Relevant bibliographies by topics / Αvβ5

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Αvβ5'

Author: Grafiati
Published: 4 June 2021
Last updated: 3 February 2022

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

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Αvβ5.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Αvβ5"

1

LUDBROOK, Steven B., Simon T. BARRY, Chris J. DELVES, and Carmel M. T. HORGAN. "The integrin alphavbeta3 is a receptor for the latency-associated peptides of transforming growth factors beta1 and beta3." Biochemical Journal 369, no. 2 (January 15, 2003): 311–18. http://dx.doi.org/10.1042/bj20020809.

Full text
Abstract:
The integrins αvβ1, αvβ5, αvβ6 and αvβ8 have all recently been shown to interact with the RGD motif of the latency-associated peptide (LAPβ1) of transforming growth factor β1 (TGFβ1), with binding to αvβ6 and αvβ8 leading to TGFβ1 activation. Previously it has been suggested that the remaining αv integrin, αvβ3, does not interact with LAPβ1. However, here we show clearly that αvβ3 does indeed interact with the LAPβ1 RGD motif. This interaction is similar to other αvβ3 ligands in terms of the cations required for adhesion, the concentrations of LAPβ1 required for binding and the ability of a small-molecule inhibitor of αvβ3, SB223245, to block the interaction. Using glutathione S-transferase fusion proteins we have mapped a minimal integrin-binding loop in LAPβ1 and then used this approach to probe the integrin-binding properties of the equivalent loops in LAPβ2 and LAPβ3. We show that the RGD motif of LAPβ3 also interacts with αvβ3, in addition to αvβ6, αvβ1 and αvβ5, whereas the corresponding loop in LAPβ2 does not interact with these integrins. These observations therefore correct a previously reported inaccuracy in the literature. Furthermore, they are important as they link αvβ3 and TGFβ, which may have implications in cancer and a number of inflammatory and fibrotic diseases where expression of both proteins has been documented.
APA, Harvard, Vancouver, ISO, and other styles
2

Seker, Aşkın, Özlem Yildirim, Özlem Kurtkaya, Aydin Sav, Murat Günel, M. Necmettin Pamir, and Türker Kılıç. "Expression of Integrins in Cerebral Arteriovenous and Cavernous Malformations." Neurosurgery 58, no. 1 (January 1, 2006): 159–68. http://dx.doi.org/10.1227/01.neu.0000192174.55131.09.

Full text
Abstract:
Abstract OBJECTIVE: To assess and compare levels and patterns of expression for integrins αvβ1, αvβ3, and αvβ5 in arteriovenous malformations (AVMs) and cavernous malformations (CCMs) of the brain. MATERIALS AND METHODS: Specimens from 10 AVM and 10 CCM lesions were selected from 112 patients with AVMs and 97 patients with CCMs who were treated microsurgically in the Department of Neurosurgery, Marmara University, Istanbul, Turkey. Sections were immunohistochemically stained with antibodies for integrins αvβ1, αvβ3, and αvβ5. Separate histological layers of the vascular wall were evaluated, and levels of expression were graded using a four-tier system. RESULTS: Integrin αvβ1 was more strongly expressed in AVMs than in CCMs. This difference was most pronounced in the endothelium and subendothelium/media. Integrin αvβ3 was more strongly expressed in CCM endothelium than in AVM endothelium (average grades, 0.9 and 0.4, respectively). All 10 of the CCM lesions expressed integrin αvβ5 in the endothelium, whereas only five of the AVMs showed minimal expression of this molecule in the endothelium. CONCLUSION: Current scientific understanding of the roles integrins play in angiogenesis is far from complete. The levels and patterns of expression for these molecules in the histological layers of the vascular walls of AVMs and CCMs provide some clues about the complex biological activities of integrins in these lesions. If one accepts the premise that immunohistochemistry has its inherent methodological problems, integrins αvβ1, αvβ3, and αvβ5 are expressed in AVMs and CCMs in different ways that may be linked to stages of angiogenic maturation. Integrin αvβ1 is expressed more strongly in endothelium and subendothelium/media of AVMs than in the corresponding layers of CCMs. Integrins αvβ3 and αvβ5 are expressed more strongly in CCM endothelium than in AVM endothelium. In addition, integrin αvβ5 staining was stronger in CCM subendothelium than AVM subendothelium/media.
APA, Harvard, Vancouver, ISO, and other styles
3

Berghoff, Anna Sophie, Orsolya Rajky, Frank Winkler, Michael Weller, Christoph Zielinski, Jens Schittenhelm, and Matthias Preusser. "Evaluation of invasion patterns and their correlation with integrin alphavbeta expression in brain metastases of solid cancers." Journal of Clinical Oncology 31, no. 15_suppl (May 20, 2013): 2059. http://dx.doi.org/10.1200/jco.2013.31.15_suppl.2059.

Full text
Abstract:
2059 Background: Understanding the pathobiology of brain metastases (BM) could guide the establishment of new targeted therapies. Methods: We collected 57 autopsy specimens of BM (primary tumor: 27 lung cancer, 6 breast cancer, 8 melanoma, 1 kidney cancer, 2 colorectal cancer, 13 other) and histologically evaluated the patterns of invasion into the surrounding brain parenchyma. Expression of the following integrins was evaluated using immunohistochemistry: with novel antibodies for αv subunit, αvβ3, αvβ5, αvβ6 and αvβ8 integrin. Results: We observed three main invasion patterns: well-demarcated (29/57, 51%), vascular co-option (10/57, 18%) and diffuse infiltration (18/57, 32%). There was no association of invasion pattern with primary tumor type, although vascular co-option was most common in melanomas (4/10, 40%). αv subunit expression was lowest in the vascular co-option group (p = 0.05, t-test). αvβ6 levels were higher in the well-demarcated group than in the vascular co-option group (p = 0.025; t-test) and were higher in lung cancer BM than in melanoma BM (0.01, t-test). αvβ3 and αvβ5 were frequently expressed in tumoral (αvβ3: 30/57, 53%; αvβ5: 55/57, 97%) and peritumoral (αvβ3: 29/57, 51%, αvβ5: 54/57 (95%) vascular structures and 27/57 (47%) specimens showed avb5 and 6/57 (11%) αvβ3 expression on tumor cells. Prior radio- or chemotherapy did not correlate with invasion pattern or integrin expression. Conclusions: We delineate three distinct invasion patterns of BM into the brain parenchyma: well-demarcated growth, vascular co-option and diffuse infiltration. Integrin expression is frequent on tumor and vascular cells in BM and associated with distinct invasion patterns. Anti-integrin therapy could be a valid treatment option in patients with BM.
APA, Harvard, Vancouver, ISO, and other styles
4

Duque, Hernando, and Barry Baxt. "Foot-and-Mouth Disease Virus Receptors: Comparison of Bovine αV Integrin Utilization by Type A and O Viruses." Journal of Virology 77, no. 4 (February 15, 2003): 2500–2511. http://dx.doi.org/10.1128/jvi.77.4.2500-2511.2003.

Full text
Abstract:
ABSTRACT Three members of the αV integrin family of cellular receptors, αVβ1, αVβ3, and αVβ6, have been identified as receptors for foot-and-mouth disease virus (FMDV) in vitro. The virus interacts with these receptors via a highly conserved arginine-glycine-aspartic acid (RGD) amino acid sequence motif located within the βG-βH (G-H) loop of VP1. Other αV integrins, as well as several other integrins, recognize and bind to RGD motifs on their natural ligands and also may be candidate receptors for FMDV. To analyze the roles of the αV integrins from a susceptible species as viral receptors, we molecularly cloned the bovine β1, β5, and β6 integrin subunits. Using these subunits, along with previously cloned bovine αV and β3 subunits, in a transient expression assay system, we compared the efficiencies of infection mediated by αVβ1, αVβ3, αVβ5, and αVβ6 among three strains of FMDV serotype A and two strains of serotype O. While all the viruses could infect cells expressing these integrins, they exhibited different efficiencies of integrin utilization. All the type A viruses used αVβ3 and αVβ6 with relatively high efficiency, while only one virus utilized αVβ1 with moderate efficiency. In contrast, both type O viruses utilized αVβ6 and αVβ1 with higher efficiency than αVβ3. Only low levels of viral replication were detected in αVβ5-expressing cells infected with either serotype. Experiments in which the ligand-binding domains among the β subunits were exchanged indicated that this region of the integrin subunit appears to contribute to the differences in integrin utilizations among strains. In contrast, the G-H loops of the different viruses do not appear to be involved in this phenomenon. Thus, the ability of the virus to utilize multiple integrins in vitro may be a reflection of the use of multiple receptors during the course of infection within the susceptible host.
APA, Harvard, Vancouver, ISO, and other styles
5

Bodero, Lizeth, Paula López Rivas, Barbara Korsak, Torsten Hechler, Andreas Pahl, Christoph Müller, Daniela Arosio, Luca Pignataro, Cesare Gennari, and Umberto Piarulli. "Synthesis and biological evaluation of RGD and isoDGR peptidomimetic-α-amanitin conjugates for tumor-targeting." Beilstein Journal of Organic Chemistry 14 (February 14, 2018): 407–15. http://dx.doi.org/10.3762/bjoc.14.29.

Full text
Abstract:
RGD-α-amanitin and isoDGR-α-amanitin conjugates were synthesized by joining integrin ligands to α-amanitin via various linkers and spacers. The conjugates were evaluated for their ability to inhibit biotinylated vitronectin binding to the purified αVβ3 receptor, retaining good binding affinity, in the same nanomolar range as the free ligands. The antiproliferative activity of the conjugates was evaluated in three cell lines possessing different levels of αVβ3 integrin expression: human glioblastoma U87 (αVβ3+), human lung carcinoma A549 (αVβ3−) and breast adenocarcinoma MDA-MB-468 (αVβ3−). In the U87, in the MDA-MB-468, and partly in the A549 cancer cell lines, the cyclo[DKP-isoDGR]-α-amanitin conjugates bearing the lysosomally cleavable Val-Ala linker were found to be slightly more potent than α-amanitin. Apparently, for all these α-amanitin conjugates there is no correlation between the cytotoxicity and the expression of αVβ3 integrin. To determine whether the increased cytotoxicity of the cyclo[DKP-isoDGR]-α-amanitin conjugates is governed by an integrin-mediated binding and internalization process, competition experiments were carried out in which the conjugates were tested with U87 (αVβ3+, αVβ5+, αVβ6−, α5β1+) and MDA-MB-468 (αVβ3−, αVβ5+, αVβ6+, α5β1−) cells in the presence of excess cilengitide, with the aim of blocking integrins on the cell surface. Using the MDA-MB-468 cell line, a fivefold increase of the IC50 was observed for the conjugates in the presence of excess cilengitide, which is known to strongly bind not only αVβ3, but also αVβ5, αVβ6, and α5β1. These data indicate that in this case the cyclo[DKP-isoDGR]-α-amanitin conjugates are possibly internalized by a process mediated by integrins different from αVβ3 (e.g., αVβ5).
APA, Harvard, Vancouver, ISO, and other styles
6

Rowedder, James E., Steve B. Ludbrook, and Robert J. Slack. "Determining the True Selectivity Profile of αv Integrin Ligands Using Radioligand Binding: Applying an Old Solution to a New Problem." SLAS DISCOVERY: Advancing the Science of Drug Discovery 22, no. 8 (April 17, 2017): 962–73. http://dx.doi.org/10.1177/2472555217703908.

Full text
Abstract:
The arginyl-glycinyl-aspartic acid (RGD) integrin subfamily contains five members that partner with the αv subunit: αvβ1, αvβ3, αvβ5, αvβ6, and αvβ8. Within the αv integrins, the epithelially restricted αvβ6 has been identified as playing a key role in the activation of transforming growth factor β that is hypothesized to be pivotal in the development of idiopathic pulmonary fibrosis (IPF). As part of a drug discovery program to identify a selective αvβ6 RGD mimetic for IPF, cell adhesion and radioligand binding assays were investigated to screen compounds to determine affinity and αv integrin selectivity. In this study, a pan-αv radioligand was characterized against all the αv integrins and used to determine accurate selectivity profiles for literature and novel RGD ligands, as well as enable an early readout on αvβ6 dissociation kinetics. It has been shown that while cell adhesion offers a high throughput and reliable format for ranking compounds, there are downsides to this format when comparing selectivity across αv integrins. By accurately defining the relationship between these assay formats, a medicinal chemistry effort has identified novel, high-affinity, and selective αvβ6 RGD mimetics with slow dissociation kinetics, with the potential to be developed into clinical candidates for IPF.
APA, Harvard, Vancouver, ISO, and other styles
7

Triantafilou, Kathy, Martha Triantafilou, Yoshikazu Takada, and Nelson Fernandez. "Human Parechovirus 1 Utilizes Integrins αvβ3 and αvβ1 as Receptors." Journal of Virology 74, no. 13 (July 1, 2000): 5856–62. http://dx.doi.org/10.1128/jvi.74.13.5856-5862.2000.

Full text
Abstract:
ABSTRACT Human parechovirus 1 (HPEV1) displays an arginine-glycine-aspartic acid (RGD) motif in the VP1 capsid protein, suggesting integrins as candidate receptors for HPEV1. A panel of monoclonal antibodies (MAbs) specific for integrins αvβ3, αvβ1, and αvβ5, which have the ability to recognize the RGD motif, and also a MAb specific for integrin α2β1, an integrin that does not recognize the RGD motif, were tested on A549 cells. Our results showed that integrin αv-specific MAb reduced infectivity by 85%. To specify which αv integrins the virus utilizes, we tested MAbs specific to integrins αvβ3 and αvβ1 which reduced infectivity significantly, while a MAb specific for integrin αvβ5, as well as the MAb specific for α2β1, showed no reduction. When a combination of MAbs specific for integrins αvβ3 and αvβ1 were used, virus infectivity was almost completely inhibited; this shows that integrins αvβ3 and αvβ1 are utilized by the virus. We therefore proceeded to test whether αv integrins' natural ligands fibronectin and vitronectin had an effect on HPEV1 infectivity. We found that vitronectin reduced significantly HPEV1 infectivity, whereas a combination of vitronectin and fibronectin abolished infection. To verify the use of integrins αvβ3 and αvβ1 as HPEV1 receptors, CHO cells transfected and expressing either integrin αvβ3 or integrin αvβ1 were used. It was shown that the virus could successfully infect these cells. However, in immunoprecipitation experiments using HPEV1 virions and allowing the virus to bind to solubilized A549 cell extract, we isolated and confirmed by Western blotting the αvβ3 heterodimer. In conclusion, we found that HPEV1 utilises both integrin αvβ3 and αvβ1 as receptors; however, in cells that express both integrins, HPEV1 may preferentially bind integrin αvβ3.
APA, Harvard, Vancouver, ISO, and other styles
8

Finnemann, Silvia C., and Enrique Rodriguez-Boulan. "Macrophage and Retinal Pigment Epithelium Phagocytosis." Journal of Experimental Medicine 190, no. 6 (September 20, 1999): 861–74. http://dx.doi.org/10.1084/jem.190.6.861.

Full text
Abstract:
Noninflammatory monocyte macrophages use αvβ3 integrin to selectively bind apoptotic cells, initiating their phagocytic removal. In a related process, the retinal pigment epithelium (RPE) employs αvβ5 integrin to recognize spent photoreceptor outer segment particles (OS). Here, we show that apoptotic cells and OS compete for binding to these receptors, indicating that OS and apoptotic cells expose surface signals recognizable by αvβ3 and αvβ5. Particle binding to αvβ5 required protein kinase C (PKC) activation. In RPE, αvβ5 binding was maximally activated even before any phagocytic challenge and was reduced by PKC inhibitors. In macrophages, it was dormant but became activated upon PKC stimulation. PKC-activated αvβ5-mediated binding in macrophages differed from constitutive binding to the same integrin receptor in RPE cells in that the former followed much faster kinetics, similar to particle binding mediated by αvβ3. Activation of αvβ5 for particle binding correlated with its recruitment into a detergent-insoluble fraction, a process sensitive to pharmacological modulation of PKC in both types of phagocytes. Furthermore, αvβ5 but not αvβ3 particle binding required actin microfilaments. These data constitute the first evidence that noninflammatory phagocytes actively regulate the earliest phase of phagocytic clearance, particle binding, by controlling receptor activity.
APA, Harvard, Vancouver, ISO, and other styles
9

Bello, Lorenzo, Jianping Zhang, Demetrios C. Nikas, Jon F. Strasser, Roberto M. Villani, David A. Cheresh, Rona S. Carroll, and Peter McL Black. "αvβ3 and αvβ5 Integrin Expression in Meningiomas." Neurosurgery 47, no. 5 (November 1, 2000): 1185–95. http://dx.doi.org/10.1097/00006123-200011000-00035.

Full text
Abstract:
Abstract OBJECTIVE Integrins are emerging as alternative receptors capable of mediating several biological functions, such as cell-matrix and cell-cell adhesion, cell migration, signal transduction, and angiogenesis. Two αv integrins, i.e., αvβ3 and αvβ5, play critical roles in mediating these activities, particularly in tumors. No data are available on the expression of these integrins in meningiomas. METHODS Using Western blot and immunohistochemical analyses with LM609 and PG32, two monoclonal antibodies capable of recognizing the functional integrin heterodimer, we evaluated the expression of αvβ3 and αvβ5 integrins in a series of 34 meningiomas of different histological subtypes and grades. We studied their expression in tumor cells and vasculature, as well as the expression of their related angiogenic factors (fibroblast growth factor 2 and vascular endothelial growth factor) and the αvβ3 ligand vitronectin. RESULTS αvβ3 and αvβ5 integrins were expressed by neoplastic vasculature and cells. αvβ3 and αvβ5 expression was associated and correlated with that of their respective growth factors (fibroblast growth factor 2 and vascular endothelial growth factor) and microvessel counts and densities. αvβ3 was more strongly expressed than αvβ5 in two cases of histologically benign meningiomas with aggressive clinical behavior. αvβ3 expression was associated with that of its related ligand vitronectin and was also evident in small vessels of brain tissue closely surrounding meningiomas. CONCLUSION Our data demonstrate the expression of αvβ3 and αvβ5 integrins in meningioma cells and vasculature. Our findings suggest a role for both of these integrins, and particularly αvβ3, in meningioma angiogenesis.
APA, Harvard, Vancouver, ISO, and other styles
10

Janes, Sam M., and Fiona M. Watt. "Switch from αvβ5 to αvβ6 integrin expression protects squamous cell carcinomas from anoikis." Journal of Cell Biology 166, no. 3 (August 2, 2004): 419–31. http://dx.doi.org/10.1083/jcb.200312074.

Full text
Abstract:
Stratified squamous epithelia express the αvβ5 integrin, but in squamous cell carcinomas (SCCs) there is down-regulation of αvβ5 and up-regulation of αvβ6. To investigate the significance of this finding, we transduced an αv-negative human SCC line with retroviral vectors encoding αv integrins. αvβ5-expressing cells underwent suspension-induced apoptosis (anoikis), whereas αv-negative cells and cells expressing αvβ6 did not. Resistance to anoikis correlated with PKB/Akt activation in suspension, but not with changes in PTEN or p110α PI3 kinase levels. Anoikis was induced in parental and αvβ6-expressing cells by inhibiting PI3 kinase. Conversely, activation of Akt or inhibition of caspases in αvβ5-expressing cells suppressed anoikis. Caspase inhibition resulted in increased phosphoAkt, placing caspase activation upstream of decreased Akt activation. Anoikis required the cytoplasmic domain of β5 and was independent of the death receptor pathway. These results suggest that down-regulation of αvβ5 through up-regulation of αvβ6 may protect SCCs from anoikis by activating an Akt survival signal.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Αvβ5"

1

Paulhe, Frédérique. "Régulation différentielle du métabolisme des phosphoinositides par les intégrines αvβ3 et αvβ5 lors de la migration des cellules musculaires lisses." Paris 7, 2002. http://www.theses.fr/2002PA077140.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Acharya, Mridu. "Expression and function of the αVβ5 integrin during human B lymphopoiesis." Thesis, University of Glasgow, 2008. http://theses.gla.ac.uk/172/.

Full text
Abstract:
The integrin αVβ5 is a receptor for sCD23 molecule and the αVβ5-CD23 interaction sustains proliferation of the pre-B cell line SMS-SB. This thesis describes further investigation into the role of αVβ5 integrin during human B cell development. B cell development in the bone marrow involves stepwise maturation of progenitor cells through different defined stages. A tight regulation of proliferation and differentiation mediates the progression of progenitor cells through this developmental pathway. A variety of signals from soluble molecules and adhesive interactions regulate this balance of proliferation and differentiation. The main aim of this work was to assess the importance of the integrin αVβ5 during B cell development by defining its expression and function during specific stages of B cell development in the bone marrow. The αVβ5 integrin was expressed by B cell precursors in the bone marrow, by different pre-B cell lines and the αVβ5-CD23 interaction sustained proliferation of some pre-B cell lines. The pre-B cell lines SMS-SB, RS4;11 and 697 showed a significant proliferative response to αVβ5 stimulation by sCD23, a sCD23-derived long peptide and anti-αVβ5 MAb 15F11. Transitional and more mature B cell lines down-regulated αVβ5 expression and did not show a proliferative response. Both αVβ5 and αVβ3 integrin could be detected on normal bone marrow B cell precursor populations, though αVβ5 was the more highly expressed integrin. In preliminary functional experiments, stimulation of CD19+/κ- cells with sCD23 induced cell proliferation whereas equivalent treatment of CD19+/κ+ cells did not. The data are consistent with the interpretation that αVβ5 integrin is expressed in B cell precursors but that its ability to sustain growth of these cells wanes as the cells mature towards a membrane immunoglobulin-positive state. The αVβ5-mediated proliferation was enhanced by the chemokine SDF-1 and PDGF but not by the cytokines IL-3, IL-4, IL-7 or IL-11. This effect was apparently restricted to earlier B cell precursors and was independent of levels of expression of both αVβ5 and CXCR4. Stimulation of SMS-SB cells by αVβ5 ligands provoked ERK phosphorylation and co-stimulation with SDF-1 promoted a more rapid and sustained ERK activation. PDGF induced a similar effect on αVβ5-mediated activation of ERKphosphorylation. These data suggest that ligation of αVβ5 by soluble, adhesion-independent stimuli activates ERK phosphorylation and this pathway can be modulated by inputs from G-protein-coupled and tyrosine kinase receptors. The murine pro-B cell line BAF03 also displayed αVβ5-mediated proliferation in response to human CD23. Preliminary experiments showed that human CD23 sustained growth of murine bone marrow B cell precursors. Therefore, these data suggest that murine B cells can also use αVβ5 integrin to sustain their growth and the studies described here in human cell lines could be translated into in vivo murine models. Further work is needed to confirm the proliferative response due to the αVβ5-CD23 interaction in normal B cell precursors in the bone marrow and to define the exact stage of development where this interaction is critical. In addition to its expression in the bone marrow B cell precursors, previous work has also demonstrated the expression of αVβ5 integrin in B cells from patients with ALL. Therefore, the αVβ5-CD23 interaction could have important implications not only in proliferation of normal B cell precursors but also in proliferation of neoplastic B cells. These data identify the αVβ5-CD23 interaction as a potentially important interaction during early B cell development, as αVβ5 expression and function is stage-specific, regulated by other molecules and can be demonstrated in both human and murine cell lines.
APA, Harvard, Vancouver, ISO, and other styles
3

Seelke, Sandra [Verfasser], Nina [Akademischer Betreuer] Kollmar, Sigrid [Akademischer Betreuer] Hoyer-Fender, and Wilfried [Akademischer Betreuer] Kramer. "Untersuchung bispezifischer Intradiabodies gegen die Integrine αvβ3, αvβ5 und α5β1 auf ihre anti-angiogenen Eigenschaften / Sandra Seelke. Gutachter: Sigrid Hoyer-Fender ; Wilfried Kramer. Betreuer: Nina Kollmar." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2013. http://d-nb.info/1044173068/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Ahmedah, Hanadi Talal A. "Correlation between the expression of integrins and their role in cancer progression : expression pattern of integrins αvβ3, αvβ5 and α5β1 in clinical and experimental tumour samples." Thesis, University of Bradford, 2015. http://hdl.handle.net/10454/14284.

Full text
Abstract:
The integrins play a crucial role in cancer cell proliferation, migration, differentiation, survival and angiogenesis. It has been shown that integrin expression is positively correlated to cancer dissemination, this suggests targeting selected integrins as an anti-metastatic strategy. The aim of this study is to investigate the effect of novel antagonists of α5β1, αvβ3 and αvβ5 integrins on cancer cell migration, a key process in tumour cell dissemination. Immunohistochemistry was used to evaluate the expression of α5, αv, β3 and β5 integrin subunits in prostate cancer tissues. Furthermore the expression of these integrin subunits in tumour and normal human head and neck tissues was compared. The expression profile of these integrin subunits in established human cancer cell lines was subsequently evaluated using immunodetection methods in cells and xenograft tumour samples. The effect of integrin inhibition on cell migration was then assessed using neutralizing antibodies against αvβ3, αvβ5, and α5β1 integrins in the scratch-wound healing assay. This assay was then used to evaluate the potential of novel small molecule integrin antagonists in preventing tumour cell migration. In H & N tissues, αvβ3, αvβ5 and α5β1 integrins are extensively expressed in tumour tissues but weakly expressed in normal tissue from the same patient. Further, prostate cancer tissues expressed variable levels of αvβ3, αvβ5 and α5β1 integrins. αvβ3 and αvβ5 integrins were expressed in variable levels in OSC-19, PC-3, DU145, DLD-1, HT-29, HUVEC, MCF-7, MCF-7ADR and M14 human tumour cell lines and in OSC-19, PC-3, HT-29 and MCF-7 xenografts. α5β1 integrin was expressed in all cell lines and xenografts except in MCF-7 cell line and HT-29 cell line and xenograft. Overall, the expression was elevated in xenografts compared to the corresponding cultured cells. Based on the expression profile and ability of cells to migrate, three cell lines (DLD-1 colon, DU145 prostate and OSC-19 HNSCC) were selected as models to further evaluate the potential of novel small molecule integrin antagonists to inhibit cell migration. The cell lines were characterized by using neutralizing antibodies against αvβ3, αvβ5, and α5β1 integrins to determine which of these three integrins were primarily involved in tumour cell migration. In DLD-1 and DU145, blocking αvβ5 and αvβ3 significantly inhibited migration, whilst the migration of OSC-19 was 50% inhibited by a multi-integrin inhibitor combination. Among the antagonists, ICT9055 and ICT9072 significantly decreased DLD-1 cell migration by 70% and 60% respectively while ICT9023, ICT9024, and ICT9026 significantly decreased DU145 cell migration by 60%, 60% and 50% respectively. The findings suggest that single integrin inhibition is not sufficient to prevent cell migration whereas dual or multiple inhibition is more effective. Two novel anti-migratory agents were identified in colon cancer and three in prostate cancer which would warrant further investigation.
APA, Harvard, Vancouver, ISO, and other styles
5

Ahmedah, Hanadi T. A. "Correlation between the expression of integrins and their role in cancer progression. Expression pattern of integrins αvβ3, αvβ5 and α5β1 in clinical and experimental tumour samples." Thesis, University of Bradford, 2015. http://hdl.handle.net/10454/14284.

Full text
Abstract:
The integrins play a crucial role in cancer cell proliferation, migration, differentiation, survival and angiogenesis. It has been shown that integrin expression is positively correlated to cancer dissemination, this suggests targeting selected integrins as an anti-metastatic strategy. The aim of this study is to investigate the effect of novel antagonists of α5β1, αvβ3 and αvβ5 integrins on cancer cell migration, a key process in tumour cell dissemination. Immunohistochemistry was used to evaluate the expression of α5, αv, β3 and β5 integrin subunits in prostate cancer tissues. Furthermore the expression of these integrin subunits in tumour and normal human head and neck tissues was compared. The expression profile of these integrin subunits in established human cancer cell lines was subsequently evaluated using immunodetection methods in cells and xenograft tumour samples. The effect of integrin inhibition on cell migration was then assessed using neutralizing antibodies against αvβ3, αvβ5, and α5β1 integrins in the scratch-wound healing assay. This assay was then used to evaluate the potential of novel small molecule integrin antagonists in preventing tumour cell migration. In H & N tissues, αvβ3, αvβ5 and α5β1 integrins are extensively expressed in tumour tissues but weakly expressed in normal tissue from the same patient. Further, prostate cancer tissues expressed variable levels of αvβ3, αvβ5 and α5β1 integrins. αvβ3 and αvβ5 integrins were expressed in variable levels in OSC-19, PC-3, DU145, DLD-1, HT-29, HUVEC, MCF-7, MCF-7ADR and M14 human tumour cell lines and in OSC-19, PC-3, HT-29 and MCF-7 xenografts. α5β1 integrin was expressed in all cell lines and xenografts except in MCF-7 cell line and HT-29 cell line and xenograft. Overall, the expression was elevated in xenografts compared to the corresponding cultured cells. Based on the expression profile and ability of cells to migrate, three cell lines (DLD-1 colon, DU145 prostate and OSC-19 HNSCC) were selected as models to further evaluate the potential of novel small molecule integrin antagonists to inhibit cell migration. The cell lines were characterized by using neutralizing antibodies against αvβ3, αvβ5, and α5β1 integrins to determine which of these three integrins were primarily involved in tumour cell migration. In DLD-1 and DU145, blocking αvβ5 and αvβ3 significantly inhibited migration, whilst the migration of OSC-19 was 50% inhibited by a multi-integrin inhibitor combination. Among the antagonists, ICT9055 and ICT9072 significantly decreased DLD-1 cell migration by 70% and 60% respectively while ICT9023, ICT9024, and ICT9026 significantly decreased DU145 cell migration by 60%, 60% and 50% respectively. The findings suggest that single integrin inhibition is not sufficient to prevent cell migration whereas dual or multiple inhibition is more effective. Two novel anti-migratory agents were identified in colon cancer and three in prostate cancer which would warrant further investigation.
Princess Nora Bint Abdul Rahman University
APA, Harvard, Vancouver, ISO, and other styles
6

Berthet, Virginie. "Rôle du clivage de l'intégrine αvβ5 dans le potentiel adhésif et migratoire des cellules d'adénocarcinome colique." Aix-Marseille 1, 2002. http://www.theses.fr/2002AIX11020.

Full text
Abstract:
Les intégrines participent aux interactions cellule-matrice extracellulaire. Elles sont formées d'une sous-unité alpha et d'une sous-unité beta. Certaines sous-unités alpha sont clivées par des convertases, ce qui libère deux chaînes restant liées entre elles par un pont disulfure. Afin de mettre en évidence le rôle de ce clivage dans la fonction des intégrines, nous avons un modèle (cellules PDX39P) dans lequel les convertases sont inhibées et les intégrines ne sont pas clivées. Nous avons constaté que les cellules PDX39P adhèrent moins sur vitronectine (VN) que les cellules témoins et cette baisse de l'adhésion n'est pas due à des changements d'affinité de alphav beta5 pour la VN. L'adhésion est un phénomène complexe qui fait intervenir des voies de signalisation, comme la phosphorylation de la FAK, qui stabilisent l'adhésion. La phosphorylation de la FAK, normalement induite par l'adhésion, est diminuée dans les cellules PDX39P. L'absence de clivage de l'intégrine alphav conduit t à des perturbations des voies de signalisation qui stabilisent l'adhésion. D'autre part, la MAPK, protéine qui participe à la migration, est sur-activée dans les cellules PDX39P. Nous avons donc étudié le rôle dans la migration. Les cellules PDX39P migrent plus sur VN que les cellules témoins. La migration est impliquée dans l'invasion et la formation des métastases. Nous avons donc estimé le pouvoir métastatique des cellules par injection sous-cutanée de cellules à des ratons immunodéprimés. Les tumeurs induites par les cellules PDX39P sont plus agressives et font plus de métastases que celles induites par les cellules témoins. Les cellules PDX39P sont plus invasives que les cellules témoins. En conclusion, l'absence de clivage de la sous-unité alphav joue un rôle important dans les différentes fonctions dans lesquels interviennent les intégrines, alphav, notamment dans les fonctions participant à la formation des métastases comme la signalisation, l'adhésion et la migration.
APA, Harvard, Vancouver, ISO, and other styles
7

Marsh, D. J. "The αvβ6 integrin in cancer." Thesis, University College London (University of London), 2011. http://discovery.ucl.ac.uk/1331896/.

Full text
Abstract:
The epithelial restricted αvβ6 integrin is known to have minimal expression in healthy tissue and to be upregulated in cancer and healing wounds. This thesis explores the role of αvβ6 in cancer and tests the hypothesis that αvβ6 has a prognostic and therapeutic utility in cancer. Using immunohistochemistry, increased αvβ6 expression was found in nonmelanoma skin cancers (NMSC), particularly in morphoeic type basal cell carcinoma. In cell culture experiments, αvβ6 was found to activate TGF-β and promote myofibroblast differentiation, producing a tumour stroma rich in smooth muscle actin (SMA). These findings prompted a study of αvβ6 and SMA as prognostic indicators in oral squamous cell carcinoma (OSCC). A study of 282 cases of OSCC found that although αvβ6 was not a prognostic marker, patients with high SMA levels had a highly significant increased risk of disease specific mortality (HR 3.06 [CI 1.65-5.66], p<0.001). Next, the utility of αvβ6 as a target was explored through the development of a single chain antibody fragment (scFv) specific for αvβ6. The scFv was tested for the delivery of targeted magnetic fluid hyperthermia (MFH), an experimental cancer treatment based on the generation of heat by magnetic nanoparticles when placed within an alternating magnetic field. The αvβ6-specific scFv (B6.3) was manufactured and high ligand specificity confirmed on ELISA and FACS analysis. B6.3 was successfully conjugated to two alternative iron nanoparticles. In-vitro studies demonstrated increased cellular uptake of scFv-nanoparticle complexes and greater cellular toxicity on exposure to MFH compared to nanoparticles alone. In conclusion, αvβ6 is a potential target for therapy in NMSC and OSCC. SMA is found to be an independent prognostic marker in OSCC and αvβ6 identified as a proinvasive factor in morphoeic BCC. Finally, the production αvβ6 specific scFvs and use for in-vitro MFH potentiates the development of αvβ6 targeted MFH cancer therapy.
APA, Harvard, Vancouver, ISO, and other styles
8

Mathias, Lucas Solla. "Ativação da via MAPK/ERK e Integrina αvβ3 pela ação da triiodotironina (T3) na modulação da expressão gênica de adipocinas e modificação do perfil lipídico em adipócitos, 3T3-L1." Botucatu, 2019. http://hdl.handle.net/11449/181721.

Full text
Abstract:
Orientador: Miriane de Oliveira
Resumo: Introdução: O hormônio triiodotironina (T3) influencia o metabolismo e desenvolvimento do tecido adiposo (TA), modulando a proliferação e diferenciação de adipócitos, podendo agir sobre os reguladores do processo de adipogênese, como o receptor ativado por proliferador de peroxissomo (PPARy). O TA está envolvido na regulação da energia corporal, sintetizando e secretando substâncias denominadas adipocinas, dentre elas a adiponectina e leptina. A adiponectina está relacionada ao aumento da sensibilidade à insulina, enquanto a leptina está envolvida com o gasto energético. O T3 pode desencadear ações por ativação de vias extranucleares, dentre elas a via MAPK/ERK e integrina αVβ3. Objetivo: Verificar a ação do T3, com participação das vias extranucleares MAPK/ERK e integrina αVβ3, na modulação de adiponectina e leptina, além de avaliar os parâmetros relacionados ao perfil adipogênico e dano de DNA. Métodos: Adipócitos, 3T3-L1, foram tratados com T3 (10nM) por uma hora, na ausência ou presença dos inibidores de MAPK/ERK – PD98059 (PD, 50uM) e da integrina αvβ3 – ácido tetraiodotiroácetico (Tetrac, 10-4M). A ausência de qualquer tratamento foi considerada grupo controle (C). Após o período de tratamento foi realizado PCRq-RT para analisar a expressão de mRNA de adiponectina e leptina, e Western Blot para expressão proteica de adiponectina, leptina, PPARy, pAKT e pERK; a viabilidade celular foi realizada pelo ensaio de MTT; a quantificação do acúmulo lipídico pelos ens... (Resumo completo, clicar acesso eletrônico abaixo)
Abstract: Introduction: The hormone triiodothyronine (T3) influences the metabolism and development of adipose tissue (TA), modulating the proliferation and differentiation of adipocytes, and can act on regulators of the adipogenic differentiation process, such as the peroxisome proliferator activated receptor). TA is involved in the regulation of body energy, synthesizing and secreting substances called adipokines, among them adiponectin and leptin. Adiponectin is related to increased insulin synaptic, since leptin is involved in energy expenditure. T3 can trigger actions by activation of extranuclear pathways, including MAPK / ERK and integrin α Vβ3. Objective: Given the role of T3 in TA and the importance of adipokines, the objective of this study is to verify the action of T3 with the participation of extranuclear pathways in the modulation of adiponectin and leptin and the parameters related to the adipogenic profile. Methods: Adipocytes, 3T3-L1, were treated with a physiological dose of T3 (10nM) for one hour, in the absence or presence of MAPK / ERK-PD98059 (PD) and integrin αvβ3 - tetraiodothyrocetic (Tetrac) integrin inhibitors. The absence of any treatment was considered as a control group (C). After the treatment period PCRqRT was performed to analyze the expression of leptin and adiponectin mRNA, and Western Blot for protein expression of adiponectin, leptin, PPARγ, pAKT and pERK; cell viability was performed by the MTT assay; the quantification of lipid accumulation by the... (Complete abstract click electronic access below)
Mestre
APA, Harvard, Vancouver, ISO, and other styles
9

Vallath, Sabarinath S. "Studying the role of integrin αVβ6 in pancreatic cancer." Thesis, Queen Mary, University of London, 2013. http://qmro.qmul.ac.uk/xmlui/handle/123456789/8663.

Full text
Abstract:
Pancreatic cancer is often referred to as the “silent killer“ due to the asymptomatic nature of the disease in the early stages and the extremely poor prognosis overall. The average one-year survival rate for PDAC patients is 24% (American Cancer Society, facts and figures, 2010), decreasing to 5%-6% over 5 years (WHO report, Pancreatic cancer, 2010). Only 20% of patients are suitable for surgical resection at the time of diagnosis and treatment options available to PDAC patients have not improved significantly over the past few decades. Thus novel therapeutic approaches are essential to treat this disease. Our experimental, clinical and pre-clinical data suggest integrin αvβ6 may be a suitable target. Bioinformatics studies using the Pancreatic Expression Database revealed that the β6 gene (ITGB6) was highly up regulated in pancreatic ductal carcinoma (PDAC) compared with normal pancreas. Further analysis carried out showed that there was a significant correlation between ITGB6 expression at the mRNA level and survival in a cohort of 292 PDAC patients. Immunohistochemistry analysis on two separate patient cohorts (n=118 and n=147) showed that normal pancreas lacked αvβ6 expression whereas 91% of PDAC tissues expressed αvβ6 at the protein level. There was no significant correlation between αvβ6 expression and survival at the protein level in both cohorts of patients tested. Flow cytometry and Western blotting analyses on a panel of PDAC cell lines confirmed expression of αvβ6 in PDAC cell lines. This study investigated the functional role of αvβ6 in PDAC cell lines. Antibody mediated function blockade of αvβ6 significantly inhibited proliferation in a dose dependent manner, specifically in αvβ6 positive PDAC cell lines. A significant reduction in migration and invasion was also observed in a panel of αvβ6 positive PDAC cell lines when treated with an αvβ6 function-blocking antibody. αvβ6 targeted antibody mediated therapy in combination with gemcitabine significantly inhibited tumour growth in a physiologically relevant pre-clinical subcutaneous xenograft model of PDAC. These data reaffirms that αvβ6 is a potential novel therapeutic target and an αvβ6 specific function-blocking antibody can be used as a novel agent to treat pancreatic adenocarcinoma patients.
APA, Harvard, Vancouver, ISO, and other styles
10

Antonow, Michelli Barcelos. "Desenvolvimento e caracterização físico-química de nanocápsulas multiparedes complexadas com zinco e funcionalizadas com RGD para reconhecimento por integrinas ανβ3 presentes em células tumorais." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2016. http://hdl.handle.net/10183/149502.

Full text
Abstract:
A funcionalização de superfície nas nanocápsulas contendo doxorrubicina com o peptídeo RGD é uma estratégia promissora devido a ligação preferencial na integrina αvβ3 expressa em células tumorais. Este estudo objetivou o desenvolvimento, caracterização e estudos biológicos de nanocápsulas multiparedes com doxorrubicina e funcionalizadas com RGD. Para isso, na primeira etapa do trabalho foi realizada a síntese do peptídeo RGD. Os produtos obtidos foram caracterizados por análises de infravermelho e RMN de 1H. Na segunda etapa foram desenvolvidas formulações de nanocápsulas com doxorrubicina ou cloridrato de doxorrubicina, e, nanocápsulas multiparedes revestidas com quitosana, íons zinco, RGD ou fenilalanina. Essas suspensões foram caracterizadas através da determinação do pH, diâmetro de partícula por diferentes técnicas, potencial zeta, eficiência de encapsulação e eficiência de associação do RGD na superfície da nanopartícula. Na terceira etapa, foram realizados ensaios de viabilidade celular por MTT após 24 e 72h com as formulações desenvolvidas em células de câncer de mama (MCF7) e glioblastoma humano (U87MG). As formulações apresentaram diferentes valores de citotoxicidade e, utilizando o Gráfico de Pareto foi possível determinar os fatores que exercem maior influencia. Em células MCF7 foi a concentração de fármaco e tempo de tratamento e, nas células U87MG além desses fatores, a funcionalização mostrou-se determinante. Além disso, foi avaliada a captação das nanocápsulas funcionalizadas com RGD e fenilalanina após 24h nas células tumorais e células de queratinócitos humanos (HaCat), com diferentes níveis de expressão da integrina αvβ3. O estudo mostrou menores valores de captação nas células HaCat (sem expressão de integrina αvβ3) para as duas formulações testadas. Finalmente as nanocápsulas funcionalizadas com RGD apresentaram maior captação em células U87MG com maior expressão da integrina αvβ3.
The surface functionalization in nanocapsules containing doxorubicin with RGD peptide is a promising strategy due to preferential binding in the αvβ3 integrin expressed on tumor cells. This study aimed the development, characterization, and biological studies of multiwall nanocapsules containing doxorubicin and functionalized with RGD. For this reason, in the first stage of this study the synthesis of RGD peptide was performed and the products characterized by infrared analysis and 1H NMR. Besides, nanocapsules formulations were developed containing doxorubicin or doxorubicin hydrochloride, and multiwall nanocapsules coated with chitosan, zinc ions, RGD or phenylalanine. These suspensions were characterized by pH determination, particle diameter by different techniques, zeta potential, encapsulation efficiency, and association efficiency of RGD on the surface of the nanoparticle. Additionally, it was performed cell viability assays by MTT after 24 and 72 hours with formulations developed in breast cancer (MCF7) and human glioblastoma cells (U87MG). Formulations showed different cytotoxicity values. The Pareto chart was possible to determine factors that have more influence. In MCF7 cells was drug concentration and treatment time, and U87MG cells, besides these factors, the functionalization was decisive. Furthermore, it was performed the cellular uptake of nanocapsules functionalized with RGD or phenylalanine after 24 hours in tumor cells and human keratinocyte cells (HaCaT), with different levels of expression αvβ3 integrin. The study showed less uptake in HaCaT cells (without expression αvβ3 integrin) for the two formulations applied, and the nanocapsules functionalized with RGD showed more uptake in U87MG cells, with higher expression of integrin αvβ3.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Αvβ5"

1

Kumar, C. Chandra, L. Armstrong, Z. Yin, M. Malkowski, E. Maxwell, He Ling, B. Yaremko, et al. "Targeting Integrins αvβ3 and αvβ5 for Bloking Tumor-Induced Angiogenesis." In Advances in Experimental Medicine and Biology, 169–80. Boston, MA: Springer US, 2000. http://dx.doi.org/10.1007/978-1-4615-4221-6_14.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Finnemann, Silvia C. "Role of αvβ5 Integrin in Regulating Phagocytosis by the Retinal Pigment Epithelium." In Advances in Experimental Medicine and Biology, 337–42. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4615-0067-4_42.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

He, Huacheng, Remant Bahadur K.C., and Peisheng Xu. "Fabrication of cRGD-Conjugated Dual-Responsive Micelles to Target αvβ5 Integrin-Overexpressed Cancer." In Methods in Pharmacology and Toxicology, 19–34. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/7653_2015_42.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Nandrot, Emeline F., Yongen Chang, and Silvia C. Finnemann. "αvβ5 Integrin Receptors at the Apical Surface of the RPE: One Receptor, Two Functions." In Advances in Experimental Medicine and Biology, 369–75. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-74904-4_43.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Mallavarapu, Mallika, and Silvia C. Finnemann. "Neural Retina and MerTK-Independent Apical Polarity of αvβ5 Integrin Receptors in the Retinal Pigment Epithelium." In Retinal Degenerative Diseases, 123–31. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-1-4419-1399-9_15.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Ruggiero, Linda, Zsolt Sarang, Zsuzsa Szondy, and Silvia C. Finnemann. "αvβ5 Integrin-Dependent Diurnal Phagocytosis of Shed Photoreceptor Outer Segments by RPE Cells Is Independent of the Integrin Coreceptor Transglutaminase-2." In Retinal Degenerative Diseases, 731–37. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4614-0631-0_93.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Beer, Ambros J., and Markus Schwaiger. "PET Imaging of αvβ3 Expression in Cancer Patients." In Methods in Molecular Biology, 183–200. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-901-7_13.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Zischinsky, Gunther, Ulrich Groth, Beate Diefenbach, and Alfred Jonczyk. "Linear and Cyclic Peptides for Integrin αvβ6 Inhibition." In Peptides: The Wave of the Future, 733–34. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_342.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Liu, Shuang, Simon P. Robinson, and D. Scott Edwards. "Radiolabeled Integrin αvβ3 Antagonists as Radiopharmaceuticals for Tumor Radiotherapy." In Contrast Agents III, 193–216. Berlin, Heidelberg: Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/b101229.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Strömblad, Staffan, Peter C. Brooks, Jürgen Becker, Mauricio Rosenfeld, and David A. Cheresh. "The Role of Integrin αvβ3 in Cell Survival and Angiogenesis." In Programmed Cell Death, 35–42. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4899-0072-2_4.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Αvβ5"

1

Sipos, Bence, Tobias Henopp, Holger Kalthoff, Günter Klöppel, and Simon L. Goodman. "Abstract 2321: Expression of functional forms of αvβ3 and αvβ5 integrins, laminin-5 and vitronectin in common human tumors: Consequences for cilengitide targeting." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2321.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Tatler, AL, M. Xu, J. Porte, A. Knox, L. Pang, and G. Jenkins. "Activation of Transforming Growth Factor-β by Human Airway Smooth Muscle Cells Via αvβ5 Integrin." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a5136.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Tancioni, Isabelle, Christine Lawson, Nichol L. G. Miller, Sean Uryu, Christine Jean, Xiao L. Chen, Ssang-Taek Lim, Kristy Ward, and David D. Schlaepfer. "Abstract 1254: FAK activity regulates αvβ5 integrin and osteopontin expression to control breast and ovarian cancer anchorage-independent growth." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1254.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Decaris, M., J. Schaub, C. Chen, J. Cha, G. Lee, M. Rexhepaj, V. Rao, et al. "Dual αVβ6/αVβ1 Inhibitor PLN-74809 Reduces Fibrogenesis in Ex Vivo and In Vivo Models of IPF." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a5875.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Gorina, E., M. Decaris, S. Turner, I. Lepist, S. Wong, E. Park, J. Cha, K. Leftheris, and E. Lefebvre. "PLN-74809, A Dual αVβ6/αVβ1, Oral, Selective Integrin Inhibitor, Is Well Tolerated and Reduces Lung TGF-β Activity in Healthy Volunteers." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a4554.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Cho, Hongkwan, Abdul Sheikh, and Daria A. Narmoneva. "Non-Specific Endothelial Cell Interactions With the Substrate Result in Cell Activation and Angiogenesis In Vitro." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19094.

Full text
Abstract:
Vascularization is critical for success of tissue engineering applications. Previous studies by us and others have shown that self-assembling peptide nanoscaffold RAD16-II promotes de novo capillary formation (angiogenesis) in vitro and neovascularization in vivo, and is a promising material for tissue engineering applications [1, 2]. However, the molecular mechanisms for cell interactions with this material are not known. Angiogenesis is mediated via interactions between integrins, which are expressed on the surface of activated endothelial cells (ECs), and extracellular matrix proteins. Among several integrins, αvβ3 is the most abundant and influential receptor regulating angiogenesis [3]. The αvβ3 integrin binds to its ligands via Arg-Gly-Asp (RGD) biding motif. However, there are no RGD motifs on RAD 16-II peptide. Instead, it contains three RAD motifs. Studies have shown that non-specific binding of αvβ3 with RAD can be retained through R and D sides [4]. The objective of this study, therefore, is to elucidate the underlying molecular mechanisms of RAD16-II nanoscaffold interactions with microvascular endothelial cells. We hypothesize that non-specific interactions between RAD16-II peptide nanoscaffold and αvβ3 integrin result in phosphorylations of β3 cytoplasmic domain, which then activate downstream angiogenic signaling pathways and promote angiogenesis.
APA, Harvard, Vancouver, ISO, and other styles
7

Maciaszek, Jamie L., Biree Andemariam, and George Lykotrafitis. "Modulation of BCAM/Lu and ICAM-4 Expression on Red Blood Cell Membranes in Physiological Stress Conditions." In ASME 2011 International Mechanical Engineering Congress and Exposition. ASMEDC, 2011. http://dx.doi.org/10.1115/imece2011-62143.

Full text
Abstract:
Using single-molecule atomic force microscopy (AFM) experiments, we report that epinephrine, a hormone secreted during stress and strenuous exercise, increases both the frequency and strength of adhesion events of sickle cell trait erythrocytes to the endothelial extracellular matrix (ECM). The specific interactions quantified include Lutheran (BCAM/Lu) and intercellular adhesion molecule-4 (ICAM-4) on the RBC surface with ECM laminin and endothelial αvβ3, respectively. These data present significant evidence of the role of epinephrine in BCAM/Lu-laminin and ICAM-4-αvβ3 bonding, and suggest mechanisms of vaso-occlusion during physical exertion in SCT.
APA, Harvard, Vancouver, ISO, and other styles
8

Haugh, Matthew G., and Laoise M. McNamara. "The Role of Integrins in Osteocyte Response to Mechanical Stimulus." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80126.

Full text
Abstract:
Bone is an exceptional material that is efficiently lightweight, possesses excellent mechanical strength and can also adapt itself in response to changes in physical activity by means of coordinated physiological processes known as modelling and remodelling. The response of bone to mechanical loading is thought to be regulated by mechanosensitive osteocyte cells that can direct the alteration of bone mass, by osteoblasts and osteoclasts, and thereby play an important role in optimizing bone strength. The mechanisms by which osteocytes sense their mechanical environment are not well understood. It has been proposed that integrin-based (αVβ3) attachments to ECM on osteocyte cell processes may facilitate mechanosensation in osteocytes [1,2]. While previous studies have shown that integrin beta;1 plays an important role in response to mechanical stimulus, the role of integrin αVβ3 in osteocyte mechanotransduction has yet to be investigated [3,4].
APA, Harvard, Vancouver, ISO, and other styles
9

Chen, Wei, Jizhong Lou, Jen Hsin, Klaus Schulten, and Cheng Zhu. "In Silico Force-Induced Unbending of αVβ3 Integrin." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206205.

Full text
Abstract:
Integrins are type I transmembrane heterodimers that consist of two noncovalently associated α- and β-subunits. They mediate cell-cell, cell-extracellular matrix, and cell-pathogen adhesions in a wide variety of physiological and pathological processes [1].
APA, Harvard, Vancouver, ISO, and other styles
10

Quigley, N., M. Weinmüller, S. Di Maro, F. S. Di Leva, S. Tomassi, F. Richter, L. Marinelli, and J. Notni. "Trimere αvβ6-Integrin-gerichtete Ga-68-Peptide mit verbesserten in-vivo-Eigenschaften." In NuklearMedizin 2020. © Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0040-1708200.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Αvβ5' for particular source types:
Journal articles Dissertations / Theses
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography