Santos, Jessica Grativol, Rodrigo Alves da Silva Peres, Aline da Rocha Matos, and Etel Rodrigues Pereira Gimba. "Osteopontin-c isoform levels are associated with SR and hnRNP differential expression in ovarian cancer cell lines." Tumor Biology 39, no. 9 (September 2017): 101042831772544. http://dx.doi.org/10.1177/1010428317725442.

Full text

Abstract:

Osteopontin-c splicing isoform activates ovarian cancer progression features. Imbalanced expression of splicing factors from serine/arginine -rich and heterogeneous ribonucleoproteins families has been correlated with the generation of oncogenic splicing isoforms. Our goal was to investigate whether there is any association between the transcriptional patterns of these splicing factors in ovarian cells and osteopontin-c expression levels. We also aimed to investigate the occurrence of these splicing factors binding sites inside osteopontin exon 4 and adjacent introns. To test associations between osteopontin-c and splicing factors expression patterns, we used an in vitro model in which OVCAR-3 cells overexpressing osteopontin-c (OVCAR-3/OPNc++) presented higher transcriptional levels of osteopontin-c than two other ovarian carcinoma cells (TOV-112D, SKOV-3) and ovarian non-tumoral cell lines (IOSE 364 and IOSE 385). The transcriptional levels of osteopontin-c, serine/arginine-rich, and hnRNP factors were evaluated using real-time polymerase chain reaction. Human Splice Finder software was used to search for putative splicing factor binding sites in osteopontin genomic regions. OVCAR-3/OPNc++ cells presented higher transcriptional levels of hnRNP than serine/arginine-rich when compared to TOV-112D, SKOV-3, and IOSE cells. TOV-112D and SKOV-3 cells also overexpressed hnRNP in relation to serine/arginine-rich transcripts. Putative binding sites for these splicing factors have been predicted on osteopontin exon 4 and their upstream and downstream intronic regions. Our data showed that higher osteopontin-c expression levels are associated with a predominance of hnRNP in relation to serine/arginine-rich transcripts and that osteopontin exon 4 and adjacent intronic sequences contain predicted binding sites for some of these tested splicing factors. In conclusion, differential expression of these splicing factors in ovarian cancer cells could be one of the putative mechanisms leading to aberrant splicing of the osteopontin primary transcript. Future work, aiming to control ovarian cancer progression by downregulating osteopontin-c levels, could include strategies that also regulate heterogeneous ribonucleoproteins and serine/arginine-rich expression levels in order to modulate osteopontin splicing.

APA, Harvard, Vancouver, ISO, and other styles

17

Lamort, Anne-Sophie, Ioanna Giopanou, Ioannis Psallidas, and Georgios T. Stathopoulos. "Osteopontin as a Link between Inflammation and Cancer: The Thorax in the Spotlight." Cells 8, no. 8 (August 2, 2019): 815. http://dx.doi.org/10.3390/cells8080815.

Full text

Abstract:

The glycoprotein osteopontin (OPN) possesses multiple functions in health and disease. To this end, osteopontin has beneficial roles in wound healing, bone homeostasis, and extracellular matrix (ECM) function. On the contrary, osteopontin can be deleterious for the human body during disease. Indeed, osteopontin is a cardinal mediator of tumor-associated inflammation and facilitates metastasis. The purpose of this review is to highlight the importance of osteopontin in malignant processes, focusing on lung and pleural tumors as examples.

APA, Harvard, Vancouver, ISO, and other styles

18

Bayless, K. J., G. A. Meininger, J. M. Scholtz, and G. E. Davis. "Osteopontin is a ligand for the alpha4beta1 integrin." Journal of Cell Science 111, no. 9 (May 1, 1998): 1165–74. http://dx.doi.org/10.1242/jcs.111.9.1165.

Full text

Abstract:

Recent work has shown that osteopontin expression is upregulated at sites of cardiovascular injury. It has been hypothesized that osteopontin provides an adhesive matrix for endothelial and smooth muscle cells during remodeling of the vascular wall following injury. Osteopontin has also been found to be synthesized by monocytes and macrophages within injury sites. Here, we present data showing that osteopontin can promote leukocyte adhesion through the alpha4beta1 integrin. In the presence of physiologic concentrations of Mg2+ and Ca2+, osteopontin purified from bovine milk promoted cell-substrate adhesion of HL-60 and Ramos cells, two model leukocyte cell lines. As with other adhesive ligands, adhesion to osteopontin required leukocyte activation. Under these conditions, no adhesion to control substrates such as bovine serum albumin was observed. Leukocyte adhesion was inhibited by anti-integrin antibodies directed at either the alpha4 or beta1 integrin subunits but not by control antibodies directed to other integrins. Further adhesion experiments revealed that leukocyte binding to osteopontin was completely inhibited by an alpha4beta1-binding peptide containing the leucine-aspartate-valine (LDV) sequence, while a control, non-binding peptide containing leucine-glutamate-valine (LEV) had minimal effects. Affinity chromatography using either surface labeled HL-60 or Ramos cell extracts revealed that the alpha4beta1 integrin specifically bound to osteopontin. Immunoprecipitation of eluted fractions from these columns positively identified the alpha4beta1 integrin. In order to localize potential alpha4beta1-binding sites within osteopontin, the protein was proteolytically cleaved with thrombin. A 30 kDa N-terminal osteopontin fragment purified using fast protein liquid chromatography promoted alpha4beta1 dependent leukocyte adhesion in a manner similar to that of the intact protein. These data collectively demonstrate that the alpha4beta1 integrin is a new adhesion receptor for osteopontin and that an alpha4beta1 binding site exists in the NH2-terminal thrombin fragment of osteopontin.

APA, Harvard, Vancouver, ISO, and other styles

19

Hong, Qu, Lawrence F. Brown, Harold F. Dvorak, and Ann M. Dvorak. "Ultrastructural Immunogold Localization of Osteopontin in Human Gastric Mucosa." Journal of Histochemistry & Cytochemistry 45, no. 1 (January 1997): 21–33. http://dx.doi.org/10.1177/002215549704500104.

Full text

Abstract:

We performed ultrastructural immunogold localization of osteopontin in the mucosa of human stomach. This adhesive glycoprotein was present in mucous and chief cells of the epithelial layer and in macrophages in the lamina propria. Parietal and endocrine cells of the epithelial layer and mast cells and plasma cells in the lamina propria did not contain osteopontin, serving as internal negative controls. Subcellular localizations of osteopontin included secretory granules and synthetic organelles in mucous and chief cells and phagolysosomes in macrophages. Extracellular concentrations of osteopontin were present in the glycocalyx and in an electron-lucent band between epithelial surface cells and the gastric lumen. Paracellular edema between the epithelium of the same cells was devoid of osteopontin. Immunogold localization of pepsinogen II was done to identify cells with mixed granule populations and contents of multicompartmental secretory granules. These studies revealed mucous cell granules and chief cell granules, each containing compartmentalized storage products, which included osteopontin and mucigen in mucous cells and osteopontin and pepsinogen II in chief cells. Cytochemical controls for the immunogold localizations were negative. The subcellular distribution of osteopontin in human gastric mucosa suggests possible roles for this glycoprotein in barrier function, host defense, and/or secretion.

APA, Harvard, Vancouver, ISO, and other styles

20

Loosen, Sven, Daniel Heise, Cees Dejong, Sanchari Roy, Frank Tacke, Christian Trautwein, Christoph Roderburg, Tom Luedde, Ulf Neumann, and Marcel Binnebösel. "Circulating Levels of Osteopontin Predict Patients’ Outcome after Resection of Colorectal Liver Metastases." Journal of Clinical Medicine 7, no. 11 (October 26, 2018): 390. http://dx.doi.org/10.3390/jcm7110390.

Full text

Abstract:

For colorectal liver metastases (CRLM), surgical resection is the only potentially curative therapy, but even successfully resected patients often face disease recurrence, leading to 5-year survival rate below 50%. Despite available preoperative stratification strategies, it is not fully elucidated which patients actually benefit from CRLM resection. Here we evaluated osteopontin, a secreted glyco-phosphoprotein, as a biomarker in the context of CRLM resection. Tissue levels of osteopontin were analysed in CRLM using reverse transcription polymerase chain reaction (RT-PCR) and immunohistochemistry. Pre- and postoperative osteopontin serum concentrations were analysed by enzyme-linked immunosorbent assay (ELISA) in 125 patients undergoing resection of CRLM as well as 65 healthy controls. Correlating with an upregulation of osteopontin tissue expression in CRLM, osteopontin serum levels were significantly elevated in patients with CRLM compared to healthy controls. Importantly, high pre- and post-operative osteopontin serum levels were associated with a poor prognosis after tumour resection. Patients with initial osteopontin serum levels above our ideal cut-off value of 264.4 ng/mL showed a significantly impaired median overall survival of 304 days compared to 1394 days for patients with low osteopontin levels. Together, our data suggest a role of osteopontin as a prognostic biomarker in patients with resectable CRLM that might help to identify patients who particularly benefit from liver resection.

APA, Harvard, Vancouver, ISO, and other styles

21

Pilli, Ganga S., Prakash V. Patil, and SG Karadesai. "Osteopontin as a Prognostic Indicator in Grading of Ovarian Epithelial Tumors." Journal of South Asian Federation of Obstetrics and Gynaecology 7, no. 2 (2015): 61–63. http://dx.doi.org/10.5005/jp-journals-10006-1324.

Full text

Abstract:

ABSTRACT Aim To determine if osteopontin expression by immunohistochemistry (IHC) can correlate with histological type and grade of epithelial ovarian cancer. Materials and methods The present work has been carried out at department of pathology, of a reputed medical college in Belgaum district of Karnataka state. The study is carried out for a period of 18 months for data collection, evaluation of the marker and data analysis. All consecutive specimens of ovarian tumors are included in the study. The study included 55 epithelial ovarian tumors and these are analyzed histopathologically. In all the cases, osteopontin expression has been studied with IHC on paraffin slides. Results This study included 41 (74.5%) benign tumors and 14 (25.5%) malignant tumors. High grade (grade III) was common in serous carcinomas than in other histological types. Fisher's exact test p-value < 0.001 was significant for expression of osteopontin and all the malignant ovarian epithelial tumors expressed osteopontin by IHC procedure on paraffin tissue sections. All high-grade epithelial ovarian tumors showed increased expression of osteopontin of +++ and low-grade tumors expressed +/++osteopontin. Conclusion The osteopontin expression was seen in all the malignant epithelial ovarian cancers and the osteopontin expression was significantly higher in high-grade epithelial ovarian cancers than low-grade epithelial ovarian cancers. How to cite this article Pilli GS, Patil PV, Karadesai SG. Osteopontin as a Prognostic Indicator in Grading of Ovarian Epithelial Tumors. J South Asian Feder Obst Gynae 2015;7(2): 61-63.

APA, Harvard, Vancouver, ISO, and other styles

22

Choi, Steve S., Lee C. Claridge, Ravi Jhaveri, Marzena Swiderska-Syn, Paul Clark, Ayako Suzuki, Thiago A. Pereira, et al. "Osteopontin is up-regulated in chronic hepatitis C and is associated with cellular permissiveness for hepatitis C virus replication." Clinical Science 126, no. 12 (February 26, 2014): 845–55. http://dx.doi.org/10.1042/cs20130473.

Full text

Abstract:

Osteopontin is up-regulated in patients with chronic hepatitis C, and directly promotes hepatitis C replication. Reducing osteopontin represses hepatitis C levels. Serum osteopontin levels correlate with disease severity and may predict response to anti-viral treatment.

APA, Harvard, Vancouver, ISO, and other styles

23

Angelucci, Adriano, Claudio Festuccia, Gabriele DAndrea, Anna Teti, and Mauro Bologna. "Osteopontin Modulates Prostate Carcinoma Invasive Capacity through RGD-Dependent Upregulation of Plasminogen Activators." Biological Chemistry 383, no. 1 (January 23, 2002): 229–34. http://dx.doi.org/10.1515/bc.2002.024.

Full text

Abstract:

Abstract Osteopontin, a noncollageneous bone matrix protein, is produced in several human tumors but its role in cancer progression has been only partially elucidated. In this study we investigated the potential role of osteopontin in the malignancy of prostate cancer cells. Chemotaxis and chemoinvasion analyses revealed a dosedependent increase in PC3 cell movement induced by osteopontin and a strict dependence of cell invasion on αvβ3 integrin function. The pattern of protease expression was modified by osteopontin and was characterized by an upregulation of plasminogen activators. Our findings suggest that osteopontin may confer selective malignant potential to prostate cancer cells through the enhancement of their invasive and proteolytic capability.

APA, Harvard, Vancouver, ISO, and other styles

24

Hotte, Sebastien J., Eric W. Winquist, Larry Stitt, Sylvia M. Wilson, and Ann F. Chambers. "Plasma osteopontin." Cancer 95, no. 3 (July 23, 2002): 506–12. http://dx.doi.org/10.1002/cncr.10709.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

RODAN, GIDEON A. "Osteopontin Overview." Annals of the New York Academy of Sciences 760, no. 1 Osteopontin (August 1995): 1–5. http://dx.doi.org/10.1111/j.1749-6632.1995.tb44614.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Pero, M. E., G. J. Killian, P. Lombardi, L. Zicarelli, L. Avallone, and B. Gasparrini. "327 IDENTIFICATION OF OSTEOPONTIN IN WATER BUFFALO SEMEN." Reproduction, Fertility and Development 19, no. 1 (2007): 279. http://dx.doi.org/10.1071/rdv19n1ab327.

Full text

Abstract:

The competitiveness of buffalo breeding will depend on the utilization of reproductive biotechnologies that allows acceleration of genetic progress. A major factor hampering the efficiency of both artificial insemination and in vitro embryo production programs in this species is male hypofertility. Reports for several species suggest that seminal plasma contains factors that influence male fertility. Osteopontin is a glycoprotein found in several biological fluids including seminal plasma, and its presence is associated with spermatozoa concentration. In cattle, expression of osteopontin was highly correlated with bull fertility, and it was proposed to be a marker to predict male fertility (Cancel et al. 1999 Biol. Reprod. 60, 454–460). No data are available about the presence or activity of osteopontin in water buffalo. The aim of this preliminary study was to determine if osteopontin is present in buffalo semen and to evaluate whether freezing procedures cause the loss of osteopontin from spermatozoa. Semen was collected in authorized semen collection centers from 6 buffalo bulls by using an artificial vagina. A collection of bovine semen was used as a positive control. An aliquot from each sample was frozen using standard procedures for semen storage. Each ejaculate was centrifuged at 600g for 10 min at room temperature, and the supernatant was recovered and centrifuged at 10 000g for 1 h at 4�C. The total protein concentration in seminal plasma and spermatozoa was determined by the Bradford method, using ovoalbumin as the standard. Proteins (50 �g) were separated by electrophoresis and analyzed by western blotting (Cancel et al. 1999). Polyclonal antibodies against bovine milk osteopontin were prepared as previously described (Cancel et al. 1997 Biol. Reprod. 57, 1293–1301). The intensities of bands indicated by western blot were quantified by densitometer. Osteopontin was detected in all samples of buffalo semen. Most of the osteopontin detected was in the seminal plasma. Relative amounts of osteopontin detected in spermatozoa were 50% or less of that detected in seminal plasma; furthermore, the protein was not found in sperm from all bulls. These results suggest that most osteopontin is produced by the ampullae and seminal vesicles, similar to what was reported for cattle (Cancel et al. 1999). Semen frozen by standard procedures showed a reduction in amount of osteopontin by up to 50%. These studies suggest that the fertility-associated protein osteopontin may be useful as a sensitive tool to evaluate whether sperm storage procedures are detrimental and result in excess loss of osteopontin from sperm. In conclusion, the results have demonstrated that osteopontin is present in buffalo seminal plasma and sperm. Further studies will examine whether the expression of osteopontin is correlated with the fertility of buffalo bulls, as has been demonstrated in bovine bulls.

APA, Harvard, Vancouver, ISO, and other styles

27

Coombes, Jason D., and Wing-Kin Syn. "Differential osteopontin functions: The role of osteopontin isoforms." Hepatology 62, no. 1 (May 6, 2015): 323–24. http://dx.doi.org/10.1002/hep.27555.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Abd El Dayem, Soha M., Abo El Magd El Bohy, Ahmed A. Battah, Mona Hamed, and Shereen Hamdy Abd El Aziz. "Osteopontin for Early Detection of Microvascular and Macrovascular Type 1 Diabetic Complication." Open Access Macedonian Journal of Medical Sciences 7, no. 21 (November 13, 2019): 3619–22. http://dx.doi.org/10.3889/oamjms.2019.613.

Full text

Abstract:

AIM: To evaluate the relationship between osteopontin and diabetes complication in type 1 diabetic patient. PATIENTS AND METHODS: Seventy types 1 diabetic and 60 healthy volunteers were studied. Full history, examination, laboratory tests of glycosylated haemoglobin (HbA1c), serum lipids {cholesterol, triglyceride (Tg), high-density lipoprotein-cholesterol (HDL-c), low-density lipoprotein – cholesterol (LDL-c)}, oxidised low-density lipoprotein (OxLDL), Osteopontin and urinary microalbuminuria (albumin/creatinine ratio) were done. Image study in the form of a carotid intimal medial thickness (cIMT) and aortic intimal medial thickness (aIMT), renal doppler for resistivity index was also done for all participant included in the study. RESULTS: Urinary albumin/creatinine ratio, lipid profile, osteopontin, cIMT and aIMT were higher in people with diabetes. Osteopontin was higher in people with diabetes with positive microalbuminuria and cIMT. Systolic blood pressure, microalbuminuria and cIMT had a positive correlation with osteopontin in people with diabetes. Stepwise multiple regression analysis showed that osteopontin had a significant correlation with cIMT. Receiver operating characteristic (ROC) curve showed that the cut off value of Osteopontin for detection of cIMT was > 60 with a specificity of 100% and sensitivity 80.5%, while that of albumin/creatinine ratio was > 64 with a specificity of 66.7 and sensitivity of 92.3. CONCLUSION: Osteopontin is higher in type 1 diabetics and is useful for early detection of diabetic microvascular and macrovascular complication.

APA, Harvard, Vancouver, ISO, and other styles

29

Rogers, S. A., B. J. Padanilam, K. A. Hruska, C. M. Giachelli, and M. R. Hammerman. "Metanephric osteopontin regulates nephrogenesis in vitro." American Journal of Physiology-Renal Physiology 272, no. 4 (April 1, 1997): F469—F476. http://dx.doi.org/10.1152/ajprenal.1997.272.4.f469.

Full text

Abstract:

Renal expression of osteopontin is enhanced in the setting of acute ischemic injury. Because of the parallels that exist between recovery from renal ischemia and renal development, we characterized the role that osteopontin plays during metanephrogenesis in the rat. Osteopontin mRNA is present in kidneys obtained from rat embryos as early as embryonic day 13 (E13). Immunohistochemical staining of metanephroi obtained from E16 rat embryos and metanephroi obtained from E13 embryos and cultured for 3 days in vitro demonstrated that osteopontin is expressed both in the developing nephron and in the ureteric bud. Addition of anti-osteopontin antibodies to metanephric organ cultures results in failure of the metanephric blastema to undergo normal tubulogenesis. Addition of the arginine-glycine-aspartic acid-containing peptide, cyclo-RGDfV, or the anti-alpha(v)beta3-integrin antibody, LM609, to cultures has a similar effect. These findings establish that osteopontin is produced within the rat metanephros during development in vivo and suggest that the binding of osteopontin to the alpha(v)beta3-integrin is required for tubulogenesis to occur in vitro. Blastemal cells within metanephroi cultured in the presence of OP199 manifest increased apoptosis compared with controls. It is possible that osteopontin plays an important anti-apoptotic role during the process of metanephric blastema condensation that is a prerequisite for the formation of nephrons in vivo.

APA, Harvard, Vancouver, ISO, and other styles

30

Madsen, K. M., L. Zhang, A. R. Abu Shamat, S. Siegfried, and J. H. Cha. "Ultrastructural localization of osteopontin in the kidney: induction by lipopolysaccharide." Journal of the American Society of Nephrology 8, no. 7 (July 1997): 1043–53. http://dx.doi.org/10.1681/asn.v871043.

Full text

Abstract:

Osteopontin is a secreted phosphoprotein that is expressed in the normal kidney and induced during various pathologic conditions associated with tubulointerstitial injury. However, the exact cellular location of osteopontin in the kidney has been a matter of controversy, and little is known about the role of osteopontin in the kidney. The purpose of this study was to establish the cellular and intracellular distribution of osteopontin in the rat kidney under normal conditions and after injection of a bacterial endotoxin lipopolysaccharide (LPS). Animals received injections of LPS or vehicle at different time intervals from 4 to 20 h before sacrifice. Kidneys were preserved by in vivo perfusion with paraformaldehyde-lysine-periodate (PLP) and processed for light and electron microscope immunocytochemistry using monoclonal antibodies to rat osteopontin. By light microscopy, immunostaining was observed in the descending thin limb and the papillary surface epithelium of both control and LPS-treated animals. After injection of LPS, osteopontin immunostaining was observed throughout the distal nephron and was also present in segments of the proximal tubule, where it was distributed in a punctate pattern. Staining was already present 4 h after injection of LPS and was maximal 6 h after injection. Electron microscopy revealed that osteopontin immunoreactivity in the descending thin limb and distal tubule cells was located in the Golgi apparatus and in small cytoplasmic vesicles, whereas in the proximal tubule labeling was observed in the vacuolar-lysosomal system. Western blot analysis demonstrated a band at approximately 70 kD and confirmed the increase in osteopontin expression after administration of LPS. These results demonstrate that osteopontin is constitutively expressed in cells of the descending thin limb and papillary surface epithelium and is induced throughout the distal tubule after administration of LPS.

APA, Harvard, Vancouver, ISO, and other styles

31

Chellaiah, M., and K. Hruska. "Osteopontin stimulates gelsolin-associated phosphoinositide levels and phosphatidylinositol triphosphate-hydroxyl kinase." Molecular Biology of the Cell 7, no. 5 (May 1996): 743–53. http://dx.doi.org/10.1091/mbc.7.5.743.

Full text

Abstract:

Based on previous studies demonstrating activation of phosphatidylinositol 3-hydroxyl kinase (PI3-kinase) and stimulation of a change in cell shape, we examined the effect of osteopontin on the association of phospholipids with gelsolin, an actin-capping/severing protein. Osteopontin stimulated a rapid increase in phosphatidylinositol bisphosphate and phosphatidylinositol triphosphate levels associated with gelsolin in Triton-soluble fractions of cell lysates. The increased levels of phosphatidylinositol triphosphate associated with gelsolin were due to stimulation of PI3-kinase activity associated with gelsolin in the Triton-soluble fractions, and they were blocked by the PI3-kinase inhibitor wortmannin. Osteopontin stimulated translocation of PI3-kinase from the Triton-insoluble to Triton-soluble gelsolin. Osteopontin also decreased Triton-soluble gelsolin/actin complexes consistent with actin uncapping, and increased F-actin levels, which were also blocked by wortmannin. The osteopontin effects were mediated through binding to the alpha(v)beta 3 integrin. Taken together, our studies indicate that osteopontin/alpha(v)beta 3-mediated changes in gelsolin-associated phosphoinositide levels and PI3-kinase activity are related to stimulation of F-actin formation in osteoclasts.

APA, Harvard, Vancouver, ISO, and other styles

32

Larsson, Anders, Johanna Helmersson-Karlqvist, Lars Lind, Johan Ärnlöv, and Tobias Rudholm Feldreich. "Strong Associations between Plasma Osteopontin and Several Inflammatory Chemokines, Cytokines, and Growth Factors." Biomedicines 9, no. 8 (July 28, 2021): 908. http://dx.doi.org/10.3390/biomedicines9080908.

Full text

Abstract:

Osteopontin is a member of the proinflammatory cytokine network, a complex system that involves many chemokines, cytokines, and growth factors. The aim of the present study was to study the associations between osteopontin and a large number of chemokines, cytokines, and growth factors. We analyzed plasma and urine osteopontin in 652 men from the Uppsala Longitudinal Study of Adult Men (ULSAM) study cohort and compared the levels with the levels of eighty-five chemokines, cytokines, and growth factors. We found significant associations between plasma osteopontin and 37 plasma biomarkers in a model adjusted for age, and 28 of those plasma biomarkers were significant in a model also adjusting for cardiovascular risk factors. There were no significant associations after Bonferroni adjustment between urine osteopontin and any of the studied plasma cytokine biomarkers. This study shows that circulating osteopontin participates in a protein–protein interaction network of chemokines, cytokines, and growth factors. The network contains responses, pathways, and receptor binding interactions relating to cytokines, regulation of the immune system, and also regulation of apoptosis and intracellular signal transduction.

APA, Harvard, Vancouver, ISO, and other styles

33

Maniatis, Konstantinos, Gerasimos Siasos, Evangelos Oikonomou, Manolis Vavuranakis, Marina Zaromytidou, Konstantinos Mourouzis, Thodoros Paraskevopoulos, Georgios Charalambous, Athanasios G. Papavassiliou, and Dimitris Tousoulis. "Osteoprotegerin and Osteopontin Serum Levels are Associated with Vascular Function and Inflammation in Coronary Artery Disease Patients." Current Vascular Pharmacology 18, no. 5 (August 10, 2020): 523–30. http://dx.doi.org/10.2174/1570161117666191022095246.

Full text

Abstract:

Background: Osteoprotegerin and osteopontin have recently emerged as key factors in both vascular remodelling and atherosclerosis progression. Interleukin-6 (IL-6) is an inflammatory cytokine with a key role in atherosclerosis. The relationship of osteoprotegerin, osteopontin, and IL-6 serum levels with endothelial function and arterial stiffness was evaluated in patients with coronary artery disease (CAD). Methods: We enrolled 219 patients with stable CAD and 112 control subjects. Osteoprotegerin, osteopontin and IL-6 serum levels were measured using an ELISA assay. Endothelial function was evaluated by flow-mediated dilation (FMD) in the brachial artery and carotid-femoral pulse wave velocity (PWV) was measured as an index of aortic stiffness. Results: There was no significant difference between control subjects and CAD patients according to age and sex. Compared with control subjects, CAD patients had significantly impaired FMD (p<0.001) and increased PWV (p=0.009). CAD patients also had significantly higher levels of osteoprotegerin (p<0.001), osteopontin (p<0.001) and IL-6 (p=0.03), compared with control subjects. Moreover, IL-6 levels were correlated with osteoprotegerin (r=0.17, p=0.01) and osteopontin (r=0.30, p<0.001) levels. FMD was correlated with osteoprotegerin levels independent of possible confounders [b coefficient= - 0.79, 95% CI (-1.54, -0.05), p=0.04]. Conclusion: CAD patients have increased osteoprotegerin, osteopontin and IL-6 levels. Moreover, there is a consistent association between osteoprotegerin and osteopontin serum levels, vascular function and inflammation in CAD patients. These findings suggest another possible mechanism linking osteoprotegerin and osteopontin serum levels with CAD progression through arterial wall stiffening and inflammation.

APA, Harvard, Vancouver, ISO, and other styles

34

Lindsey, Merry L., Fouad A. Zouein, Yuan Tian, Rugmani Padmanabhan Iyer, and Lisandra E. de Castro Brás. "Osteopontin is proteolytically processed by matrix metalloproteinase 9." Canadian Journal of Physiology and Pharmacology 93, no. 10 (October 2015): 879–86. http://dx.doi.org/10.1139/cjpp-2015-0019.

Full text

Abstract:

Osteopontin is robustly upregulated following myocardial infarction (MI), which suggests that it has an important role in post-MI remodeling of the left ventricle (LV). Osteopontin deletion results in increased LV dilation and worsened cardiac function. Thus, osteopontin exerts protective effects post-MI, but the mechanisms have yet to be defined. Matrix metalloproteinases (MMPs) regulate LV remodeling post-MI, and osteopontin is a known substrate for MMP-2, -3, -7, and -9, although the cleavage sites have not been mapped. Osteopontin-derived peptides can exert distinct biological functions that may depend on their cleavage sites. We mapped the MMP-9 cleavage sites via LC-MS/MS analysis using label-free and N-terminal labeling methods, and compared them with those of MMP-2, -3, and -7. Each MMP yielded a unique cleavage profile with few overlapping cleavage sites. Using synthetic peptides, we validated 3 sites for MMP-9 cleavage at amino acid positions 151–152, 193–194, and 195–196. Four peptides were synthesized based on the upstream- and downstream-generated fragments and were tested for biological activity in isolated cardiac fibroblasts. Two peptides increased cardiac fibroblast migration rates post-wounding (p < 0.05 compared with the negative control). Our study highlights the importance of osteopontin processing, and confirms that different cleavage sites generate osteopontin peptides with distinct biological functions.

APA, Harvard, Vancouver, ISO, and other styles

35

Kuykindoll, R. J., H. Nishimura, D. B. Thomason, and S. K. Nishimoto. "Osteopontin expression in spontaneously developed neointima in fowl (Gallus gallus)." Journal of Experimental Biology 203, no. 2 (January 15, 2000): 273–82. http://dx.doi.org/10.1242/jeb.203.2.273.

Full text

Abstract:

Fowl show spontaneous elevation of blood pressure and neointimal plaque formation in the abdominal aorta at young ages. A similar neointima can be induced by a balloon-catheter-induced endothelium injury to the fowl aorta. Both spontaneously developed and injury-induced vascular lesions exhibit subendothelial hyperplasia consisting of neointimal cells with a synthetic phenotype and abundant extracellular matrix. The role of the extracellular matrix in the formation of neointima is not known. In this study, we investigated whether osteopontin, an adhesive glycoprotein present in the extracellular matrix, is expressed in aortic smooth muscle tissue of the fowl abdominal aorta, in spontaneously developed neointimal plaques and in the aortic smooth muscle underlying neointimal plaques. Crude protein extracted from isolated aortic smooth muscle tissues and neointimal plaques was fractionated by SDS-polyacrylamide gel electrophoresis and analyzed by immunoblotting with rabbit anti-fowl osteopontin (provided by Dr L. C. Gerstenfeld, Boston University) or anti-α smooth muscle actin antibodies. The anti-fowl osteopontin antibody predominantly recognized a 66–70 kDa protein band in neointimal plaques that co-migrated with the osteopontin phosphoprotein from chick bone. In contrast, intact aortic smooth muscle and the smooth muscle underlying neointimal plaques equally expressed three proteins (66–70 kDa, approximately 50 kDa and approximately 43 kDa) recognized by the anti-osteopontin antibody. Anti-α smooth muscle actin antibody recognized a 43 kDa protein band, and the expression of α smooth muscle actin was higher in aortic smooth muscle than in neointimal plaques. Osteopontin mRNA expression was examined using reverse transcription-polymerase chain reaction (RT-PCR) of total RNA from vascular tissues with specific primers constructed on the basis of the reported fowl osteopontin nucleotide sequence. The PCR products from intact aortic smooth muscle and neointimal plaques correspond to the product from recombinant plasmid cDNA (a gift from Dr L. C. Gerstenfeld) transcribed in vitro. These results suggest that osteopontin is synthesized in intact aortic smooth muscle and neointimal plaques in fowl and that unmetabolized approximately 66 kDa osteopontin protein is a predominant form in the neointima, indicating that osteopontin protein may be actively synthesized in the neointima.

APA, Harvard, Vancouver, ISO, and other styles

36

Hunter, G. K., C. L. Kyle, and H. A. Goldberg. "Modulation of crystal formation by bone phosphoproteins: structural specificity of the osteopontin-mediated inhibition of hydroxyapatite formation." Biochemical Journal 300, no. 3 (June 15, 1994): 723–28. http://dx.doi.org/10.1042/bj3000723.

Full text

Abstract:

Osteopontin is a phosphorylated sialoprotein containing a conserved sequence of contiguous aspartic acid residues. This protein is expressed at high levels in mineralized tissues and has previously been shown to inhibit the in vitro formation of hydroxyapatite (HA). In the present study, protein modification and model compound studies have been used to identify the structural features of osteopontin that are responsible for its crystal-modulating properties. Using metastable calcium phosphate solutions buffered by autotitration, osteopontin caused half-maximal inhibition of HA formation at a concentration (IC50) of 0.06 microgram/ml. The hen egg yolk phosphoprotein phosvitin was a much weaker inhibitor, while dextran sulphate had no effect. The synthetic polypeptide poly(aspartic acid) was almost as effective an inhibitor of HA formation as osteopontin (IC50 0.11 microgram/ml), whereas poly(glutamic acid) was more than a thousand times less potent (IC50 155 micrograms/ml). In a steady-state agarose gel system, much higher polypeptide concentrations were required for inhibition of HA formation, but a similar relative order of inhibitory effectiveness was observed. Treatment of osteopontin with alkaline phosphatase removed 84% of the covalently bound phosphate and reduced its HA-inhibiting activity by more than 40-fold. Treatment with glycine ethyl ester in the presence of carbodi-imide modified 86% of the carboxylate groups in osteopontin and reduced its inhibitory activity by 6-fold. These findings indicate that osteopontin is a potent inhibitor of HA formation. This activity requires phosphate and carboxylate groups, possibly including the conserved sequence of contiguous aspartic acid residues. Osteopontin may act as an inhibitor of phase separation in physiological fluids of high supersaturation.

APA, Harvard, Vancouver, ISO, and other styles

37

Rittling, Susan R., and David T. Denhardt. "Osteopontin Function in Pathology: Lessons from Osteopontin-Deficient Mice." Nephron Experimental Nephrology 7, no. 2 (April 23, 1999): 103–13. http://dx.doi.org/10.1159/000020591.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Lorenzen, Johan, Svjetlana Lovric, Robert Krämer, Hermann Haller, and Marion Haubitz. "Osteopontin in antineutrophil cytoplasmic autoantibody-associated vasculitis: relation to disease activity, organ manifestation and immunosuppressive therapy." Annals of the Rheumatic Diseases 69, no. 6 (April 27, 2010): 1169–71. http://dx.doi.org/10.1136/ard.2009.113621.

Full text

Abstract:

BackgroundOsteopontin is a pleiotropic cytokine involved in the recruitment and retention of neutrophils to sites of inflammation, which are the primary targets cells in antineutrophil cytoplasmic autoantibody-associated vasculitis (AAV). Osteopontin may play a role in the pathogenesis of AAV.Methods24 patients with systemic AAV and six patients with limited granulomatous disease were included. 19 patients were followed up at 6 and 12 months after the initiation of immunosuppressive therapy. 21 matched healthy volunteers and 20 body mass index and glomerular filtration rate-matched patients with IgA nephropathy were included as controls. Plasma levels of osteopontin were measured by ELISA. Disease activity was gauged by the Birmingham vasculitis activity score (BVAS) and C-reactive protein (CRP).ResultsOsteopontin levels are elevated compared with controls (healthy p<0.001; IgA p<0.001).Osteopontin levels decrease significantly during follow-up (p=0.02). Osteopontin levels correlate with disease activity (BVAS r=0.93; CRP r=0.73; all p<0.001) as well as erythrocyturia (r=0.7, p<0.001) and proteinuria (r=0.54, p=0.007).ConclusionsActive AAV is characterised by increased plasma levels of osteopontin, which decrease dramatically with successful therapy. Osteopontin may mediate the inflammatory process in AAV through the recruitment of neutrophils.

APA, Harvard, Vancouver, ISO, and other styles

39

Boggio, Elena, Chiara Dianzani, Casimiro Luca Gigliotti, Maria Felicia Soluri, Nausicaa Clemente, Giuseppe Cappellano, Erika Toth, et al. "Thrombin Cleavage of Osteopontin Modulates Its Activities in Human CellsIn Vitroand Mouse Experimental Autoimmune EncephalomyelitisIn Vivo." Journal of Immunology Research 2016 (2016): 1–13. http://dx.doi.org/10.1155/2016/9345495.

Full text

Abstract:

Osteopontin is a proinflammatory cytokine and plays a pathogenetic role in multiple sclerosis and its animal model, experimental autoimmune encephalomyelitis (EAE), by recruiting autoreactive T cells into the central nervous system. Osteopontin functions are modulated by thrombin cleavage generating N- and C-terminal fragment, whose individual roles are only partly known. Published data are difficult to compare since they have been obtained with heterogeneous approaches. Interestingly, thrombin cleavage of osteopontin unmasks a cryptic domain of interaction withα4β1integrin that is the main adhesion molecule involved in lymphocyte transmigration to the brain and is the target for natalizumab, the most potent drug preventing relapses. We produced recombinant osteopontin and its N- and C-terminal fragments in an eukaryotic system in order to allow their posttranslational modifications. We investigated,in vitro,their effect on human cells andin vivoin EAE. We found that the osteopontin cleavage plays a key role in the function of this cytokine and that the two fragments exert distinct effects bothin vitroandin vivo. These findings suggest that drugs targeting each fragment may be used to fine-tune the pathological effects of osteopontin in several diseases.

APA, Harvard, Vancouver, ISO, and other styles

40

Kars, T. U., M. Kulaksızoğlu, and İ. Kılınç. "Serum osteopontin can improve papillary thyroid cancer risk assessment of Bethesda III thyroid nodules: a preliminary study." Endocrine Oncology 1, no. 1 (July 1, 2021): 17–22. http://dx.doi.org/10.1530/eo-21-0005.

Full text

Abstract:

Objective Thyroid cancer can be detected in 5–10% of patients with thyroid nodules. Management may be a challenge if fine-needle aspiration biopsy yields Bethesda III findings. Most of these cases undergo surgery and are ultimately found benign. Our aim was to evaluate whether serum osteopontin can accurately estimate thyroid cancer risk in cases with cytologically Bethesda III thyroid nodules and, thereby, decrease the number of unnecessary surgical interventions. Design and Methods We obtained blood samples of cases with repeated cytologically Bethesda III thyroid nodules before surgery, and followed up the pathology results after thyroidectomy. We evaluated serum osteopontin from 36 patients with papillary thyroid cancer and compared them with 40 benign cases. Results Serum osteopontin levels in patients with papillary thyroid cancer are significantly higher than in benign cases (mean serum osteopontin: 10.48 ± 3.51 ng/mL vs6.14 ± 2.29 ng/mL, P < 0.001). The area under the receiver operating characteristics curve was 0.851, suggesting that serum osteopontin could have considerable discriminative performance. Conclusions In our preliminary study, high serum osteopontin levels can predict the risk of papillary thyroid cancer in thyroid nodules with Bethesda III cytology. Further studies are necessary to confirm these findings.

APA, Harvard, Vancouver, ISO, and other styles

41

Albu (Matasariu), Daniela Roxana, Elena Mihalceanu, Alina Pangal, Carmen Vulpoi, Mircea Onofriescu, Luciana Nitoi, Alexandra Mihaila, Gabriel Costachescu, Daniela Constantinescu, and Irina Dumitrascu. "Can Osteopontin Be Considered a Biomarker for Endometriosis?" Revista de Chimie 68, no. 9 (October 15, 2017): 2132–34. http://dx.doi.org/10.37358/rc.17.9.5840.

Full text

Abstract:

Endometriosis is a multifactorial disease that is manifested by infertility and pelvic pain. The purpose of the study was to evaluate the effect of progesterone treatment on the serum level of osteopontin, a multipotent cytokine, in patients with endometriosis. The study was prospective and we evaluated osteopontin levels that were measured in the serum of 40 patients with endometriosis and 12 healthy women using a standardized Enzyme-Linked Immunosorbent Assay (ELISA) kit. Osteopontin seric levels were lower in endometriosis patients and increased after progesterone treatment. Because of the large dispersion of data even in the control group, we find the association between osteopontin and endometriosis questionable.

APA, Harvard, Vancouver, ISO, and other styles

42

Zubareva, E. Yu, and M. A. Senchukova. "Prognostic and predictive significance of osteopontin in malignant neoplasms." Advances in Molecular Oncology 8, no. 2 (July 28, 2021): 23–28. http://dx.doi.org/10.17650/2313-805x-2021-8-2-23-28.

Full text

Abstract:

Osteopontin is an extracellular matrix protein which is produced by different types of cells and plays an important functional role in many biological processes. This review discusses the main functions of osteopontin, its role in the progression and chemoresistance of malignant neoplasms, in the regulation of epithelial-mesenchymal transition, angiogenesis, and the body’s immune response to the tumor. The article considers the currently known mechanisms by which osteopontin affects to the survival, mobility and invasion of tumor cells, to tumor sensitivity to drug treatment, as well as the prospects for a integrated study of the predictive significance of osteopontin, markers of hypoxia, angiogenesis, epithelial- mesenchymal transition, and immunological tolerance.

APA, Harvard, Vancouver, ISO, and other styles

43

CHEN, BO-LIN, GUI-YING ZHANG, SHI-PING WANG, QIAN LI, MEI-HUA XU, YUE-MING SHEN, LU YAN, et al. "The combined treatment of praziquantel with osteopontin immunoneutralization reduces liver damage in Schistosoma japonicum-infected mice." Parasitology 139, no. 4 (February 6, 2012): 522–29. http://dx.doi.org/10.1017/s0031182011002241.

Full text

Abstract:

SUMMARYThe aim of this study was to evaluate the therapeutic effects of osteopontin neutralization treatment on schistosome-induced liver injury in BALB/C mice. We randomly divided 100 BALB/C mice into groups A, B, C, D and group E. Mice in all groups except group A were abdominally infected with schistosomal cercariae to induce a schistosomal hepatopathological model. Mice in group C, D and group E were respectively administered with praziquantel, praziquantel plus colchicine and praziquantel plus neutralizing osteopontin antibody. We extracted mouse liver tissues at 3 and 9 weeks after the ‘stool-eggs-positive’ day, observed liver histopathological changes by haematoxylin-eosin and Masson trichrome staining and detected the expression of osteopontin, alpha-smooth muscle actin (α-SMA) and transforming growth factor-beta (TGF-β1) by immunohistochemistry, RT-PCR and Western blot. We found that praziquantel plus neutralizing osteopontin antibody treatment significantly decreased the granuloma dimension, the percentage of collagen and the expression of osteopontin, α-SMA and TGF-β1 compared to praziquantel plus colchicine treatment in both the acute and chronic stage of schistosomal liver damage (P<0·05). So we believe that the combined regimen of osteopontin immunoneutralization and anti-helminthic treatment can reduce the granulomatous response and liver fibrosis during the schistosomal hepatopathologic course.

APA, Harvard, Vancouver, ISO, and other styles

44

Khalil, Ashraf, Jamalat Elgedawy, Mohammed F. Faramawi, Ashraf Elfert, Ibrahim Salama, Ahmed Abbass, Hala Elsaid, and Hatem Elsebaai. "Plasma Osteopontin Level as a Diagnostic Marker of Hepatocellular Carcinoma in Patients with Radiological Evidence of Focal Hepatic Lesions." Tumori Journal 99, no. 1 (January 2013): 100–107. http://dx.doi.org/10.1177/030089161309900117.

Full text

Abstract:

Aims Hepatocellular carcinoma is one of the most aggressive malignant tumors and has limited treatment options. Needle-guided biopsies have been utilized as a tool to diagnose malignant focal hepatic lesions. These techniques are discouraged because of their complications. Nowadays, alpha fetoprotein is the most widely used tumor marker for screening and diagnosis of hepatocellular carcinoma. Nevertheless, this marker has limitations. The diagnostic role of plasma osteopontin as an adjuvant or alternative marker to alpha fetoprotein to detect hepatocellular carcinoma in Egyptian patients with focal hepatic lesions was evaluated in this study. Subject and methods Eighty participants were recruited from the Egyptian National Liver Institute and were self-assigned to three groups, namely, focal hepatic lesions (n = 40), liver cirrhosis (n = 20), and controls (n = 20). Participants' plasma osteopontin and serum alpha fetoprotein levels were determined and were compared across the three groups. Results The discriminatory ability of plasma osteopontin for hepatocellular carcinoma was lower than that of alpha fetoprotein. Osteopontin and alpha fetoprotein were not correlated with each other. Neither the gender nor the age of the patients showed a significant association with plasma osteopontin level. Conclusion Measuring plasma osteopontin level alone has no advantage over serum alpha fetoprotein in patients with focal hepatic lesions due to chronic liver disease.

APA, Harvard, Vancouver, ISO, and other styles

45

Scatena, Marta, Manuela Almeida, Michelle L. Chaisson, Nelson Fausto, Roberto F. Nicosia, and Cecilia M. Giachelli. "NF-κB Mediates αvβ3 Integrin-induced Endothelial Cell Survival." Journal of Cell Biology 141, no. 4 (May 18, 1998): 1083–93. http://dx.doi.org/10.1083/jcb.141.4.1083.

Full text

Abstract:

The αvβ3 integrin plays a fundamental role during the angiogenesis process by inhibiting endothelial cell apoptosis. However, the mechanism of inhibition is unknown. In this report, we show that integrin-mediated cell survival involves regulation of nuclear factor-kappa B (NF-κB) activity. Different extracellular matrix molecules were able to protect rat aorta- derived endothelial cells from apoptosis induced by serum withdrawal. Osteopontin and β3 integrin ligation rapidly increased NF-κB activity as measured by gel shift and reporter activity. The p65 and p50 subunits were present in the shifted complex. In contrast, collagen type I (a β1-integrin ligand) did not induce NF-κB activity. The αvβ3 integrin was most important for osteopontin-mediated NF-κB induction and survival, since adding a neutralizing anti-β3 integrin antibody blocked NF-κB activity and induced endothelial cell death when cells were plated on osteopontin. NF-κB was required for osteopontin- and vitronectin-induced survival since inhibition of NF-κB activity with nonphosphorylatable IκB completely blocked the protective effect of osteopontin and vitronectin. In contrast, NF-κB was not required for fibronectin, laminin, and collagen type I–induced survival. Activation of NF-κB by osteopontin depended on the small GTP-binding protein Ras and the tyrosine kinase Src, since NF-κB reporter activity was inhibited by Ras and Src dominant-negative mutants. In contrast, inhibition of MEK and PI3-kinase did not affect osteopontin-induced NF-κB activation. These studies identify NF-κB as an important signaling molecule in αvβ3 integrin-mediated endothelial cell survival.

APA, Harvard, Vancouver, ISO, and other styles

46

Ge, Xiaodong, Yongke Lu, Tung-Ming Leung, Esben S. Sørensen, and Natalia Nieto. "Milk osteopontin, a nutritional approach to prevent alcohol-induced liver injury." American Journal of Physiology-Gastrointestinal and Liver Physiology 304, no. 10 (May 15, 2013): G929—G939. http://dx.doi.org/10.1152/ajpgi.00014.2013.

Full text

Abstract:

Alcohol consumption is a leading cause of liver disease worldwide; thus, there is an urgent need to develop novel therapeutic interventions. Key events for the onset and progression of alcoholic liver disease result in part from the gut-to-liver interaction. Osteopontin is a cytokine present at high concentration in human milk, umbilical cord, and infants' plasma with beneficial potential. We hypothesized that dietary administration of milk osteopontin could prevent alcohol-induced liver injury perhaps by maintaining gut integrity and averting hepatic inflammation and steatosis. Wild-type mice were fed either the control or the ethanol Lieber-DeCarli diets alone or in combination with milk osteopontin for 3 wk, and parameters of gut and liver damage were measured. Milk osteopontin protected the stomach and the gut by increasing gland height, crypt cell plus enterocyte proliferation, and mucin content in addition to lowering macrophages, plasmacytes, lymphocytes, and neutrophils in the mucosa and submucosa in alcohol-fed mice. Milk osteopontin targeted the gut-liver axis, preserving the expression of tight-junction proteins in alcohol-fed mice thus maintaining intestinal integrity and permeability. There was protection from liver injury since transaminases, the activity scores, triglyceride levels, neutrophil infiltration, 3-nitrotyrosine residues, lipid peroxidation end products, translocation of gram-negative bacteria, lipopolysaccharide levels, and tumor necrosis factor-α were lower in cotreated than in ethanol-fed mice. Furthermore, milk osteopontin diminished ethanol-mediated liver injury in OPN knockout mice. Milk osteopontin could be a simple effective nutritional therapeutic strategy to prevent alcohol hepatotoxicity due, among others, to gut protective, anti-inflammatory, and anti-steatotic actions.

APA, Harvard, Vancouver, ISO, and other styles

47

Gillezeau, Christina N., Maaike van Gerwen, Julio Ramos, Bian Liu, Raja Flores, and Emanuela Taioli. "Biomarkers for malignant pleural mesothelioma: a meta-analysis." Carcinogenesis 40, no. 11 (June 5, 2019): 1320–31. http://dx.doi.org/10.1093/carcin/bgz103.

Full text

Abstract:

Abstract Malignant pleural mesothelioma (MPM) is a rare but aggressive cancer, and early detection is associated with better survival. Mesothelin, fibulin-3 and osteopontin have been suggested as screening biomarkers. The study conducted a meta-analysis of the mean differences of mesothelin, osteopontin and fibulin-3 in blood and pleural samples. PubMed searches were conducted for studies that measured levels of mesothelin, osteopontin and fibulin-3 in participants with MPM compared with malignancy, benign lung disease or healthy participants. Thirty-two studies with mesothelin levels, 12 studies with osteopontin levels and 9 studies with fibulin-3 levels were included in the meta-analysis. Statistically significant mean differences were seen between MPM patients and all other comparison groups for mesothelin blood and pleural levels. Statistically significant differences in blood osteopontin levels were seen between participants with benign lung disease and healthy participants compared with participants with MPM, but not when comparing participants with cancer with MPM participants. There were not enough studies that reported osteopontin levels in pleural fluid to complete a meta-analysis. Statistically significant differences were seen in both blood and pleural levels of fibulin-3 in MPM patients compared with all other groups. On the basis of these results, mesothelin and fibulin-3 levels appear to be significantly lower in all control groups compared with those with MPM, making them good candidates for screening biomarkers. Osteopontin may be a useful biomarker for screening healthy individuals or those with benign lung disease but would not be useful for screening patients with malignancies.

APA, Harvard, Vancouver, ISO, and other styles

48

Hillerdal, Gunnar. "Mesothelin and osteopontin." European Respiratory Journal 42, no. 2 (July 31, 2013): 557.1–557. http://dx.doi.org/10.1183/09031936.00052213.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Pantazopoulos, Ioannis, Theodoros Xanthos, Paraskevi Boura, and Konstantinos Syrigos. "Mesothelin and osteopontin." European Respiratory Journal 42, no. 2 (July 31, 2013): 557.2–558. http://dx.doi.org/10.1183/09031936.00064413.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Salloum, Fadi N., and Vinh Q. Chau. "Osteopontin in HFpEF." Journal of the American College of Cardiology 73, no. 21 (June 2019): 2719–21. http://dx.doi.org/10.1016/j.jacc.2019.03.477.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Journal articles on the topic 'Osteopontiini'

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles