Relevant bibliographies by topics / ΑVβ6 integrin

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

Academic literature on the topic 'ΑVβ6 integrin'

Author: Grafiati
Published: 22 February 2025

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Journal articles on the topic "ΑVβ6 integrin"

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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.

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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.
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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.

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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.
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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.

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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.
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Jackson, Terry, Stuart Clark, Stephen Berryman, Alison Burman, Stephanie Cambier, Dezhi Mu, Stephen Nishimura, and Andrew M. Q. King. "Integrin αvβ8 Functions as a Receptor for Foot-and-Mouth Disease Virus: Role of the β-Chain Cytodomain in Integrin-Mediated Infection." Journal of Virology 78, no. 9 (May 1, 2004): 4533–40. http://dx.doi.org/10.1128/jvi.78.9.4533-4540.2004.

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ABSTRACT Field isolates of foot-and-mouth disease virus (FMDV) have been shown to use three αv integrins, αvβ1, αvβ3, and αvβ6, as cellular receptors. Binding to the integrin is mediated by a highly conserved RGD motif located on a surface-exposed loop of VP1. The RGD tripeptide is recognized by several other members of the integrin family, which therefore have the potential to act as receptors for FMDV. Here we show that SW480 cells are made susceptible to FMDV following transfection with human β8 cDNA and expression of αvβ8 at the cell surface. The involvement of αvβ8 in infection was confirmed by showing that virus binding and infection of the transfected cells are inhibited by RGD-containing peptides and by function-blocking monoclonal antibodies specific for either the αvβ8 heterodimer or the αv chain. Similar results were obtained with a chimeric αvβ8 including the β6 cytodomain (αvβ8/6), showing that the β6 cytodomain can substitute efficiently for the corresponding region of β8. In contrast, virus binding to αvβ6 including the β8 cytodomain (αvβ6/8) was lower than that of the wild-type integrin, and this binding did not lead to infection. Further, the αvβ6 chimera was recognized poorly by antibodies specific for the ectodomain of αvβ6 and displayed a relaxed sequence-binding specificity relative to that of wild-type integrin. These data suggest that the β6 cytodomain is important for maintaining αvβ6 in a conformation required for productive infection by FMDV.
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Duque, Hernando, Michael LaRocco, William T. Golde, and Barry Baxt. "Interactions of Foot-and-Mouth Disease Virus with Soluble Bovine αVβ3 and αVβ6 Integrins." Journal of Virology 78, no. 18 (September 15, 2004): 9773–81. http://dx.doi.org/10.1128/jvi.78.18.9773-9781.2004.

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ABSTRACT At least four members of the integrin family of receptors, αVβ1, αVβ3, αVβ6, and αVβ8, have been identified as receptors for foot-and-mouth disease virus (FMDV) in vitro. Our investigators have recently shown that the efficiency of receptor usage appears to be related to the viral serotype and may be influenced by structural differences on the viral surface (H. Duque and B. Baxt, J. Virol. 77:2500-2511, 2003). To further examine these differences, we generated soluble αVβ3 and αVβ6 integrins. cDNA plasmids encoding the individual complete integrin αV, β3, and β6 subunits were used to amplify sequences encoding the subunits' signal peptide and ectodomain, resulting in subunits lacking transmembrane and cytoplasmic domains. COS-1 cells were transfected with plasmids encoding the soluble αV subunit and either the soluble β3 or β6 subunit and labeled with [35S]methionine-cysteine. Complete subunit heterodimeric integrins were secreted into the medium, as determined by radioimmunoprecipitation with specific monoclonal and polyclonal antibodies. For the examination of the integrins' biological activities, stable cell lines producing the soluble integrins were generated in HEK 293A cells. In the presence of divalent cations, soluble αVβ6 bound to representatives of type A or O viruses, immobilized on plastic dishes, and significantly inhibited viral replication, as determined by plaque reduction assays. In contrast, soluble αVβ3 was unable to bind to immobilized virus of either serotype; however, virus bound to the immobilized integrin, suggesting that FMDV binding to αVβ3 is a low-affinity interaction. In addition, soluble αVβ3 did not neutralize virus infectivity. Incubation of soluble αVβ6 with labeled type A12 or O1 resulted in a significant inhibition of virus adsorption to BHK cells, while soluble αVβ3 caused a low (20 to 30%), but consistent, inhibition of virus adsorption. Virus incubated with soluble αVβ6 had a lower sedimentation rate than native virus on sucrose density gradients, but the particles retained all of their structural proteins and still contained bound integrin and, therefore, were not exhibiting characteristics of a picornavirus A particle.
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Kossatz, Susanne, Ambros Johannes Beer, and Johannes Notni. "It’s Time to Shift the Paradigm: Translation and Clinical Application of Non-αvβ3 Integrin Targeting Radiopharmaceuticals." Cancers 13, no. 23 (November 26, 2021): 5958. http://dx.doi.org/10.3390/cancers13235958.

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For almost the entire period of the last two decades, translational research in the area of integrin-targeting radiopharmaceuticals was strongly focused on the subtype αvβ3, owing to its expression on endothelial cells and its well-established role as a biomarker for, and promoter of, angiogenesis. Despite a large number of translated tracers and clinical studies, a clinical value of αvβ3-integrin imaging could not be defined yet. The focus of research has, thus, been moving slowly but steadily towards other integrin subtypes which are involved in a large variety of tumorigenic pathways. Peptidic and non-peptidic radioligands for the integrins α5β1, αvβ6, αvβ8, α6β1, α6β4, α3β1, α4β1, and αMβ2 were first synthesized and characterized preclinically. Some of these compounds, targeting the subtypes αvβ6, αvβ8, and α6β1/β4, were subsequently translated into humans during the last few years. αvβ6-Integrin has arguably attracted most attention because it is expressed by some of the cancers with the worst prognosis (above all, pancreatic ductal adenocarcinoma), which substantiates a clinical need for the respective theranostic agents. The receptor furthermore represents a biomarker for malignancy and invasiveness of carcinomas, as well as for fibrotic diseases, such as idiopathic pulmonary fibrosis (IPF), and probably even for Sars-CoV-2 (COVID-19) related syndromes. Accordingly, the largest number of recent first-in-human applications has been reported for radiolabeled compounds targeting αvβ6-integrin. The results indicate a substantial clinical value, which might lead to a paradigm change and trigger the replacement of αvβ3 by αvβ6 as the most popular integrin in theranostics.
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Samanen, James, Zdenka Jonak, David Rieman, and Tian-Li Yue. "Vascular Indications for Integrin αv Antagonists." Current Pharmaceutical Design 3, no. 6 (December 1997): 545–84. http://dx.doi.org/10.2174/138161280306221010111710.

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Abstract: During early investigations into the biology associated with the platelet integrin αlIbβ3, monoclonal antibodies to αllbβ3 indicated that an αllbβ3-like integrin was expressed on endothelial cells, smooth muscle cells and on a variety of cancer cell lines. That integrin became known as the vitronectin receptor. It was shown to contain the same β3 subunit as αllbβ3, but it contained a different alpha subunit, named αv. Instead of a large family of β3 integrins, a large family of av integrins was discovered. To date, the family includes αvβI, αvβ3, αvβ5, αvβ6 and αvβ8. Two members of the family, αvβ3 and αvβ5, have received the most attention, showing potential in therapeutic targets as diverse as osteoporosis, restenosis and angiogenesis. This paper focuses on the potential vascular indications for av antagonists. It reviews the role of αvβ3 and αvβ5 as smooth muscle cell and endothelial cell adhesion receptors, as well as their capacity to mediate cell spreading and migration as signaling receptors. The current evidence for the role of αvβ3 and αvβ5 in restenosis and angiogenesis is reviewed. Endothelial cells, smooth muscle cells, and macrophages (mΦ) express either integrin, depending upon the cytokine that drives the migratory phenotype. Accessory membrane-bound molecules and matrix-degrading proteinases, as well as subcellular second messengers are reviewed. A model for the involvement of Integrin Associated Protein (IAP), and its ligation by thrombospondin is also proposed. A number of αv antagonists that inhibit cell adhesion to αvβ3 and αvβ5 have succeeded in proof of concept experiments in animal disease models. Nonpeptide av antagonists with high selectivity and adequate oral bioavailability have also been discovered. Thus, the field of av antagonists is poised to move into clinical development in the areas of restenosis, cancer, and ocular angiogenesis. Other areas that could blossom with potential for av antagonists include rheumatoid arthritis and atherosclerosis.
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Burman, Alison, Stuart Clark, Nicola G. A. Abrescia, Elizabeth E. Fry, David I. Stuart, and Terry Jackson. "Specificity of the VP1 GH Loop of Foot-and-Mouth Disease Virus for αv Integrins." Journal of Virology 80, no. 19 (October 1, 2006): 9798–810. http://dx.doi.org/10.1128/jvi.00577-06.

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ABSTRACT Foot-and-mouth disease virus (FMDV) can use a number of integrins as receptors to initiate infection. Attachment to the integrin is mediated by a highly conserved arginine-glycine-aspartic acid (RGD) tripeptide located on the GH loop of VP1. Other residues of this loop are also conserved and may contribute to integrin binding. In this study we have used a 17-mer peptide, whose sequence corresponds to the GH loop of VP1 of type O FMDV, as a competitor of integrin-mediated virus binding and infection. Alanine substitution through this peptide identified the leucines at the first and fourth positions following RGD (RGD+1 and RGD+4 sites) as key for inhibition of virus binding and infection mediated by αvβ6 or αvβ8 but not for inhibition of virus binding to αvβ3. We also show that FMDV peptides containing either methionine or arginine at the RGD+1 site, which reflects the natural sequence variation seen across the FMDV serotypes, are effective inhibitors for αvβ6. In contrast, although RGDM-containing peptides were effective for αvβ8, RGDR-containing peptides were not. These observations were confirmed by showing that a virus containing an RGDR motif uses αvβ8 less efficiently than αvβ6 as a receptor for infection. Finally, evidence is presented that shows αvβ3 to be a poor receptor for infection by type O FMDV. Taken together, our data suggest that the integrin binding loop of FMDV has most likely evolved for binding to αvβ6 with a higher affinity than to αvβ3 and αvβ8.
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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.

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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).
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Kossatz, Susanne, and Johannes Notni. "Frischer Wind für Integrine." Der Nuklearmediziner 44, no. 02 (June 2021): 152–59. http://dx.doi.org/10.1055/a-1395-0735.

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ZusammenfassungSelektive PET- oder SPECT- Radiopharmaka sind inzwischen nicht nur für αvβ3, sondern auch weitere der 24 verschiedenen Integrine verfügbar, zum Beispiel α5β1, αvβ6, αvβ8 und α6. Da diese unter anderem auch von verschiedenen Karzinomen und im Zuge von Fibrose exprimiert werden, ist die Vorstellung, dass Integrine nur als Zielstrukturen für die Bildgebung von Angiogenese in Betracht kommen, endgültig überholt. Die derzeit besten Aussichten auf eine breite klinische Anwendung, sowohl diagnostisch als auch therapeutisch, haben derzeit αvβ6-Integrin-Radiopharmaka, da αvβ6 von vielen malignen Krebsarten (v. a. Pankreas-, Plattenepithel-, Basalzell-, Lungen- und Colonkarzinom) überexprimiert wird.
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Dissertations / Theses on the topic "ΑVβ6 integrin"

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

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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.
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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.

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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.
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Hayward, Mary-Kate. "Mechanostimulation of integrin αvβ6 and fibronectin in DCIS myoepithelial cells." Thesis, Queen Mary, University of London, 2018. http://qmro.qmul.ac.uk/xmlui/handle/123456789/54057.

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Alterations to the tumour microenvironment is a common feature of many cancers, including breast cancer, and there is increasing evidence that alterations to the microenvironment, including; increased integrin expression, ECM deposition and protease activity, promote cancer progression. Most invasive breast cancers arise from a preinvasive stage, ductal carcinoma in situ (DCIS). Previous work in our laboratory has shown the microenvironment of DCIS is altered, such that myoepithelial cells (MECs) switch to a tumour-promoting phenotype, associated with upregulation of integrin αvβ6 and fibronectin (FN) expression. Mechanisms by which integrin αvβ6 and FN expression are regulated is unclear. We show DCIS progression into invasion is accompanied by an increase in MEC expression of integrin αvβ6 and periductal FN deposition, and their expression were associated in DCIS. These findings were modelled in isolated primary DCIS-MECs, primary normal MECs and MEC lines, with and without integrin αvβ6 expression, where integrin αvβ6-positive MECs upregulating FN expression. We identified integrin αvβ6-positive DCIS ducts were larger than integrin αvβ6-negative DCIS ducts, and mechanical stretching of primary normal MECs and a normal MEC line led to upregulation of integrin αvβ6 expression and FN deposition in a TGFβ-dependent manner. We further show upregulation of integrin αvβ6 and FN by MECs mediate TGFβ-dependent upregulation of MMP13 which promotes breast cancer cell invasion in vitro. These data show altered tissue mechanics in DCIS and MEC expression of integrin αvβ6 and FN deposition are linked, and implicate TGFβ in their activation. These findings suggest integrin αvβ6 and FN may be used as markers to stratify DCIS patients.
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Ylipalosaari, M. (Merja). "Matrix metalloproteinases (MMPs) in oral carcinomas." Doctoral thesis, University of Oulu, 2005. http://urn.fi/urn:isbn:9514277309.

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Abstract Matrix metalloproteinases, MMPs, are a family of enzymes capable of modulating connective tissue components. The expression of several MMPs is increased in oral squamous cell carcinomas (OSCCs). They are assumed to have an important role in the development and progression of OSCCs. However, the exact role and mechanism of the regulation of MMPs in malignant transformation are still largely unknown. In this study, tumour-associated trypsin-2 (TAT-2) was detected in OSCC tissue sections, and its role in MMP-2 and -9 regulation in carcinoma cells was evaluated. The TAT-2 gene was transfected into two different OSCC cell lines and one immortalized oral epithelial cell line. In TAT-2-transfected cells, MMP-9 activation increased OSCC cell invasion in chicken chorionallantoic membrane assay. Increased intravasation was prevented by tumour-associated trypsin inhibitor or specific gelatinase-inhibiting CTT-peptide. TAT-2 also converted MMP-1, -8, -13 and -3 into smaller molecular weight forms in vitro. However, TAT-2-transfected OSCC cells showed no conversion. TAT-2 was demonstrated to degrade powerfully type I collagen into small fragments in vitro. The cell surface receptor αvβ6 integrin is strongly up-regulated in OSCCs. By using β6-transfected OSCC cells, it was demonstrated that αvβ6 integrin down-regulates MMP-13 expression. However, this integrin did not regulate other collagenases or TIMP-1. β6-transfected cells invaded more efficiently through the basement membrane matrix, but their migration through type I collagen remained unchanged. MMP-8 expression was detected for the first time in head and neck squamous cell carcinoma (HNSCC) cell lines and corresponding cultured dermal and tumour fibroblasts. The localization of MMP-8 in HNSCC was determined by immunohistochemical stainings and in situ hybridization. MMP-8 production levels in carcinoma cells were faint and sporadic in HNSCCs sections. Ninety-two primary mobile tongue SCCs were subjected to MMP-8 immunohistochemical staining, and the staining results were compared to survival rates. MMP-8 was associated with improved disease-free survival in females but not in males.
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Dirheimer, Luca. "Ciblage de modèles cellulaires 3D par des agents de contrastes fluoresçant dans le proche infrarouge : application à la chirurgie guidée par la fluorescence des cancers de la tête et du cou." Electronic Thesis or Diss., Université de Lorraine, 2024. http://www.theses.fr/2024LORR0159.

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La résection chirurgicale constitue le traitement de première intention des cancers de la tête et du cou (HNSCC). La berge peropératoire est un facteur de pronostic majeur pour la survie globale des patients. Actuellement, il existe peu d’outils pour discriminer de manière fiable et en temps réel le tissu tumoral du tissu sain. La chirurgie guidée par la fluorescence (FGS) proche infrarouge (NIR) est une méthode d’imagerie utilisant le marquage fluorescent des tissus tumoraux afin de fournir une image de contraste augmentée. Le but de ces travaux est l’étude de la distribution de Quantum Dots (QDs) et d’IRDye-680, deux agents de contrastes fluorescents, couplés au peptide A20FMDV2 afin de cibler les cellules tumorales ORL au travers de l’intégrine αVβ6, surexprimée dans ces cancers. L’étude de l’accumulation et de la localisation de ces agents est réalisée sur modèle sphéroïde en monoculture et coculture (cellules cancéreuses de la langue/fibroblastes) afin de mieux représenter l’impact du microenvironnement tumoral sur la délivrance des agents de contraste. L’étude se poursuivra par le développement de nouveaux modèles sphéroïdes, mimant davantage le microenvironnement tumoral de la sphère ORL
Surgical resection is the first-line treatment for head and neck cancer (HNSCC). Theintraoperative margin is a major prognostic factor for the overall survival of patients. Currently, there are few tools to reliably discriminate tumor tissue from healthy tissue in real time. Near Infrared (NIR) Fluorescence Guided Surgery (FGS) is an imaging method using fluorescent labeling of tumor tissue to provide an enhanced contrast image. The aim of this work is to study the distribution of Quantum Dots (QDs) and IRDye-680, two fluorescent contrast agents, coupled to the A20FMDV2 peptide to target ENT tumor cells through the αVβ6 integrin, which is overexpressed in these cancers. The accumulation and localization of these agents was studied using spheroid models in monoculture and coculture (tongue cancer cells/fibroblasts) to better represent the impact of the tumor microenvironment on the delivery of these contrast agents. The study is continuing with the development of new spheroid models that better represent the tumor microenvironment found in the ENT sphere
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Nieberler, Markus [Verfasser], Klaus-Dietrich Akademischer Betreuer] Wolff, Andreas [Akademischer Betreuer] Kolk, and Henning [Akademischer Betreuer] [Bier. "Entwicklung und klinische Etablierung einer intraoperativen zytologischen Diagnostik der Knocheninfiltration bei Kopf-Hals-Karzinomen mit Charakterisierung von αvβ6 Integrin als Biomarker invasiver Karzinomzellen / Markus Peter Nieberler. Gutachter: Klaus-Dietrich Wolff ; Andreas Kolk ; Henning August Bier. Betreuer: Klaus-Dietrich Wolff." München : Universitätsbibliothek der TU München, 2014. http://d-nb.info/1058214454/34.

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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.

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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
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Elsharif, Amal A. M. "Functional Investigation of Dual αvβ3 and αllbβ3 Integrin Inhibition in Haematological and Solid Tumour Models." Thesis, University of Bradford, 2018. http://hdl.handle.net/10454/16883.

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Invasion and metastasis of cancer is the leading cause of increased mortality. In addition, haematological malignancies (leukaemia and lymphoma) are a significant cause of morbidity and mortality in both children and adults. Therefore, new treatments which will inhibit cancer progression are required. Integrin adhesion receptors, particularly the RGD-binding integrin subfamily comprising αvβ3, αvβ5, αvβ6, αvβ8, αllbβ3, α5β1, α8β1 and αvβ1 are related to progress and spread of cancer and poor prognosis. Because of the importance of integrin biology in the regulation of cancer dissemination, the integrin receptors are being utilised as targets to regulate cancer progression. The goal of this study was to develop a dual αvβ3/ αIIbβ3 expressing model for testing integrin antagonists. Expression of αv, αIIb, and β3 integrin subunits was characterised using immunofluorescence and flow cytometry in a panel of cell lines. After characterising the expression of αv, αIIb and β3 integrin subunits in inducible and natural expression models (K562 and MCF-7 cells respectively), functional tests for cellular adhesion, detachment and migration were determined. Phorbol 12-myristate 13-acetate (PMA)-treated K562 cells showed increased adhesion on fibrinogen compared to untreated cells. Adhesion of cancer cells (K562 ± PMA and MCF-7) to fibrinogen was inhibited and detachment was induced by the known β3 antagonists, cRGDfV and GR104453. Migration of cancer cells (K562 without PMA and MCF-7) was inhibited by combination of the known β3 antagonists. A panel of 12 novel small molecules developed in the ICT was investigated for cytotoxicity and activity in the validated function assays. ICT9055 was the most potent antagonist in inhibition of cell adhesion, migration, and inducing cell detachment. The data presented in this thesis had selected models and assays for evaluating small molecule integrin antagonists and identified ICT9055 as a promising molecule to develop for further preclinical evaluation.
The Libyan Embassy; Omer Al Mukhtar University, Faculty of Medical Technology, Derna, Libya.
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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.

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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.
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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.

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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
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Book chapters on the topic "ΑVβ6 integrin"

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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.

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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.

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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.

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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.

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Lin, Hung-Yun, Shaker A. Mousa, and Paul J. Davis. "Demonstration of the Receptor Site for Thyroid Hormone on Integrin αvβ3." In Methods in Molecular Biology, 61–65. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7902-8_7.

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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.

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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.

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Hong, Hao, and Weibo Cai. "Integrin αvβ3-Targeted Optical Imaging with Metal Oxide Nanomaterials: Focusing on Zinc Oxide." In Methods in Pharmacology and Toxicology, 123–34. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/7653_2015_60.

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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.

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Bürkle, Martin A., S. A. Pahernik, A. Sutter, A. Jonczyk, K. Meßmer, and M. Dellian. "Antiangiogenetische Therapie von Tumoren durch Inhibition des Integrins αvβ3 mit einem zyklischen Peptid." In Deutsche Gesellschaft für Chirurgie, 349–53. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-60133-0_67.

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Conference papers on the topic "ΑVβ6 integrin"

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Ballke, S., J. Löprich, T. Kaltenbacher, R. Rad, T. Groll, H. Notni, and K. Steiger. "αvβ6-Integrin Expression im endogenen Mausmodell: Ein Maus – Mensch Vergleich." In 67. Jahrestagung der Fachgruppe Pathologie der Deutschen Veterinärmedizinischen Gesellschaft. Georg Thieme Verlag KG, 2024. http://dx.doi.org/10.1055/s-0044-1787339.

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Decaris, Martin, Mahru An, Richard Ahn, Steve Ho, Vikram Rao, Erine Budi, Brenda Ho, et al. "Dual αVβ6/αVβ1 integrin inhibitor bexotegrast reduces fibrogenesis in pathological cell populations present in the fibrotic human lung." In ERS International Congress 2023 abstracts. European Respiratory Society, 2023. http://dx.doi.org/10.1183/13993003.congress-2023.oa899.

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Panda, Rupayana, Satya Narayan Sahu, and Jasaswini Tripathy. "Investigating the binding interactions of arg-gly-asp peptide with integrin αvβ3 and αvβ6: An In Silico study." In 2ND INTERNATIONAL CONFERENCE ON EMERGING SMART MATERIALS IN APPLIED CHEMISTRY (ESMAC-2021): ESMAC-2021. AIP Publishing, 2023. http://dx.doi.org/10.1063/5.0126508.

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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.

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Sutcliffe, Julie L. "Abstract IA-13: Molecularly targeted imaging and treatment via the integrin αvβ6." In Abstracts: AACR Virtual Special Conference on Pancreatic Cancer; September 29-30, 2020. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.panca20-ia-13.

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Vallath, Sabari, Emaunela Gadaletta, Claude Chelala, Aldo Scarpa, Ian R. Hart, Hemant M. Kocher, and John F. Marshall. "Abstract B42: Toward targeting integrin αvβ6 for the therapy of pancreatic cancer." 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-b42.

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Moore, Kate M., Gareth J. Thomas, Stephen W. Duffy, Jane Warwick, Rhian Gabe, Patrick Chou, Ian O. Ellis, et al. "Abstract B046: Therapeutic targeting of integrin αvβ6 in high-risk breast cancer." In Abstracts: AACR Special Conference on Advances in Breast Cancer Research: Genetics, Biology, and Clinical Applications - October 3-6, 2013; San Diego, CA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1557-3125.advbc-b046.

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Vallath, Sabari, Claire Reader, Jennifer Morton, Owen Sansom, Jeff Evans, Andrew Biankin, Simon T. Barry, Hemant Kocher, and John F. Marshall. "Abstract B53: The integrin αvβ6 is a promising therapeutic target for treating PDAC." 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-b53.

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Reader, Claire S., Jennifer P. Morton, Owen J. Sansom, and John F. Marshall. "Abstract A18: The integrin αvβ6 regulates PDAC cell growth and stromal cell behavior." 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-a18.

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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.

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