Relevant bibliographies by topics / Integrin alpha 5

Academic literature on the topic 'Integrin alpha 5'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Integrin alpha 5"

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Simon, E. E., C. H. Liu, M. Das, S. Nigam, T. J. Broekelmann, and J. A. McDonald. "Characterization of integrins in cultured human renal cortical tubule epithelial cells." American Journal of Physiology-Renal Physiology 267, no. 4 (October 1, 1994): F612—F623. http://dx.doi.org/10.1152/ajprenal.1994.267.4.f612.

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We have characterized the integrins present on cultured tubule epithelial cells from human renal cortexes, enriched for proximal cells, using fluorescence microscopy, immunoprecipitation, and cell adhesion assays. By immunofluorescence, the alpha 3-integrin subunit stained most intensely and was present on all cells predominantly at cell-cell contacts. The alpha 6-subunit was present on all cells in a pattern consistent with extracellular matrix contacts. The alpha 5-subunit was present on most cells in a cell-matrix contact pattern; alpha V-subunit was weakly positive and occasionally seen in cell-matrix contacts. The alpha 2-subunit was present on clusters of distal tubule cells, predominantly at cell-cell contacts. Immunoprecipitation revealed the predominant integrin to be alpha 3 beta 1 with some alpha 2 beta 1, presumably contributed by distal cells. The alpha 5 beta 1-, alpha 6 beta 1-, alpha 6 beta 4-, and alpha V beta 3-integrins, as well as trace amounts of alpha 1 beta 1-integrins, were also present. The alpha 4 beta 1-integrin was not detected. Initial attachment to fibronectin was mediated by alpha V beta 3- and alpha 5 beta 1-integrins; initial attachment to laminin was mediated by the alpha 6 beta 1- and alpha 3 beta 1- integrins and, in some preparations, by an unidentified integrin; and initial attachment to collagen type IV was mediated by alpha V beta 3-integrin and an unidentified beta 1-integrin. After extensively immunodepleting membrane extracts with anti-alpha 1, -alpha 2, -alpha 3, -alpha 4, -alpha 5, -alpha 6, and -alpha V antibodies, an anti-beta 1 antibody still precipitated an integrin. Its electrophoretic mobility differs from the laminin-binding alpha 7 beta 1-integrin. Thus we have identified many of the integrins on cortical tubule cells and their role in mediating initial attachment to extracellular matrix. However, the cell adhesion assays and immunoprecipitations suggest the presence of an unidentified beta 1-integrin that may mediate renal tubule cell attachment to laminin and collagen.
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Wu, C., A. J. Fields, B. A. Kapteijn, and J. A. McDonald. "The role of alpha 4 beta 1 integrin in cell motility and fibronectin matrix assembly." Journal of Cell Science 108, no. 2 (February 1, 1995): 821–29. http://dx.doi.org/10.1242/jcs.108.2.821.

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The alpha 4 beta 1 integrin has been suggested to play important roles in embryogenesis and pathogenesis of many diseases which involve both cell adhesion and cell migration. Previous studies using anti-alpha 4 beta 1 antibodies and fibronectin (Fn) fragments have suggested that alpha 4 beta 1 integrins may be involved in cell motility on Fn and vascular cell adhesion molecule-1 (VCAM-1). However, the cells used in these studies also express other Fn integrin receptors including alpha 5 beta 1 integrin, which is known to function in cell motility on Fn. To test whether alpha 4 beta 1 integrins mediate cell motility on Fn and VCAM-1 in the absence of alpha 5 beta 1 integrin, we expressed human alpha 4 integrin in a Chinese hamster ovary (CHO) cell line that is deficient in alpha 5 beta 1 integrin (CHO B2). The parental alpha 5 deficient CHO B2 cells were unable to adhere, spread or migrate on Fn, nor could they assemble a fibrillar Fn matrix. Expression of alpha 4 beta 1 integrin in the CHO B2 cells enabled the cells to adhere, spread and migrate on Fn and on VCAM-1 but not to assemble a fibrillar Fn matrix. The cellular processes mediated by the interaction of alpha 4 beta 1 with Fn or VCAM-1 were inhibited by the CS1 peptide derived from the major alpha 4 beta 1 binding site on Fn. These findings demonstrate that alpha 4 beta 1 integrins not only function as cell adhesion receptors but also as cell motility receptors for Fn and VCAM-1 independent of alpha 5 beta 1. Moreover, they reveal important functional differences between Fn binding integrins. The alpha 4-positive, alpha 5-negative CHO cells described in this report will be useful tools in studying the mechanism of molecular signalling during integrin mediated cellular processes.
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Muschler, J. L., and A. F. Horwitz. "Down-regulation of the chicken alpha 5 beta 1 integrin fibronectin receptor during development." Development 113, no. 1 (September 1, 1991): 327–37. http://dx.doi.org/10.1242/dev.113.1.327.

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We have characterized the diversity of the chicken beta 1 integrin family and studied the expression of individual receptors during development. The diversity of the beta 1 integrin family was investigated by affinity purifying the beta 1 integrins from a variety of adult and embryonic tissues. These purifications reveal the relative levels of expression and also the differential expression of the alpha subunits in those tissues. Monoclonal antibodies were generated against the prominent ‘band 1’ of the embryonic chicken integrins and used to characterize the expression of this alpha subunit in embryonic and adult tissues. This alpha subunit is shown to be the chicken homologue of human alpha 5 fibronectin receptor. The chicken alpha 5 beta 1 integrin is the most prominent beta 1 integrin in the embryo and is expressed on the majority of cell types through the day 17 stage. The distribution of this receptor in the embryo closely parallels the distribution of its ligand, fibronectin. In adult tissues, expression of this receptor is greatly diminished relative to the expression of other alpha subunits. The cell type distribution is highly restricted: limited primarily to the vasculature and to connective tissue regions. These studies reveal a prominent role for the alpha 5 beta 1 integrin in embryonic cell types and a down-regulation of this receptor on many cell types during development.
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Milner, R., and C. Ffrench-Constant. "A developmental analysis of oligodendroglial integrins in primary cells: changes in alpha v-associated beta subunits during differentiation." Development 120, no. 12 (December 1, 1994): 3497–506. http://dx.doi.org/10.1242/dev.120.12.3497.

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We have examined the expression of integrins on primary oligodendroglial cells during the differentiation of the proliferative oligodendrocyte precursor (O-2A progenitor) cell to the postmitotic oligodendrocyte. Cells of the oligodendrocyte lineage expressed a limited repertoire of integrins: alpha 6 beta 1 and alpha v integrins including alpha v beta 1, alpha v beta 3 and alpha v beta 5, as well as a potentially novel integrin alpha v beta 80 kDa. Integrin expression was developmentally regulated; during differentiation alpha v beta 1 was reduced and alpha v beta 5 upregulated. These results suggest that laminin and vitronectin are important extracellular matrix ligands for oligodendrocytes, and provide a rational explanation for previous observations that RGD peptides inhibit the expression of myelin-specific genes. They also suggest a simple model by which switching of integrin beta subunits might regulate differentiation. As chimeric beta 1 integrins with a beta 5 cytoplasmic domain support proliferation less well than normal beta 1 integrins (Pasqualini and Hemler (1994), J. Cell Biol. 125, 447–460) the switch from alpha v beta 1 to alpha v beta 5 might play a key instructive role in the cessation of proliferation and subsequent differentiation.
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Adams, J. C., and F. M. Watt. "Expression of beta 1, beta 3, beta 4, and beta 5 integrins by human epidermal keratinocytes and non-differentiating keratinocytes." Journal of Cell Biology 115, no. 3 (November 1, 1991): 829–41. http://dx.doi.org/10.1083/jcb.115.3.829.

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We have compared the adhesive properties and integrin expression profiles of cultured human epidermal keratinocytes and a strain of nondifferentiating keratinocytes (ndk). Both cell types adhered to fibronectin, laminin, and collagen types I and IV, but ndk adhered more rapidly and at lower coating concentrations of the proteins. Antibody blocking experiments showed that adhesion of both cell types to fibronectin was mediated by the alpha 5 beta 1 integrin and to laminin by alpha 3 beta 1 in synergy with alpha 2 beta 1. Keratinocytes adhered to collagen with alpha 2 beta 1, but an antibody to alpha 2 did not inhibit adhesion of ndk to collagen. Both cell types adhered to vitronectin by alpha v-containing integrins. Immunoprecipitation of surface-iodinated and metabolically labeled cells showed that in addition to alpha 2 beta 1, alpha 3 beta 1, and alpha 5 beta 1, both keratinocytes and ndk expressed alpha 6 beta 4 and alpha v beta 5. ndk expressed all these integrins at higher levels than normal keratinocytes. ndk, but not normal keratinocytes, expressed alpha v beta 1 and alpha v beta 3; they also expressed alpha 1 beta 1, an integrin that was not consistently detected on normal keratinocytes. Immunofluorescence experiments showed that in stratified cultures of normal keratinocytes integrin expression was confined to cells in the basal layer; terminally differentiating cells were unstained. In contrast, all cells in the ndk population were integrin positive. Our observations showed that the adhesive properties of ndk differ from normal keratinocytes and reflect differences in the type of integrins expressed, the level of expression and the distribution of integrins on the cell surface. ndk thus have a number of characteristics that distinguish them from normal basal keratinocytes.
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Jin, D. K., A. J. Fish, E. A. Wayner, M. Mauer, S. Setty, E. Tsilibary, and Y. Kim. "Distribution of integrin subunits in human diabetic kidneys." Journal of the American Society of Nephrology 7, no. 12 (December 1996): 2636–45. http://dx.doi.org/10.1681/asn.v7122636.

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Integrins are cell-surface protein receptors that participate in cell adhesion to multiple extracellular matrix ligands, and consist of alpha and beta chain heterodimers. This study examined altered integrin distribution in diabetic nephropathy by investigating 12 human diabetic kidney biopsies, which were compared with normal human kidney. Diabetic nephropathy is characterized by mesangial expansion and progressive thickening of the glomerular basement membrane. Based on morphometric studies of mesangial expansion, diabetic nephropathy was determined to be moderate or severe. Three different patterns (P) of altered intensity of integrin staining were observed. In the mesangial integrin P, the intensity of integrin subunit staining of mesangial cells (alpha 1, alpha 2, alpha 3, beta 1, alpha V, alpha V beta 5) was increased in moderate diabetic nephropathy and further increased in severe diabetic nephropathy. In the epithelial integrin P, integrin subunits localized to epithelial cells (alpha V, beta 3, alpha V beta 3, alpha V beta 5) were increased to the same extent in moderate and severe diabetic nephropathy. In the endothelial integrin P, integrin subunits localized to endothelial cells (alpha 3, alpha 5, alpha 6, beta 1) were increased in moderate diabetic nephropathy but returned to normal kidney staining intensity in severe diabetic nephropathy. From these observations, it was concluded that there is significant alteration in the expression of integrin subunits in diabetic nephropathy that is related to the severity of diabetic mesangial expansion. Additionally, the spectrum of integrin subunit alteration appears to be unique to individual glomerular cell types. Given the role of integrins in cell-surface interactions with extracellular matrix components, abnormalities in the expression of these molecules may be important in the pathogenesis of diabetic nephropathy.
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Whittaker, C. A., and D. W. DeSimone. "Integrin alpha subunit mRNAs are differentially expressed in early Xenopus embryos." Development 117, no. 4 (April 1, 1993): 1239–49. http://dx.doi.org/10.1242/dev.117.4.1239.

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Adhesion of cells to extracellular matrix proteins is mediated, in large part, by transmembrane receptors of the integrin family. The identification of specific integrins expressed in early embryos is an important first step to understanding the roles of these receptors in developmental processes. We have used polymerase chain reaction methods and degenerate oligodeoxynucleotide primers to identify and clone Xenopus integrin alpha subunits from neurula-stage (stage 17) cDNA. Partial cDNAs encoding integrin subunits alpha 2, alpha 3, alpha 4, alpha 5, alpha 6 and an alpha IIb-related subunit were cloned and used to investigate integrin mRNA expression in early embryos by RNase protection assay and whole-mount in situ hybridization methods. Considerable integrin diversity is apparent early in development with integrins alpha 2, alpha 3, alpha 4, alpha 5 and alpha 6 each expressed by the end of gastrulation. Both alpha 3 and alpha 5 are expressed as maternal mRNAs. Zygotic expression of alpha 2, alpha 3, alpha 4 and alpha 6 transcripts begins during gastrulation. Integrin alpha 5 is expressed at relatively high levels during cleavage, blastula and gastrula stages suggesting that it may represent the major integrin expressed in the early embryo. We demonstrated previously that integrin beta 1 protein synthesis remains constant following induction of stage 8 animal cap cells with activin (Smith, J. C., Symes, K., Hynes, R. O. and DeSimone, D. W. (1990) Development 108, 289–298.). Here we report that integrin alpha 3, alpha 4 and alpha 6 mRNA levels increase following induction with 10 U/ml activin-A whereas alpha 5, beta 1 and beta 3 mRNA levels remain unchanged. Whole-mount in situ hybridization reveals that alpha 3 mRNAs are expressed by cells of the involuting mesoderm in the dorsal lip region of early gastrulae. As gastrulation proceeds, alpha 3 expression is localized to a stripe of presumptive notochordal cells along the dorsal midline. In neurulae, alpha 3 mRNA is highly expressed in the notochord but becomes progressively more restricted to the caudalmost portion of this tissue as development proceeds from tailbud to tadpole stages. In addition, alpha 3 is expressed in the forebrain region of later stage embryos. These data suggest that integrin-mediated adhesion may be involved in the process of mesoderm involution at gastrulation and the organization of tissues during embryogenesis.
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Dalton, S. L., E. Scharf, R. Briesewitz, E. E. Marcantonio, and R. K. Assoian. "Cell adhesion to extracellular matrix regulates the life cycle of integrins." Molecular Biology of the Cell 6, no. 12 (December 1995): 1781–91. http://dx.doi.org/10.1091/mbc.6.12.1781.

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The expression of alpha 5 beta 1 integrin on the surface of fibroblasts requires adhesion to substratum. We have examined the basis for this adhesion-dependent surface expression by comparing the life cycle of integrins in parallel cultures of adherent and nonadherent cells. Results of biosynthetic labeling experiments in NRK fibroblasts showed that the synthesis and biosynthetic processing of the beta 1 integrin subunit proceed in the absence of cell attachment; however, when examining the behavior of preexisting cell surface integrins, we observed that the alpha beta 1 integrins are internalized and degraded when adhesion to substratum is blocked. A kinetic analysis of integrin internalization in cycloheximide-treated NRK cells showed that each of the fibroblast integrins we examined (in both the beta 1 and beta 3 families) are lost from the cell surface after detachment from substratum. Thus, the default integrin life cycle in fibroblasts involves continuous synthesis, processing, transport to the cell surface, and internalization/degradation. Interestingly, studies with NIH-3T3 cells expressing alpha 1 beta 1 integrin showed that the loss of cell-surface alpha 5 beta 1 integrin is blocked by adhesion of cells to dishes coated with type IV collagen (a ligand for alpha 1 beta 1 integrin) as well as fibronectin. Similarly, adhesion of these cells to dishes coated with type IV collagen stabilizes the surface expression of alpha 5 beta 1 as well as alpha 1 beta 1 integrin. We propose that the adhesion of fibroblasts to extracellular matrix protein alters the integrin life cycle and permits retention of these proteins at the cell surface where they can play important roles in transmitting adhesion-dependent signals.
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Hynes, R. O., E. E. Marcantonio, M. A. Stepp, L. A. Urry, and G. H. Yee. "Integrin heterodimer and receptor complexity in avian and mammalian cells." Journal of Cell Biology 109, no. 1 (July 1, 1989): 409–20. http://dx.doi.org/10.1083/jcb.109.1.409.

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We report data showing that the integrin receptor complex in chickens contains several discrete heterodimers all sharing the beta 1-integrin subunit combined separately with different alpha-subunits. Using antisera to synthetic peptides based on cDNA sequences of chicken and human alpha-integrin subunits to analyze the integrin complement of avian and mammalian cells, we show that band 2 of the chicken integrin complex contains alpha-subunits related to both alpha 3- and alpha 5-subunits of human integrins. alpha 3 beta 1 and alpha 5 beta 1 have both previously been shown in human cells to be fibronectin receptors and alpha 3 beta 1 can also act as a receptor for laminin and collagen. We also provide evidence for the presence, in band 1 of the chicken integrin complex, of a third integrin alpha-subunit which is also alpha 5 related. This integrin subunit exists in a separate heterodimer complex with beta 1 and binds to fibronectin-affinity columns. These results provide explanations for published data showing that the avian integrin complex contains receptor activity for a variety of extracellular matrix proteins. We conclude that the chicken integrin complex comprises a set of beta 1-integrin heterodimers equivalent to the human VLA antigens and includes at least two fibronectin receptors. Finally, we show that chicken embryo fibroblasts also contain a beta 3-class integrin related to the RGD receptors defined in various human cells.
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Pilewski, J. M., J. D. Latoche, S. M. Arcasoy, and S. M. Albelda. "Expression of integrin cell adhesion receptors during human airway epithelial repair in vivo." American Journal of Physiology-Lung Cellular and Molecular Physiology 273, no. 1 (July 1, 1997): L256—L263. http://dx.doi.org/10.1152/ajplung.1997.273.1.l256.

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Airway epithelium is subject to injury during inflammation and exposure to a variety of inhaled and infectious agents. Little is known about the expression of integrins during human airway epithelial regeneration and differentiation after injury. We therefore characterized integrin subunit expression after mechanical injury in an in vivo xenograft model of human bronchial epithelium. On the migrating cells at the edges of surface epithelial wounds, there was increased expression of the alpha v-, beta 5-, beta 6-, and alpha 5-integrin subunits. During the later phase of repair, the increased expression of alpha v-, beta 5-, and beta 6-subunits persisted, but the expression of the beta 8-subunits was restricted to basal cells. In addition, there was a redistribution of the alpha 2- and alpha 6-collagen/laminin-binding integrins to suprabasal epithelial layers. There was no expression of the beta 3- or alpha 4-integrin subunit on reparative epithelium. A similar upregulation of alpha v-, beta 5-, and beta 6-integrin receptor subunits was observed in areas of undifferentiated airway from cystic fibrosis patients. Injured epithelium was found to be significantly more susceptible to gene transfer with a recombinant adenovirus, suggesting that the increased integrin expression has implications for the acquisition of adenovirus infections and for lung-directed gene therapy.
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Dissertations / Theses on the topic "Integrin alpha 5"

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Zimmermann, Dunja. "Der Einfluss cyclischer RGD-Peptide auf die Wechselwirkung Fibronectin-Integrin [alpha]5[beta]1[alpha 5 beta 1]." [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=970414277.

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Künneken, Kerstin. "Rekombinante Mini-Laminin-5-Proteine zur Charakterisierung der 3 1-Integrin-Bindung [Alpha-3-Beta-1-Integrin-Bindung]." [S.l. : s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=967391334.

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Nguyen, Beth P. "Integrin alpha 6 beta 4 ligation to laminin 5 and phosphoinositide 3-OH kinase define differences in alpha 3 beta 1-laminin 5 and alpha 2 beta 1-collagen spreading : implications for epidermal wound repair /." Thesis, Connect to this title online; UW restricted, 1999. http://hdl.handle.net/1773/9286.

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Siller-Jackson, Arlene J. "Connexin 43 hemichannels are regulated by mechanical stress and [alpha]5 integrin in osteocyte-like cells : a dissertation /." San Antonio : UTHSC, 2007. http://proquest.umi.com/pqdweb?did=1400962241&sid=1&Fmt=2&clientId=70986&RQT=309&VName=PQD.

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Mysinger, Cynthia. "CAR is not required for adenovirus infection: Integrin alpha v beta 5 mediates binding to CAR-negative cells." Diss., Search in ProQuest Dissertations & Theses. UC Only, 2009. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3359557.

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Vignoud, Lucile. "Étude du rôle des motifs NPXY dans la fonction de l'intégrine alpha 5/beta 1." Grenoble 1, 1996. http://www.theses.fr/1996GRE10274.

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Le travail presente concerne l'etude du role joue par les deux motifs peptidiques npxy localises dans le domaine cytoplasmique de la sous-unite beta 1 des integrines. Par analogie avec le recepteur des ldl, ces deux motifs etaient assimiles au signal d'internalisation npxy permettant une association au complexe d'adaptines ha-2 et une internalisation dependante des puits a clathrine. En generant des lignees stables exprimant des integrines a sous-unite beta 1 mutees, nous avons montre que contrairement a d'autres recepteurs, les motifs npxy n'intervenaient pas dans l'internalisation de l'integrine alpha 5/beta 1. En revanche, nous avons observe que chacun des motifs npxy etait indispensable a l'assemblage des adherences focales. L'affinite pour le ligand extracellulaire n'etant pas affectee par les mutations realisees, nos resultats attribuent aux deux motifs npxy un role en tant que sites d'interaction, ou permettant la formation de sites d'interaction, avec une ou plusieurs proteines cytoplasmiques necessaires a l'assemblage des adherences focales. L'analyse de la fixation in vitro de la taline sur les chaines beta 1 mutees au niveau des sequences npxy, indique que cette proteine, pourtant necessaire a l'etablissement des adherences focales, n'est pas la proteine cible qui interagit avec les motifs npxy des integrines pour permettre leur recrutement au sein de ces adherences. La taline n'est pas suffisante a elle seule pour permettre l'assemblage des adherences focales. L'identite des proteines interagissant avec la sous-unite beta 1 de maniere dependante des motifs npxy, reste a determiner. L'immunoprecipitation des integrines a sous-unite beta 1 humaine dans des conditions menagees, a mis en evidence leur association avec diverses proteines cellulaires, controlee par le premier motif npxy (tyr 783). Ces proteines, non identifiees, pourraient jouer un role essentiel dans l'organisation des adherences focales, dependante du premier motif npxy de la sous-unite beta 1 des integrines, et/ou dans la signalisation cellulaire
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Parks, William. "Force activation of I domain containing and lacking integrins on live cells." Thesis, Georgia Institute of Technology, 2010. http://hdl.handle.net/1853/42695.

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Cellular adhesion plays a crucial role in the biological function of cells, allowing them to communicate and signal, as well as physically anchor, by enabling them to adhere to either other cells or the extra cellular matrix (ECM). This process is regulated by several factors including intrinsic bond kinetics, internal cellular signaling, environment, force exerted on the bond, and force history of the bond. Concerning the force and force history dependence, the observation of catch bonds in integrin binding has asked as more questions than it has answered. To explore the force and force history dependence this process, each bond was loaded to a peak force before relaxing to a much lower force that was held for the duration of the measurement. Two different integrins were studied, both of which have in previous works exhibited a catch bond. Furthermore, the effects of different metal ion conditions and an allosteric antagonist were also studied to elucidate the conformational effects on force priming of integrin. What was observed was that I domain, or αA domain, possessing integrin, whether tested against its more active or less active binding state, changed very little in terms of off rate once the priming force was applied. However in the I domain, or αA domain, lacking integrin, the observed off rate changed as well. It seems that force priming is capable of causing integrin to bind in a stronger manner regardless of the other conditions used to either activate or inhibit binding. However the way in which the binding is strengthened depends on the receptors structure.
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Quinn, Jeffrey Alan. "Requirement of integrin [alpha]5[beta]1 and tyrosine phosphorylation of SHC for prohb-EGF release by GPR30, a seven transmembrane receptor for estrogen /." View online ; access limited to URI, 2006. http://0-wwwlib.umi.com.helin.uri.edu/dissertations/dlnow/3225328.

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Kaufmann, Martin. "Lipid Bilayers Supported by Multi-Stimuli Responsive Polymers." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2013. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-106231.

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Artificial lipid bilayers formed on solid surface supports are widespread model systems to study physical, chemical, as well as biological aspects of cell membranes and fundamental interfacial interactions. The approach to use a thin polymer film representing a cushion for lipid bilayers prevents incorporated membrane proteins from pinning to the support and mimics the native environment of a lipid bilayer in certain aspects of the extracellular matrix and intracellular structures. A key component for cell anchorage to extracellular fibronectin is the transmembrane adhesion receptor alpha(5)beta(1) integrin. Its transport dynamics and clustering behavior plays a major role in the assembly of focal adhesions, which mediate mechanical forces and biochemical signals of cells with their surrounding. The system investigated herein is envisioned to use extrinsically controlled stimuli-responsive polymer cushions to tune the frictional drag between polymer cushion and mobile membranes with incorporated integrins to actively regulate lipid membrane characteristics. To attain this goal, a temperature- and pH-responsive polymer based on poly(N-isopropylacrylamide) copolymers containing varying amounts of carboxyl-group-terminated comonomers at different aliphatic spacer lengths (PNIPAAm-co-carboxyAAM) was surface-grafted to a poly(glycidyl methacrylate) anchorage layer. The swelling transitions were characterized using atomic force microscopy, ellipsometry and quartz crystal microbalance with dissipation monitoring (QCM-D) and found to be tunable over a wide range of temperature and pH. In agreement with the behavior of the polymers in solution, longer alkyl spacers decreased the phase transition temperature T(P) and higher contents of carboxylic acid terminated comonomers increased T(P) at alkaline conditions and decreased T(P) at acidic conditions. Remarkably, the point where the degree of carboxyl group deprotonation balances the T(P)-lowering effect of the alkyl spacer was distinctive for each alkyl spacer length. These findings illustrate how the local and global balance of hydrophilic and hydrophobic interactions along the copolymer chain allows to adjust the swelling transition to temperatures below, comparable, or above those observed for PNIPAAm homopolymers. Additionally, it could be shown that surface-grafting leads to a decrease in T(P) for PNIPAAm homopolymers (7°C) and copolymers (5°C - 10°C). The main reason is the increase in local polymer concentration of the swollen film constrained by dense surface anchorage in comparison to the behavior of dilute free chains in solution. In accordance with the Flory-Huggins theory, T(P) decreases with increasing concentration up to the critical concentration. Biological functionalization of the PNIPAAm-co-carboxyAAm thin films was demonstrated for the cell adhesion ligand peptide cRGD via carbodiimide chemistry to mimic extracellular binding sites for the cell adhesion receptors integrin. The outcome of QCM-D measurements of cRGD-functionalized surfaces showed a maintained stimuli-responsiveness with slight reduction in T(P). A drying/rehydration procedure of a 9:1 lipid mixture of the cationic lipid dioleoyl-trimethylammoniumpropane (DOTAP) and the zwitterionic dioleoyl-phosphatidylcholine (DOPC) was utilized to form lipid bilayer membranes on PNIPAAm-co-carboxyAAM cushions. Fluorescence recovery after photobleaching (FRAP) revealed that lipid mobility was distinctively higher (6.3 - 9.6) µm2 s-1 in comparison to solid glass support ((3.0 - 5.9) µm2 s-1). In contradiction to the initial expectations, modulation of temperature and pH led to poor variations in lipid mobility that did not correlate with the PNIPAAm cushion swelling state. The results suggested a weak coupling of the lipid bilayer with PNIPAAm polymer cushions that can be slightly tuned by electrostatic interactions. The transmembrane adhesion receptor alpha(5)beta(1) integrin was reconstituted into liposomes consisting of DOPC/sphingomyelin/cholesterol 2:2:1 for the formation of polymer cushioned bilayers. PNIPAAm- co-carboxyAAM and maleic acid (MA) copolymers were used as cushions, both with the option for cRGD functionalization. On the MA copolymer cushions, fusion of proteoliposomes resulted in supported bilayers with mobile lipids as confirmed by FRAP. However, incorporated integrins were immobile. In an attempt to explain this observation, the medium-sized cytoplasmic integrin domain was accounted to hamper the movement by steric interactions with the underlying polymer chains in conjunction with electrostatic interactions of the cationic cytoplasmic domain with the oppositely charged MA copolymer. On the PNIPAAm-co-carboxyAAM cushion only a drying/rehydration procedure lead to bilayer formation. However, again the integrins were immobile, presumably due to the harsh treatment during preparation. Nevertheless, the results of the investigated set of PNIPAAm copolymer films suggest their application as temperature- and pH-responsive switchable layers to control interfacial phenomena in bio-systems at different physiological conditions. The PNIPAAm-co-carboxyAAm cushioned bilayer system represents a promising step towards extrinsically controlled membrane – substrate interactions.
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Roger, Patrica. "Role des integrines et des asialogangliosides dans les mecanismes d'adherence bacterienne a l'epithelium respiratoire." Reims, 1998. http://www.theses.fr/1998REIMM201.

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Book chapters on the topic "Integrin alpha 5"

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Barrett, Audrey, and Fred Galloway. "The Nonprofit Ethics Survey." In Online Instruments, Data Collection, and Electronic Measurements, 57–75. IGI Global, 2013. http://dx.doi.org/10.4018/978-1-4666-2172-5.ch004.

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The Nonprofit Ethics Survey serves as the only empirically supported survey instrument specifically designed for nonprofit organizations to assess their ethical culture. Development of the instrument occurred through the use of principal components analysis conducted on a sample of 530 nonprofit affiliates. The results of the analysis yielded six parsimonious scales integral to assessing nonprofit ethics. To evaluate the internal reliability of each scale a measure of Cronbach’s Alpha was also calculated. The alpha coefficients ranged from 0.86 - 0.94, indicating the survey provides a reliable means of measuring the constructs integral to assessing organizational ethics in nonprofit agencies. The creation of a statistically sound instrument designed for use with nonprofit organizations ensures that nonprofit leaders have the needed tools to accurately self-assess.
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Conference papers on the topic "Integrin alpha 5"

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Hong, Ji Hyung, Jeong-Hun Lee, Na Ra Yoon, Suk Hee Hong, and Yoon Ho Ko. "Abstract 2340: Integrin subunit alpha 5: Potential prognostic biomarker in lung adenocarcinoma." 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.am2018-2340.

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Larzabal, Leyre, Miriam Redrado, Arrate Lopez de Aberasturi, Paloma Rueda, Maria J. Rodriguez, Lissette Lopez, Luis Montuenga, and Alfonso Calvo. "Abstract 2696: TMPRSS4 regulates levels of integrin alpha-5 in NSCLC through miR-205 activity." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-2696.

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Kuninty, PR, R. Bansal, TN Satav, MF Bijlsma, HV Laarhoven, A. Östman, and J. Prakash. "PO-009 A novel integrin alpha 5 binding peptide potentiates effects of chemotherapy in pancreatic cancer." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.544.

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O'Neill, Kealan, Austin Reece, Abdallah Alzoubi, Michie Toba, Masahiko Oka, Ivan F. McMurtry, and Karen A. Fagan. "Blockade Of Either Alpha-5 And Beta-1 Integrin Inhibits Pulmonary Arterial Contraction: Possible Role In PAH." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4829.

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Connell, Brendan, Pavel Kopach, Wenying Ren, Raghav Joshi, Steven Naber, and Paul Mathew. "Abstract 114: Aberrant integrin alpha v and alpha 5 expression patterns in prostate adenocarcinomas and bone-metastases from prostate cancer are consistent with a bone-colonizing phenotype." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-114.

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Connell, Brendan, Pavel Kopach, Wenying Ren, Raghav Joshi, Steven Naber, and Paul Mathew. "Abstract 114: Aberrant integrin alpha v and alpha 5 expression patterns in prostate adenocarcinomas and bone-metastases from prostate cancer are consistent with a bone-colonizing phenotype." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-114.

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Ren, Wenying, Raghav Joshi, and Paul Mathew. "Abstract 5499: A potent BH3 mimetic targeting BCL-XLinduces apoptosis regulated by PTEN loss and integrin alpha 5 in prostate cancer cells." 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.am2018-5499.

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Zarogiannis, Sotirios G., Aristotelis S. Filippidis, Solana Fernandez, Asta Jurkuvenaite, Namasivayam Ambalavanan, Andrei Stanishevsky, Yogesh K. Vohra, and Sadis Matalon. "Short-Term Exposure Of Clara-Like Human Epithelial Cells (H441) To Ultrafine Nano-TiO2 Impairs Migration And Adhesion Via Integrin Alpha-5 Down-Regulation." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1192.

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Ren, Wenying, Raghav Joshi, and Paul Mathew. "Abstract 5091: Synergistic apoptosis induced by combined PI3 kinase and bcl-xl inhibition in genotypic subsets of prostate cancer is attenuated by a feedback signaling loop via the alpha-5 integrin." 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.am2016-5091.

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Joshi, Raghav, Wenying Ren, and Paul Mathew. "Abstract 1902: The comparative superiority of a bispecific antibody targeting alpha v and alpha 5 integrins is uniquely characterized by induced degradation of integrins." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-1902.

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Reports on the topic "Integrin alpha 5"

1

Turner-Haenssen, Keneshia. Role of Integrin Alpha 5 in ErbB2-Mediated Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 2009. http://dx.doi.org/10.21236/ada513289.

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