Relevant bibliographies by topics / Pancreatic cancer Sp proteins

Contents

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

Academic literature on the topic 'Pancreatic cancer Sp proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 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 'Pancreatic cancer Sp proteins.'

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 "Pancreatic cancer Sp proteins"

1

Abdelrahim, Maen, Shengxi Liu, and Stephen Safe. "Induction of Endoplasmic Reticulum-induced Stress Genes in Panc-1 Pancreatic Cancer Cells Is Dependent on Sp Proteins." Journal of Biological Chemistry 280, no. 16 (March 8, 2005): 16508–13. http://dx.doi.org/10.1074/jbc.c500030200.

Full text
Abstract:
Endoplasmic reticulum (ER) stress plays a critical role in multiple diseases, and pharmacologically active drugs can induce cell death through ER stress pathways. Stress-induced genes are activated through assembly of transcription factors on ER stress response elements (ERSEs) in target gene promoters. Gel mobility shift and chromatin immunoprecipitation assays have confirmed interactions of NF-Y and YY1 with the distal motifs of the tripartite ERSE from the glucose-related protein 78 (GRP78) gene promoter. The GC-rich nonanucleotide (N9) sequence, which forms the ER stress response binding factor (ERSF) complex binds TFII-I and ATF6; however, we have now shown that in Panc-1 pancreatic cancer cells, this complex also binds Sp1, Sp3, and Sp4 proteins. Sp proteins are constitutively bound to the ERSE; however, activation of GRP78 protein (or reporter gene) by thapsigargin or tunicamycin is inhibited after cotransfection with small inhibitory RNAs for Sp1, Sp3, and Sp4. This study demonstrates that Sp transcription factors are important for stress-induced responses through their binding to ERSEs.
APA, Harvard, Vancouver, ISO, and other styles
2

Oberoi, Shilpa, Rajesambhaji Borade, Neal McCollum, Santhi D. Konduri, Jimmie F. Colon, Cheryl H. Baker, and Maen Abdelrahim. "M2025 Inhibiting Pancreatic Cancer Growth and Sensitizing the Tumor to Radiotherapy Through Downregulation of SP Proteins." Gastroenterology 134, no. 4 (April 2008): A—453. http://dx.doi.org/10.1016/s0016-5085(08)62118-6.

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

Higgins, Kelly J., Maen Abdelrahim, Shengxi Liu, Kyungsil Yoon, and Stephen Safe. "Regulation of vascular endothelial growth factor receptor-2 expression in pancreatic cancer cells by Sp proteins." Biochemical and Biophysical Research Communications 345, no. 1 (June 2006): 292–301. http://dx.doi.org/10.1016/j.bbrc.2006.04.111.

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

Fernandez-Zapico, M. E., S. Tsuji, and R. Urrutia. "GLOBAL FUNCTIONAL ANALYSIS OF SP/KLF PROTEINS IDENTIFY KLF11 AS NOVEL TUMOR SUPPRESSOR CANDIDATE FOR PANCREATIC CANCER." Pancreas 31, no. 4 (November 2005): 441. http://dx.doi.org/10.1097/01.mpa.0000193667.32396.85.

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

Abdelrahim, Maen, Roger Smith, Robert Burghardt, and Stephen Safe. "Role of Sp Proteins in Regulation of Vascular Endothelial Growth Factor Expression and Proliferation of Pancreatic Cancer Cells." Cancer Research 64, no. 18 (September 15, 2004): 6740–49. http://dx.doi.org/10.1158/0008-5472.can-04-0713.

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

Safe, Stephen, Vijayalekshmi Nair, and Keshav Karki. "Metformin-induced anticancer activities: recent insights." Biological Chemistry 399, no. 4 (March 28, 2018): 321–35. http://dx.doi.org/10.1515/hsz-2017-0271.

Full text
Abstract:
AbstractMetformin is a widely used antidiabetic drug, and there is evidence among diabetic patients that metformin is a chemopreventive agent against multiple cancers. There is also evidence in human studies that metformin is a cancer chemotherapeutic agent, and several clinical trials that use metformin alone or in combination with other drugs are ongoing.In vivoandin vitrocancer cell culture studies demonstrate that metformin induces both AMPK-dependent and AMPK-independent genes/pathways that result in inhibition of cancer cell growth and migration and induction of apoptosis. The effects of metformin in cancer cells resemble the patterns observed after treatment with drugs that downregulate specificity protein 1 (Sp1), Sp3 and Sp4 or by knockdown of Sp1, Sp3 and Sp4 by RNA interference. Studies in pancreatic cancer cells clearly demonstrate that metformin decreases expression of Sp1, Sp3, Sp4 and pro-oncogenic Sp-regulated genes, demonstrating that one of the underlying mechanisms of action of metformin as an anticancer agent involves targeting of Sp transcription factors. These observations are consistent with metformin-mediated effects on genes/pathways in many other tumor types.
APA, Harvard, Vancouver, ISO, and other styles
7

Hurtado, Myrna, Umesh T. Sankpal, Aboubacar Kaba, Shahela Mahammad, Jaya Chhabra, Deondra T. Brown, Raj K. Gurung, Alvin A. Holder, Jamboor K. Vishwanatha, and Riyaz Basha. "Novel Survivin Inhibitor for Suppressing Pancreatic Cancer Cells Growth via Downregulating Sp1 and Sp3 Transcription Factors." Cellular Physiology and Biochemistry 51, no. 4 (2018): 1894–907. http://dx.doi.org/10.1159/000495715.

Full text
Abstract:
Background/Aims: Targeting survivin, an anti-apoptotic protein and mitotic regulator, is considered as an effective therapeutic option for pancreatic cancer (PaCa). Tolfenamic acid (TA) showed anti-cancer activity in pre-clinical studies. A recent discovery demonstrated a copper(II) complex of TA (Cu-TA) can result in higher activity. In this study, the ability of Cu-TA to inhibit survivin and its transcription factors, Specificity protein (Sp) 1 and 3 in PaCa cell lines and tumor growth in mouse xenograft model were evaluated. Methods: Cell growth inhibition was measured in MIA PaCa-2 and Panc1 cells for 2 days using CellTiter-Glo kit. Sp1, Sp3 and survivin expression (by Western blot and qPCR), apoptotic cells and cell cycle phase distribution (by flow cytometry) were evaluated. A pilot study was performed using athymic nude mice [treated with vehicle/Cu-TA (25 or 50 mg/kg) 3 times/week for 4 weeks. Results: The IC50 value for Cu-TA was about half than TA.Both agents repressed the protein expression of Sp1/Sp3/survivin, Cu-TA was more effective than TA. Especially effect on survivin inhibition was 5.2 (MIA PaCa-2) or 6.4 (Panc1) fold higher and mRNA expression of only survivin was decreased. Apoptotic cells increased with Cu-TA treatment in both cell lines, while Panc1 showed both effect on apoptosis and cell cycle (G2/M) arrest. Cu-TA decreased the tumor growth in mouse xenografts (25 mg/kg: 48%; 50 mg/kg: 68%). Additionally, there was no change observed in mice body weights, indicating no overt toxicity was occurring. Conclusion: These results show that Cu-TA can serve as an effective survivin inhibitor for inhibiting PaCa cell growth.
APA, Harvard, Vancouver, ISO, and other styles
8

Zheng, Lanhong, Xiangjie Zhu, Kangli Yang, Meihong Zhu, Ammad Farooqi, Daole Kang, Mi Sun, et al. "PBN11-8, a Cytotoxic Polypeptide Purified from Marine Bacillus, Suppresses Invasion and Migration of Human Hepatocellular Carcinoma Cells by Targeting Focal Adhesion Kinase Pathways." Polymers 10, no. 9 (September 19, 2018): 1043. http://dx.doi.org/10.3390/polym10091043.

Full text
Abstract:
The development of antitumor drugs has attracted cancer researchers and the identification of novel antitumor lead compounds is certainly of great interest. The fermentation broth of Bacillus sp. N11-8, which was isolated from the Antarctic waters, showed cytotoxicity towards different cells. A cytotoxic polypeptide, PBN11-8, was purified from the fermentation broth of Bacillus sp. N11-8 using ultrafiltration, ammonium sulfate precipitation, anion exchange liquid chromatography and high performance liquid chromatography (HPLC). Cloning and sequence analysis showed that PBN11-8 polypeptide (MW: ~19 kDa by the electrospray-ionization (ESI)) displayed high similarity with peptidase M84 from Bacillus pumilus. PBN11-8 possessed moderate cytotoxicity towards several cancer cell lines with IC50 values of 1.56, 1.80, 1.57, and 1.73 µg/mL against human hepatocellular carcinoma cell line BEL-7402, human renal clear cell adenocarcinoma cell line 786-0, human hepatocellular carcinoma cell line HepG2, and human pancreatic cancer cell line Panc-28, respectively. Moreover, the polypeptide displayed weak cytotoxicity towards normal cell line renal tubular epithelial cell line HK2 and human normal liver cell line L02 cells. Wound healing migration and Transwell experiments demonstrate that PBN11-8 could inhibit the migration and invasion of BEL-7402. Further investigation revealed that PBN11-8 suppresses focal adhesion kinase (FAK)-mediated adhesion, migration, and invasion by disturbing FAK/extracellular regulated protein kinases (ERK) signaling and matrix metalloproteinase-2(MMP-2) and matrix metalloproteinase-9 (MMP-9) in BEL-7402 cells. Thus, PBN11-8 represents a potential novel anti-cancer lead compound.
APA, Harvard, Vancouver, ISO, and other styles
9

Patel, Asish, Sukhwinder Kaur, Lynette Smith, Chandrakanth Are, and Surinder Batra. "Diagnostic potential of mucins in pancreatic juice for pancreatic cancer." Journal of Clinical Oncology 34, no. 4_suppl (February 1, 2016): 222. http://dx.doi.org/10.1200/jco.2016.34.4_suppl.222.

Full text
Abstract:
222 Background: Pancreatic juice remains an underutilized resource for diagnosing pancreatic cancer. Mucins are high molecular weight glycoproteins differentially upregulated in pancreatic cancer, and we hypothesize that their profile in pancreatic juice may have diagnostic potential. Methods: Pancreatic juice was obtained during endoscopy from non-healthy non-pancreatic control (NHPC, n = 57), chronic pancreatitis (CP, n = 23), and pancreatic cancer (PC, n = 23) patients. Sandwich ELISA was used to detect MUC1, MUC4, MUC5AC, CA125, and CA19-9. Kruskal-Wallis test and Wilcoxon rank sum test for group and pairwise comparison was done with p < 0.05 as significant. Logistic regression with ROC curve modeling of log transformed data was done for each biomarker individually and in combination to determine odds ratio (OR), sensitivity (SN), and specificity (SP) for PC. Results: PC vs NHPC: MUC5AC had the best individual performance for diagnosing PC with an OR = 2.78 (95% CI = 1.51-5.13), AUC = 0.81, and optimal SN/SP of 0.83 and 0.67, respectively. CA125 was increased in PC with an OR = 2.31 (95% CI = 1.4-4.0), AUC = 0.73, and optimal SN/SP of 0.88 and 0.67. CA19-9 was increased in PC with an OR = 1.5 (95% CI = 1.2-1.8), AUC = 0.76, and optimal SN/SP of 0.73 and 0.70. A combination of MUC1, MUC5AC, CA125, and CA19-9 outperformed all individual markers and had the largest AUC (0.89) with optimal SN/SP of 0.84 and 0.79. PC vs CP: MUC1 concentration in PC was significantly less than CP with an OR = 0.21 (95%CI = 0.088-0.49), AUC = 0.82, and optimal SN/SP of 0.87 and 0.78. PC vs NHPC+CP: MUC1 was decreased significantly in PC with an OR = 0.65 (95% CI = 0.44-0.96), AUC = 0.69, and optimal SN/SP of 0.87 and 0.63. CA125 was increased in PC with an OR = 1.64 (95%CI = 1.1-2.4), AUC = 0.66, and optimal SN/SP of 0.67 and 0.64. CA19-9 was increased in PC with an OR = 1.32 (95%CI = 1.1-1.6), AUC = 0.68, and optimal SN/SP of 0.63 and 0.67. A combination of MUC1, MUC5AC, CA125, and CA19-9 had an AUC = 0.86 with optimal SN/SP of 0.87 and 0.77 for PC. Conclusions: MUC1, MUC5AC, CA125, and CA19-9 combination provides a significantly improved diagnostic panel compared to any individual marker in pancreatic juice for detecting malignancy.
APA, Harvard, Vancouver, ISO, and other styles
10

Mann, Karen M., Haoqiang Ying, Joseph Juan, Nancy A. Jenkins, and Neal G. Copeland. "KRAS-related proteins in pancreatic cancer." Pharmacology & Therapeutics 168 (December 2016): 29–42. http://dx.doi.org/10.1016/j.pharmthera.2016.09.003.

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

Dissertations / Theses on the topic "Pancreatic cancer Sp proteins"

1

Higgins, Kelly Jean. "Regulation of vascular endothelial growth factor receptor-2 in pancreatic and breast cancer cells by Sp proteins." Texas A&M University, 2003. http://hdl.handle.net/1969.1/6010.

Full text
Abstract:
Vascular endothelial growth factor receptor-2 (VEGFR2) is a key angiogenic factor, and angiogenesis is an important physiological process associated with neovascularization, growth, and metastasis of many different tumors. The mechanism of VEGFR2 gene expression was investigated in MiaPaCa-2, Panc-1, and AsPC-1 pancreatic cancer cells transfected with a series of VEGFR2 promoter deletion/mutated constructs, and the results indicated that the GC-rich –60 to –37 region of the promoter was essential for VEGFR2 expression in these cell lines. EMSA and ChIP assays showed that Sp proteins are expressed and bind to the proximal GC-rich region of the VEGFR2 promoter. RNA interference studies on Sp proteins demonstrated that Sp1, Sp3, and Sp4 all contributed to VEGFR2 gene/protein expression in pancreatic cancer cells. VEGFR2 gene expression was also investigated in ZR-75 and MCF-7 breast cancer cells. ZR-75 cells treated with 10 nM 17b-estradiol (E2) increased VEGFR2 mRNA levels/protein expression. The VEGFR2 promoter was induced by E2 in ZR-75 cells, and analysis of the VEGFR2 promoter identified the GC rich -60 to -37 region that was required for E2-mediated transactivation. EMSA and ChIP assays confirmed that Sp1, Sp3, and Sp4 proteins are expressed in ZR-75 cells and bind the proximal GC-rich region of the VEGFR2 promoter. RNA interference was used to determine the relative contributions of Sp proteins on hormonal regulation of VEGFR2 through ER/Sp complexes, and interestingly, in ZR-75 cells, hormone-induced activation of VEGFR2 involves ERa/Sp3 and ERa/Sp4 but not ERa/Sp1. In MCF-7 cells treated with 10 nM E2, VEGFR2 mRNA levels were decreased. Analysis of the VEGFR2 promoter revealed that the same GC-rich region important for E2-mediated upregulation in ZR-75 cells was responsible for E2-dependent downregulation of VEGFR2 gene expression in MCF-7 cells. EMSA and ChIP assays confirmed that Sp1, Sp3, and Sp4 proteins are expressed in MCF-7 cells and bind to the proximal GC-rich region of the VEGFR2 promoter. RNA interference studies showed that Sp1, Sp3, and Sp4 are involved in the E2-mediated downregulation of VEGFR2 in MCF-7 cells, and ERa/Sp protein-promoter interactions are accompanied by recruitment of the corepressor SMRT using the ChIP assay.
APA, Harvard, Vancouver, ISO, and other styles
2

Abdel, Rahim Ma'en Ahmad. "Gene silencing in cancer cells using siRNA : genetic and functional studies." Diss., Texas A&M University, 2004. http://hdl.handle.net/1969.1/218.

Full text
Abstract:
Sequence-specific small interfering RNA (siRNA) duplexes can be used for gene silencing in mammalian cells and as mechanistic probes for determining gene function. Transfection of siRNA for specificity protein 1 (Sp1) in MCF-7 or ZR-75 cells decreased Sp1 protein in nuclear extracts, and immunohistochemical analysis showed that Sp1 protein in transfected MCF-7 cells was barely detectable. Decreased Sp1 protein in MCF-7 was accompanied by a decrease in basal and estrogen-induced transactivation and cell cycle progression. These results clearly demonstrate the key role of Sp1 protein in regulating growth and gene expression of breast cancer cells. The aryl hydrocarbon (AhR) is a ligand-activated nuclear transcription factor. siRNA for the AhR decreased TCDD-induced CYP1A1 protein, CYP1A1dependent activity, and luciferase activity in cells transfected with an Ah-responsive construct. 17β-Estradiol (E2) induces proliferation of MCF-7 cells, and this response is inhibited in cells cotreated with E2 plus TCDD. The effects of TCDD on E2-induced cell cycle progression were partially blocked in MCF-7 cells transfected with siRNA for AhR. The decrease in AhR protein in MCF-7 cells was also accompanied by increased G0/G1 → S phase progression. Surprisingly, TCDD alone induced G0/G1 → S phase progression and exhibited estrogenic activity in MCF-7 cells transfected with siRNA for the AhR. In contrast, degradation of the AhR in HepG2 liver cancer cells resulted in decreased G0/G1 → S phase progression, and this was accompanied by decreased expression of cyclin D1, cyclin E, cdk2 and cdk4. In the absence of ligand, the AhR exhibits growth inhibitory (MCF-7) and growth promoting (HepG2) activity that is cell context-dependent. Sp family proteins play a complex role in regulation of pancreatic cancer cells growth and expression of genes required for growth, angiogenesis and apoptosis. Sp1, Sp3 and Sp4 cooperatively activate VEGF promoter constructs in these cells; however, only Sp3 regulates cell proliferation. siRNA for Sp3 inhibits phosphorylation of retinoblastoma protein, blocks G0/G1 → S phase progression of Panc-1 cells, and upregulates p27 protein/promoter activity. Thus, Sp3 plays a critical role in angiogenesis (VEGF upregulation) and the proliferation of Panc-1 cells by a novel mechanism of Sp3-dependent suppression of the cyclin-dependent kinase inhibitor p27.
APA, Harvard, Vancouver, ISO, and other styles
3

Balmaña, Esteban Meritxell. "Pancreatic cancer markers based on aberrant glycosylation of serum proteins." Doctoral thesis, Universitat de Girona, 2016. http://hdl.handle.net/10803/392636.

Full text
Abstract:
Cancer is one of the leading causes of death worldwide. Pancreatic ductal adenocarcinoma (PDAC) is characterized by high intrinsic aggressiveness and late diagnosis, causing poor prognosis and resulting in the lowest five-year survival rate among all cancers. Nowadays, there is no biomarker for PDAC diagnosis approved. The survival rate of cancer patients increases when they are diagnosed in the early stages of the pathology; and for this reason, the research of new biomarkers is of great interest. Tumour cells present aberrant glycosylation on their cell surface and also in the secreted glycoconjugates. Hence, a strategy for new tumour biomarker discovery is based on the identification of specific glycoforms. This work has explored the glycosylation of two serum glycoproteins, the alpha-1-acid glycoprotein (AGP) and the ceruloplasmin (CP). The glycosylation of the epithelial mucins MUC1 and MUC5AC in healthy and PDAC tissues has also been analysed.
El càncer és una de les principals causes de mort. L’adenocarcinoma ductal pancreàtic (PDAC) es caracteritza per una alta agressivitat i un diagnòstic tardà, causant un pronòstic desolador i resultant en el càncer amb la taxa relativa de supervivència als cinc anys menor. Actualment no es disposa d’un biomarcador per al diagnòstic del PDAC.La supervivència dels pacients augmenta quan són diagnosticats en els estadis inicials; per aquest motiu, la recerca de nous marcadors és de gran importància. Les cèl·lules tumorals presenten una glicosilació aberrant en la seva superfície cel·lular i també en els glicoconjugats que secreten. Per tant, una estratègia per al descobriment de nous biomarcadors es basa en la identificació de glicoformes específiques. Aquesta tesi ha explorat la glicosilació de dues glicoproteïnes del sèrum, la alfa-1-glicoproteïna àcida i la ceruloplasmina. També s’ha analitzat la glicosilació de les mucines epitelials MUC1 i MUA5AC en teixits sans i de PDAC.
APA, Harvard, Vancouver, ISO, and other styles
4

Bastien, Jacynthe. "Inhibitor of apoptosis proteins and associated factors in pancreatic cancer." Thesis, University of Ottawa (Canada), 2005. http://hdl.handle.net/10393/29194.

Full text
Abstract:
Since the phenomenon was first identified, apoptosis has been proposed to serve as a barrier to the development of cancer in metazoans. Over the years, the inability to carry out apoptosis has been implicated in the initiation, formation and progression of tumors. Moreover, acquired resistance to apoptosis is now believed to represent a major obstacle to the successful application of oncotherapies. Caspases play a central role in the induction and execution of apoptosis. As such, their activity must be tightly regulated. To date, inhibitor of apoptosis proteins (IAPs) are the only known intrinsic regulators of caspase function. The present study focused on the identification of molecular targets differentially expressed in normal and cancer cells that could serve to facilitate the rational design of anti-cancer therapies. We hypothesized that variations in the levels of key apoptotic regulators such as caspases, IAPs and their antagonists could conceivably contribute to the acknowledged resistance of pancreatic cancer cells to cytotoxic therapies. Our first specific aim was to derive an expression profile of apoptotic modulator/effector genes in pancreatic cancer cell lines. Our analysis uncovered a tendency towards up-regulation of IAP expression (namely cIAP-2) and down-regulation of pro-apoptotic factors such as caspases and the Xiap antagonist Xaf-1 in these cell lines. In particular, Xaf1 protein expression appeared to be completely repressed in neoplastic cell lines. Moreover, over-expression of one or more IAPs was observed in several solid malignancies. Lastly, while Xiap expression and subcellular localization were not altered in evolving intraductal lesions and pancreatic tumors, immunohistological surveys uncovered over-expression and nuclear redistribution of cIAP-1, cIAP-2 and survivin in pancreatic adenocarcinomas. Our second objective was to determine if differential expression of IAPs influenced the sensitivity of three human pancreatic cancer cell lines to drug-induced apoptosis. In vitro studies uncovered a good correlation between transcriptional up-regulation of IAPs, caspase-dependent cleavage of Xiap, activation of downstream effector caspase-3 and rapidity of onset of etoposide-induced apoptosis in these cell lines. In particular, endogenous levels of cIAP-2 mRNA appeared to be good predictors of etoposide-responsiveness. However, attempts at sensitizing pancreatic cancer cells to etoposide by down-modulating Xiap expression via over-expression of Xaf-1 or siRNA-mediated degradation of Xiap were unsuccessful. (Abstract shortened by UMI.)
APA, Harvard, Vancouver, ISO, and other styles
5

Suliman, Muhtadi. "Interactome analysis of pancreatic cancer expressed proteins : a yeast two hybrid approach." Aix-Marseille 2, 2008. http://theses.univ-amu.fr.lama.univ-amu.fr/2008AIX22002.pdf.

Full text
Abstract:
L'adénocarcinome pancréatique (PDAC) est aujourd’hui un problème important de santé publique. Les traitements conventionnels contre le cancer ont peu d'impact sur le cours de cette maladie. Les changements génétiques impliqués dans la progression du PDAC concernent souvent des gènes qui codent pour des protéines liées à différentes voies de transduction de signal. Ce fait indique l'importance d’identifier le rôle et les relations entre les multiples voies de signalisation impliquées dans le PDAC. Dans ce travail nous utilisons une approche double-hybride chez la levure pour identifier des interactions impliquant des protéines exprimées dans des cellules cancéreuses pancréatiques. Dans la première partie de cette thèse, un groupe particulier de protéines, les protéines d’échafaudage, contenant de multiples domaines (SH3), a été étudié. Nous avons identifié plusieurs molécules interagissant avec ces protéines, modulant la prolifération cellulaire, la survie (CIZ1, BIRC6, RBBP6), la signalisation (LTBP4, Notch2, TOM1L1, STK24) et la dynamique des membranes (PLSCR1, DDEF2, VCP). Certaines protéines interagissant avec (Vav2, ITSN1, Stac) sont connues pour leurs différents rôles dans le vésicules de transport, l'endocytose ainsi que dans d’autres processus de régulation. Nous avons aussi dentifié des interactions protéiques assurées par d’autres protéines exprimées dans le pancréas, et ce pour identifier les événements qui sont spécifiques aux cellules cancéreuses pancréatiques. PTFIA est un activateur de transcription qui joue un rôle déterminant dans l’organogenèse pancréatique, il est aussi impliqué dans la maintenance du pancréas exocrine. Cette protéine contient un domaine HLH qui facilite la conversion des monomères inactifs en dimères s’activant pendant les étapes appropriées du développement. Nous avons identifié plusieurs molécules interagissant avec cette protéine, modulant la prolifération cellulaire (GCIP); différentiation de macrophage (PRKX) et la tumorigenesis d'intestinal. KLF6 est un facteur de transcription qui peut activer ou inhiber des gènes impliqués dans la régulation du cycle cellulaire. Quelques études présentent KLF6 comme étant un facteur de transcription impliqué dans la prolifération cellulaire. Il a été récemment démontré qu’il était déréglé dans des multiples cancers (prostate et ovaires), dérèglement traduit par une perte d’hétérozygotie. Nous avons identifié plusieurs molécules interagissant avec cette protéine, modulant la Ribosylation (PARP10) et l’adhésion (MSN). ArgBP2 a été récemment identifié comme étant un nouveau marqueur pour le cancer pancréatique et potentiellement une nouvelle cible thérapeutique. ArgBP2 est un substrat et interacteur des tyrosines kinases Arg et Abl, il a aussi été trouvé concentré sur les fibres d'actine. ArgBP2 appartiennent à une famille de protéines d'échafaudage qui incluent la vinexine et le CAP/ponsin; ils participent à la régulation de l’adhésion cellulaire, l’organisation du cytosquelette d'actine et la signalisation, en aval, des récepteurs de facteurs de croissance. La protéine ArgBP2 est caractérisée par un domaine (SoHo) dans la région N-terminal et trois domaines SH3 dans la région de C-terminal. Nous avons identifié la protéine CIP4 (Cdc42 interacting protein 4) comme étant un nouvel interacteur d’ArgBP2. Nous avons montré que, par cette interaction, ArgBP2 pouvait augmenter la capacité de c-Abl à phosphiryler CIP4 et que CIP4, après interaction, pouvait inhiber la phosphorylation d'ArgBP2. L’utilisation de petites molécules capables de perturber les interactions et l'analyse de l’effet de ces pertes d’interactions sur la croissance des cellules cancéreuses pancréatiques, in vivo et in vitro, pourraient permettre d’identifier des agents thérapeutiques potentiels pour le traitement du cancer pancréatique, une des maladies les plus meurtrières connues.
APA, Harvard, Vancouver, ISO, and other styles
6

Sarrats, Carbó Ariadna. "Glycan alterations of serum proteins as tumour markers. Prostate-specific antigen in prostate cancer and acute-phase proteins in pancreatic cancer." Doctoral thesis, Universitat de Girona, 2011. http://hdl.handle.net/10803/31943.

Full text
Abstract:
Els pacients amb càncer presenten una taxa de supervivència superior si es diagnostiquen a estadis inicials, per la qual cosa és indispensable disposar de marcadors tumorals adequats. Glicoformes de proteïnes específiques es podrian utilizar com marcadors tumorals. S’han investigat les subformes i glicosilació de l’Antígen Prostàtic Específic (PSA) per millorar la seva capacitat de diagnosis de pacients amb càncer de pròstata vs aquells amb hiperplàsia benigna prostàtica. També s’han avaluat glicoproteïnes sèriques amb alteracions glucídiques en pacients de càncer de pàncrees, comparat amb pacients amb pancreatitis crònica i controls. S’ha observat una disminució de la fucosilació core i sialilació del PSA en càncer de pròstata i un augment de la fucosilació core i Sialyl-Lewis X en algunes Proteïnes de fase Aguda en càncer de pàncrees. Aquest canvis s’haurien d’avaluar en un cohort de pacients més gran per determinar el seu paper en el cribratge, diagnòstic o monitorització dels cancers estudiats.
The survival rate of cancer patients is increased when they are diagnosed at localized stage, for which the availability of adequate tumour markers is crucial. The determination of specific tumour‐associated glycoforms may either improve the specificity of known cancer biomarkers such Prostate-Specific Antigen (PSA) or allow the discovery of new tumour markers. This work has investigated PSA subforms and their glycosylation with the aim to improve the differentiation between prostate cancer and benign prostatic hyperplasia. In addition, serum glycoproteins with altered glycosylation have been evaluated in pancreatic cancer patients, compared to chronic pancreatitis patients and healthy controls. A decrease of PSA core fucosylation and sialylation in Prostate cancer and an increase in some Acute-Phase Proteins core fucosylation and Sialyl-Lewis X in pancreatic cancer were observed. These changes should be evaluated in a larger cohort of patients to determine their role as prostate and pancreatic cancer biomarkers, respectively.
APA, Harvard, Vancouver, ISO, and other styles
7

Dawson, Amanda Caroline St Vincent???s Hospital Clinical School UNSW. "Evaluation of novel molecular markers from the WNT pathway : a stepwise regression model for pancreatic cancer survival." Awarded by:University of New South Wales. St Vincent???s Hospital Clinical School, 2007. http://handle.unsw.edu.au/1959.4/31528.

Full text
Abstract:
Optimisation of the conventional tripartite of pancreatic cancer (PC) treatment have led to significant improvements in mortality, however further knowledge of the underlying molecular processes is still required. Transcript profiling of mRNA expression of over 44K genes with microarray technology demonstrated upregulation of secreted frizzled related protein 4 (sFRP4) and ??-catenin in PC compared to normal pancreata. Their pathway ??? Wnt signalling is integral to transcriptional regulation and aberrations in these molecules are critical in the development of many human malignancies. Immunohistochemistry protocols were evaluated by two independent blinded examiners for antigen expression differences associated with survival patterns in 140 patients with biopsy verified PC and a subset of 23 normal pancreata with substantial observer agreement (kappa value 0.6-0.8). A retrospective cohort was identified from 6 Sydney hospitals between 1972-2003 and archival formalin fixed tissue was collected together with clinicopathological data. Three manual stepwise regression models were fitted for overall, disease-specific and relapse-free survival to determine the value of significant prognostic variables in risk stratification. The models were fitted in a logical order using a careful strategy with step by step interpretation of the results. Immunohistochemistry demonstrated increased sFRP4 membranous expression (> 10%) in 49/95 PC specimens and this correlated with improved overall survival (HR:0.99;95%CI:0.97-6.40;LRchi2=134.75; 1df; ??< 0.001). Increased sFRP4 cytoplasmic staining (> 2/3) in 46/85 patients increased the disease-specific survival (HR:0.52;95%CI:0.31-0.89;LR test statistic =248.40;1df;??< 0.001). Increasing ??-catenin membranous expression (< _60%) in 26/116 patients was associated with an increased risk of overall death (HR:3.18;95%CI:1.14-8.89;LR test statistic =4.61;1df,??< 0.05). Increasing cytoplasmic expression in 65/114 patients was protective and was associated with prolonged survival on univariate, but not multivariate analysis (Disease specific survival HR:0.75;95%CI:0.56-1.00;logrank chi2=3.91;1df; ??=0.05). Increased nuclear ??-catenin expression in 65/114 patients was associated with prolonged survival (disease-specific HR:0.92;95%CI:0.83-1.02; LR test statistic= 49.72;1df;??< 0.001). At the conclusion, 12 patients (8.6%) remained alive, 122 died of their disease (68 males versus 54 females). They were followed for a median of 8.7 months (range 1.0-131.3) months. The median age was 66.5 years (range 34.4-96.0, standard deviation 10.9) years. Pancreatic resection was achieved in 79 patients with 46.8% achieving RO resection. The 30 day post-operative mortality was 2.1%. The overall 1 year survival rate was (33.7% ; 95%CI: 25.78-33.79) with a 5 year survival of (2.87%, 95%CI: 2.83-6.01) and a median survival of (8.90 months; 95%CI: 7.5-10.2). The median disease-specific survival was (9.40; 95%CI: 7.9-10.5 months) and the median time to relapse was 1.2 months (95%CI 1.0-1.2 months). A central tenet of contemporary cancer research is that an understanding of the genetic and molecular abnormalities that accompany the development and progression of cancer is critical to further advances in diagnosis, treatment and eventual prevention. High throughput tissue microarrays were used to study expression of two novel tumour markers in a cohort of pancreatic cancer patients and identified sFRP4 and ??-catenin as potential novel prognostic markers.
APA, Harvard, Vancouver, ISO, and other styles
8

Appleman, Victoria A. "Mechanisms of KRAS-Mediated Pancreatic Tumor Formation and Progression: A Dissertation." eScholarship@UMMS, 2012. https://escholarship.umassmed.edu/gsbs_diss/600.

Full text
Abstract:
Pancreatic cancer is the 4th leading cause of cancer related death in the United States with a median survival time of less than 6 months. Pancreatic ductal adenocarcinoma (PDAC) accounts for greater than 85% of all pancreatic cancers, and is marked by early and frequent mutation of the KRAS oncogene, with activating KRAS mutations present in over 90% of PDAC. To date, though, targeting activated KRAS for cancer treatment has been very difficult, and targeted therapies are currently being sought for the downstream effectors of activated KRAS. Activation of KRAS stimulates multiple signaling pathways, including the MEK-ERK and PI3K-AKT signaling cascades, but the role of downstream effectors in pancreatic tumor initiation and progression remains unclear. I therefore used primary pancreatic ductal epithelial cells (PDECs), the putative cell of origin for PDAC, to determine the role of specific downstream signaling pathways in KRAS activated pancreatic tumor initiation. As one third of KRAS wild type PDACs harbor activating mutations in BRAF , and KRAS and BRAF mutations appear to be mutually exclusive, I also sought to determine the effect of activated BRAF (BRAF V600E ) expression on PDECs and the signaling requirements downstream of BRAF. I found that both KRAS G12D and BRAF V600E expressing PDECs displayed increased proliferation relative to GFP expressing controls, as well as increased PDEC survival after challenge with apoptotic stimuli. This survival was found to depend on both the MEK-ERK and PI3K-AKT signaling cascades. Surprisingly, I found that this survival is also dependent on the IGF1R, and that activation of PI3K/AKT signaling occurs downstream of MEK/ERK activation, and is dependent on signaling through the IGF1R. Consistent with this, I find increased IGF2 expression in KRAS G12D and BRAF V600E expressing PDECs, and show that ectopic expression of IGF2 rescues survival in PDECs with inhibited MEK, but not PI3K. Finally, I showed that the expression of KRAS G12D or BRAF V600E in PDECs lacking both the Ink4a/Arf and Trp53 tumor suppressors is sufficient for tumor formation following orthotopic transplant of PDECs, and that IGF1R knockdown impairs KRAS and BRAF-induced tumor formation in this model. In addition to these findings within PDECs, I demonstrate that KRAS G12D or BRAF V600E expressing tumor cell lines differ in MEK-ERK and PI3K-AKT signaling from PDECs. In contrast to KRAS G12D or BRAF V600E expressing PDECs, activation of AKT at serine 473 in the KRAS G12D or BRAF V600E expressing tumor cell lines does not lie downstream of MEK, and only the inhibition of PI3K alone or both MEK and the IGF1R simultaneously results in loss of tumor cell line survival. However, inhibition of MEK, PI3K, or the IGF1R in KRAS G12D or BRAF V600E expressing tumor cell lines also resulted in decreased proliferation relative to DMSO treated cells, demonstrating that all three signaling cascades remain important for tumor cell growth and are therefore viable options for pancreatic cancer therapeutics.
APA, Harvard, Vancouver, ISO, and other styles
9

Quattrochi, Brian J. "Subtle Controllers: MicroRNAs Drive Pancreatic Tumorigenesis and Progression: A Dissertation." eScholarship@UMMS, 2015. https://escholarship.umassmed.edu/gsbs_diss/776.

Full text
Abstract:
Pancreatic ductal adenocarcinoma (PDAC) is among the most lethal malignancies in the United States, with an average five-year survival rate of just 6.7%. One unifying aspect of PDAC is mutational activation of the KRAS oncogene, which occurs in over 90% of PDAC. Therefore, inhibiting KRAS function is likely an effective therapeutic strategy for this disease, and current research in our lab and others is focused on identifying downstream effectors of KRAS signaling that may be therapeutic targets. miRNAs are powerful regulators of gene expression that can behave as oncogenes or tumor suppressors. Dysregulation of miRNA expression is commonly observed in human tumors, including PDAC. The mir-17~92 cluster of miRNAs is an established oncogene in a variety of tumor contexts, and members of the mir-17~92 cluster are upregulated in PDAC, but their role has not been explored in vivo. This dissertation encompasses two studies exploring the role of miRNAs in pancreatic tumorigenesis. In Chapter II, I demonstrate that deletion of the mir-17~92 cluster impairs PDAC precursor lesion formation and maintenance, and correlates with reduced ERK signaling in these lesions. mir-17~92 deficient tumors and cell lines are also less invasive, which I attribute to the loss of the miR-19 family of miRNAs. In Chapter III, I find that Dicer heterozygosity inhibits PDAC metastasis, and that this phenotype is attributable to an increased sensitivity to anoikis. Ongoing experiments will determine whether shifts in particular miRNA signatures between cell lines can be attributed to this phenotype. Together these findings illustrate the importance of miRNA biogenesis, and the mir-17~92 cluster in particular, in supporting PDAC development and progression.
APA, Harvard, Vancouver, ISO, and other styles
10

Quattrochi, Brian J. "Subtle Controllers: MicroRNAs Drive Pancreatic Tumorigenesis and Progression: A Dissertation." eScholarship@UMMS, 2004. http://escholarship.umassmed.edu/gsbs_diss/776.

Full text
Abstract:
Pancreatic ductal adenocarcinoma (PDAC) is among the most lethal malignancies in the United States, with an average five-year survival rate of just 6.7%. One unifying aspect of PDAC is mutational activation of the KRAS oncogene, which occurs in over 90% of PDAC. Therefore, inhibiting KRAS function is likely an effective therapeutic strategy for this disease, and current research in our lab and others is focused on identifying downstream effectors of KRAS signaling that may be therapeutic targets. miRNAs are powerful regulators of gene expression that can behave as oncogenes or tumor suppressors. Dysregulation of miRNA expression is commonly observed in human tumors, including PDAC. The mir-17~92 cluster of miRNAs is an established oncogene in a variety of tumor contexts, and members of the mir-17~92 cluster are upregulated in PDAC, but their role has not been explored in vivo. This dissertation encompasses two studies exploring the role of miRNAs in pancreatic tumorigenesis. In Chapter II, I demonstrate that deletion of the mir-17~92 cluster impairs PDAC precursor lesion formation and maintenance, and correlates with reduced ERK signaling in these lesions. mir-17~92 deficient tumors and cell lines are also less invasive, which I attribute to the loss of the miR-19 family of miRNAs. In Chapter III, I find that Dicer heterozygosity inhibits PDAC metastasis, and that this phenotype is attributable to an increased sensitivity to anoikis. Ongoing experiments will determine whether shifts in particular miRNA signatures between cell lines can be attributed to this phenotype. Together these findings illustrate the importance of miRNA biogenesis, and the mir-17~92 cluster in particular, in supporting PDAC development and progression.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "Pancreatic cancer Sp proteins"

1

Chang, Victor T. Visceral pain. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199656097.003.0134.

Full text
Abstract:
Visceral pain is pain that arises from, in, or around internal organs. Common examples include chest pain and functional abdominal pain. In palliative medicine, well-known visceral pain syndromes include pain from pancreatic cancer and bowel obstruction. Recent advances have increased our understanding of the diagnostic challenges and therapeutic possibilities for patients with visceral pain syndromes. Understanding the basis of referred pain is a key component of patient assessment. The complexity of visceral nociception and pain signalling is being unravelled through anatomical, immunohistochemical, and functional studies. On a molecular level, families of receptors and signalling proteins have now been described that will lead to a future with innovative therapies. This knowledge has developed within the paradigms of pain pathways, peripheral activation and peripheral and central sensitization, thereby linking and distinguishing visceral pain from somatic and neuropathic pain. Treatment options for visceral pain in palliative care encompass a wide variety of medical, interventional, and psychological approaches. With appropriate diagnostic measures and careful consideration of therapeutic options, most patients can achieve satisfactory relief.
APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Pancreatic cancer Sp proteins"

1

Bouvet, Michael, and Robert M. Hoffman. "In Vivo Imaging of Pancreatic Cancer with Fluorescent Proteins in Mouse Models." In Methods in Molecular Biology, 51–67. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-797-2_4.

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

Jain, Aditi, Samantha Z. Brown, Henry L. Thomsett, Eric Londin, and Jonathan R. Brody. "Evaluation of Post-transcriptional Gene Regulation in Pancreatic Cancer Cells: Studying RNA Binding Proteins and Their mRNA Targets." In Methods in Molecular Biology, 239–52. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8879-2_22.

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

"Sp-Like Proteins." In Encyclopedia of Cancer, 3487. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_5427.

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

Wang, Xueling, Rui Zhang, Lijuan Zhang, and Zibin Tian. "Glycated serum proteins: High in pancreatic cancer and low in preeclampsia." In Progress in Molecular Biology and Translational Science, 321–33. Elsevier, 2019. http://dx.doi.org/10.1016/bs.pmbts.2019.01.007.

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

Conference papers on the topic "Pancreatic cancer Sp proteins"

1

Chen, Ru, Sheng Pan, Anirban Maitra, Diane Simeone, David Dawson, and Teresa Brentnall. "Abstract 2866: Proteins associated with pancreatic cancer survival in patients with resectable pancreatic ductal adenocarcinoma." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2866.

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

Nkembo, Augustine T., Olufisayo Salako, Rosemary Poku, Tryphon Mazu, Byron Aguilar, Hernan Flores-Rozas, and Nazarius S. Lamango. "Abstract 2035: Targeting the hyperactive polyisoprenylated monomeric G-proteins functions in pancreatic cancer." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-2035.

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

Larson, Alaina C., Shelby M. Knoche, and Joyce C. Solheim. "Abstract 1658: Gemcitabine impacts expression of antigen presentation proteins by pancreatic cancer cells." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-1658.

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

Rocker, Jana D., Carlo Contreras, Lee W. Thompson, Russell E. Brown, Jack A. DiPalma, and Lewis K. Pannell. "Abstract B4: Depletion of antibodies and serum-derived proteins to facilitate LC-MS detection of pancreas-specific proteins in pancreatic ductal secretions." In Abstracts: AACR Special Conference on Pancreatic Cancer: Progress and Challenges; June 18-21, 2012; Lake Tahoe, NV. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.panca2012-b4.

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

Surcel, Alexandra, Eric S. Schiffhauer, Dustin G. Thomas, Qingfeng Zhu, Kathleen DiNapoli, Maik Herbig, Oliver Otto, et al. "Abstract 3154: Harnessing the adaptive potential of mechanoresponsive proteins to overwhelm pancreatic cancer dissemination and invasion." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3154.

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

Liss, Andrew S., Sabikun Nahar, Jennifer A. Mertz, Barbara Bryant, Robert J. Sims, Carlos Fernandez-del Castillo, Keith D. Lillemoe, Andrew L. Warshaw, and Sarah P. Thayer. "Abstract B107: BET proteins are key mediators of pancreatic cancer cell growth and its tumor microenvironment." In Abstracts: AACR Special Conference on Pancreatic Cancer: Innovations in Research and Treatment; May 18-21, 2014; New Orleans, LA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.panca2014-b107.

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

Lothe, Inger Marie Bowitz, Tone Ikdahl, Trond Buanes, Knut Jørgen Labori, Ole Petter Clausen, Gunhild M. Mælandsmo, Kjetil Boye, Tor Jacob Eide, and Elin Kure. "Abstract A50: KRAS mutational status and expressions of p53 and S100A4 proteins in pancreatic adenocarcinomas." In Abstracts: AACR Special Conference on Pancreatic Cancer: Progress and Challenges; June 18-21, 2012; Lake Tahoe, NV. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.panca2012-a50.

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

Sakaue, Takahiko, Hironori Koga, Masaru Fukahori, Yasuko Imamura, Toru Nakamura, Yoshinobu Okabe, Yu Ikezono, et al. "Abstract 3955: Expression of cancer stem cell-associated proteins in exosomes derived from ascites of patients with advanced pancreatic cancer." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3955.

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

Alewine, Christine, Rebekah Landsman, Michael Rudloff, Emily Kolyvas, Jinqiu Chen, and Ira Pastan. "Abstract B37: Mesothelin-targeted immunotoxin RG7787 (LMB-100) preferentially depletes secreted proteins and short-lived intracellular proteins to augment tumor cell killing by taxanes." In Abstracts: AACR Special Conference on Pancreatic Cancer: Advances in Science and Clinical Care; May 12-15, 2016; Orlando, FL. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.panca16-b37.

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

Chandana, Sreenivasa R., Cheryl Leece, Manisha Bhutani, and Barbara A. Conley. "Abstract 1657: HSP90 inhibition down regulates EGFR and its effector signaling proteins in pancreatic cancer cell lines." 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.am10-1657.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Pancreatic cancer Sp proteins' 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