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Results for “Integrin beta1”

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At least 19 recordsLinked to original sources
PubMed1992

The role of beta 1 integrin in spreading and myofibrillogenesis in neonatal rat cardiomyocytes in vitro.

The influence of the extracellular matrix (ECM) on cell behavior, myofibrillogenesis and cytoarchitecture was investigated in neonatal rat cardiac myocytes in vitro. Cell behavior was examined by analyzing cell spreading on different ECM components under a variety of experimental conditions. Area measurements were made on digitized images of cells grown for various time intervals on fibronectin (FN), laminin (LN), collagens I and III (C I+III), plastic, and bovine serum albumin (BSA). The amount of spreading was varied on the different matrices and was maximal on FN greater than LN greater than C I+III greater than plastic greater than BSA. Addition of anti-beta 1 integrin antibodies to myocytes cultured on FN, LN and C I+III blocked spreading outward on the substrates and altered normal myofibrillogenesis, especially on LN. Concomitantly, the integrin antibodies induced the formation of giant pseudopodial processes which protruded upward from the substrates. These pseudopods contained actin polygonal networks which exhibited a regular geometrical configuration. Effects of the ECM on cytoarchitecture was examined by analyzing the temporal and spatial patterns of fluorescence and immunogold labeling of cytoskeletal and integrin proteins as myocytes spread in culture. The first indication of sarcomeric patterns was the appearance at 4 hours of striations formed by lateral alignment of alpha-actinin aggregates into Z bands. At later times, vinculin at 8 hours and beta 1 integrin at 22 hours became co-localized with alpha-actinin at the Z bands and focal adhesions. These data indicate that ECM components influence myocyte spreading and that myofibril assembly and/or stability is associated with ECM-integrin-cytoskeleton associations.

Actinin↗
PubMed1992

Enhancement of CD3-induced activation of human intestinal intraepithelial lymphocytes by stimulation of the beta 7-containing integrin defined by HML-1 monoclonal antibody.

Intraepithelial lymphocytes (IEL) form a large population of T cells in close contact with the intestinal lumen and differ from lymphocytes in other lymphoid compartments by their predominant CD8+ phenotype and the strong expression of the recently characterized beta 7-containing integrin defined by the monoclonal antibody (mAb) HML-1. The aim of the present in vitro study was to investigate the possible role of the integrin defined by HML-1 in the activation of human IEL via the CD3-T cell receptor (TcR) pathway. The proliferative response of IEL to optimal concentrations of immobilized OKT3 was found to be similar to that of peripheral blood lymphocytes enriched in CD8+ cells. When co-immobilized with suboptimal concentrations of OKT3, antibodies directed against CD11a, CD29 and the beta 7-containing integrin defined by HML-1 exerted a strong synergistic effect on the proliferative response and on the expression of CD25 and CD71 antigens by human IEL. These data indicate that the CD3-TcR pathway is functional in human IEL and contrast with previous observations suggesting that the CD3-TcR pathway was difficult to elicit in human IEL. Furthermore, the present data show that the immune response of human IEL can be modulated via interactions between integrins expressed by IEL and their respective ligands in the mucosa and suggest that IEL's activation may depend on the level of expression of integrin ligands in the epithelium, particularly of the expression of the as yet unknown ligand for the IEL-specific integrin defined by HML-1.

Adult↗
PubMed1992

Beta 1 integrins isolated from embryonic chicken fibroblasts bind to monomers and polymers of type I collagen.

The avian integrin beta 1 subfamily consists of multiple alpha-beta subunit heterodimers. We employed two different physical states of type I collagen, monomers and fibrils, in the isolation and characterization of avian collagen integrins. Affinity chromatography showed that three integrins, tentatively designated alpha 155 beta 1 (band 1), alpha 5a beta 1, and alpha 3 beta 1 (band 2), bind fibrillar and monomeric collagen under physiological ionic conditions and require divalent cations for binding activity. Sodium chloride gradients (0-0.5 M) were used to assess the functional ability of the integrins to remain bound to the two forms of type I collagen. The results show that integrins elute from the two forms of collagen with distinct fractionation profiles. One integrin, alpha 155 beta 1, binds fibrillar collagen with relatively higher affinity than the other beta 1 receptors. This same avian integrin, alpha 155 beta 1, is immunoreactive with an antiserum (Hynes et al., 1989) raised against a peptide that corresponds to the entire alpha 5 cytoplasmic domain, and coincidently, part of the alpha 6 cytoplasmic domain (de Curtis et al., 1991). Cell biological studies employing double immunofluorescence show that integrins recognized by this antiserum co-localize with extracellular deposits of type I collagen.

Animals↗
PubMed1992

Regulation of T cell proliferation by anti-CD49d and anti-CD29 monoclonal antibodies.

The beta 1 integrin VLA-4 (alpha 4 beta 1, CD49d/CD29), which is expressed on a large subpopulation of peripheral blood T lymphocytes, functions as a receptor for the endothelial adhesion protein VCAM-1 and the extracellular matrix protein fibronectin. Previous studies showed that immobilized fibronectin enhanced anti-CD3 monoclonal antibody (mAb)-induced T cell proliferation through binding to the integrins VLA-4 and VLA-5 (alpha 5 beta 1, CD49e/CD29). We studied the ability of the anti-CD49d mAb L25 to potentiate proliferation. T cell proliferation was induced by subthreshold concentrations of anti-CD3 mAb (mAb OKT3) coimmobilized with mAb L25 but not with coimmobilized anti-CD29 (beta 1) mAb. Soluble anti-CD29 mAb inhibited the proliferation induced by coimmobilized mAb OKT3 and L25 but not proliferation induced by mAb OKT3 with PMA or coimmobilized anti-CD26 mAb.

Antigens, CD↗
PubMed1992

Immunohistochemical localization of beta 1-integrins in anterior cruciate and medial collateral ligaments of human and rabbit.

The integrins are a family of adhesion-mediating cell surface receptors that play critical roles in cell-extracellular matrix interactions and have been shown to be important in the healing response in several tissues. We have studied integrin expression in normal human and rabbit anterior cruciate (ACL) and medial collateral (MCL) ligaments of the knee as a preamble to studies of beta 1-integrin expression in healing ligaments. Histologic sections of human and rabbit ACL and MCL were probed for integrin expression utilizing integrin-specific monoclonal antibodies (mAbs) followed by immunoperoxidase detection. Staining of human specimens with mAbs revealed the presence of beta 1-, alpha 1-, and alpha 5-integrin chains on the tissue fibroblasts of both ACL and MCL, while staining of rabbit specimens with rabbit integrin-reactive monoclonals revealed the presence of beta 1- and alpha 5-integrin on these ligaments. Equivalent amounts of the integrins studied were present on normal ACL and MCL. We conclude that the rabbit is an appropriate model for analyzing the expression and functional role of integrins in ligament wound healing.

Animals↗
PubMed1992

Adhesion in skeletal muscle during regeneration.

Adhesion molecules were studied in regenerating skeletal muscle immunohistochemically and ultrastructurally after a standardized trauma. In normal muscle, extracellular matrix (ECM) protein tenascin was restricted to myotendinous junctions (MTJ), while the integrin beta 1-subunit was present also on the sarcolemma. After injury, tenascin increased on the outer surface of regenerating myofibers, where cellular fibronectin also accumulated. Later, tenascin concentrated at the tips of regenerating myofibers, where new MTJs were formed. The beta 1-subunit disappeared on necrotized myofibers and reappeared on regenerating fibers in a thicker layer. The regenerating myofibers were invested by a basal lamina, except for the growth cones at the distal ends, which were laminin-negative until the formation of MTJs occurred. These results indicate that regenerating muscle cells are attached to the ECM in a way that allows both growth of the muscle cells across the scar and their use before the regeneration is completed.

Animals↗
PubMed1992

Phenotypic expression of integrin membrane receptors on spontaneously proliferating CD8 cells in human T-lymphotropic virus type II (HTLV-II)-infected individuals.

Spontaneous lymphocyte proliferation in the absence of exogenous stimulators was examined in asymptomatic HTLV-II-seropositive (n = 12) and seronegative individuals (n = 16). Mean spontaneous lymphocytic proliferation significantly increased on day 8 postculture in HTLV-II-infected individuals (5762 +/- 899 cpm) compared with normal controls (2034 +/- 925 cpm, P less than 0.01). The proliferating cells in infected individuals were predominantly T cells; neither B cells nor monocytes demonstrated any proliferation. Phenotypic analysis of cultured cells from individuals with HTLV-II infection demonstrated differential expression of integrin molecules as defined by anti-CD29 and anti-S6F1 (42.8 +/- 4.2 and 39.6 +/- 5.9%, respectively) on CD8 cells, as compared with day 0 peripheral blood mononuclear cells (PBMC) from infected individuals (19.7 +/- 3.5 and 19.9 +/- 1.9%, respectively) or normal controls (12.9 +/- 3.1 and 11.5 +/- 2.5%, respectively; P less than 0.001 for both comparisons). These CD8+ cells did not express CD16 or CD11b. The culture supernatants derived from the spontaneously proliferating cells had significantly increased levels of sCD8 and sCD25 (765 +/- 180 and 1805 +/- 320 U/ml, respectively) compared with those from normal controls (222 +/- 120 and 305 +/- 90 U/ml, respectively; P less than 0.01). Furthermore, culture supernatants derived from spontaneously proliferating PBMC from HTLV-II-infected individuals had no detectable levels of HTLV antigen and did not stimulate proliferation of PBMC from normal donors. These results suggest that the spontaneous proliferation in HTLV-II asymptomatic carriers is due to expansion of CD8 cells expressing integrin receptors which may serve as costimulatory molecules for their activation.

Adult↗
PubMedDate not supplied

Invasion by cultured human follicular thyroid cancer correlates with increased beta 1 integrins and production of proteases.

A recognized model of tumor invasion requires cells to adhere to epithelial basement membrane and extracellular matrix components triggering release of proteases thus allowing cancer cells to invade the substrate. This adhesion is mediated by beta 1 integrins, a family of receptors to substrates such as collagen, laminin, and fibronectin. In order to study tumor invasion in follicular thyroid cancer (FTC), we used cell lines derived from a single patient's FTC primary tumor (FTC-133), neck lymph node metastases (FTC-236), and lung metastases (FTC-238). In vitro invasion as determined by the ability of the tumor cells to penetrate Matrigel was assessed by scanning electron microscopy. FTC-133 did not invade, FTC-236 was moderately invasive, and FTC-238 was highly invasive. Immunoprecipation with a monoclonal antibody to beta 1 integrin subunits and SDS-PAGE showed increased synthesis and flow cytometry showed increased expression of this subunit in FTC-236 and FTC-238 compared to FTC-133. Proteolytic activity was assessed by gelatin zymography. FTC-238 cell extract and conditioned media exhibited a more complex array of proteases consistent with activated type I collagenase and stromelysin compared to the less invasive clones, however 72 and 92 kd gelatinases consistent with type IV collagenases were present in the conditioned media from all three lines. In conclusion, in vitro invasion parallels in vivo metastasis by the source cells in the FTC-133/236/238 cell-lines. The ability to invade basement membrane preparation correlates with increased synthesis and expression of beta 1 integrins and activation of tumor proteases.

Adenocarcinoma↗
PubMed1991

Antibodies to different members of the beta 1 (CD29) integrins induce homotypic and heterotypic cellular aggregation.

Members of the beta 1 (CD29) integrin family are involved in cellular adhesion to extracellular matrix. However, there have been several reports of CD29 integrin participation in intercellular adhesion. For example, the treatment of the human T cell line Jurkat with antibodies to alpha 4 (CD49d) causes homotypic aggregation. The present report describes the induction of aggregation of Jurkat cells by antibodies to alpha 5 (CD49e) and to a lesser extent by antibodies to the common beta 1/CD29 chain of these integrins. The metabolic requirements for these aggregations are compared with that of the CD49d-induced process. The possible involvement of fibronectin in the cytoadhesion appears to be unlikely as (1) the aggregates form in the absence of plasma fibronectin; (2) antibodies to fibronectin do not inhibit the cell adhesion; and (3) exogenous fibronectin does not influence the process. One of the cognate partners involved in the CD49e-induced aggregation appears to be present on non-antibody-treated Jurkat cells as the cells are coincorporated into aggregates of anti-CD49e-stimulated cells. The adhesion does not appear to involve members of the CD2, CD3, CD4, or CD18 receptor groups. These results indicate that interaction with alpha 4, alpha 5 chain or the beta 1 chain of the CD29 integrins leads to the induction of intercellular adhesion. The possible biological significance of this process is discussed.

Animals↗
PubMed1992

Perturbation of beta 1 integrin-mediated adhesions results in altered somite cell shape and behavior.

Cell contact and adhesion between somites and the axial extracellular matrix (ECM) is likely to play a fundamental role in vertebrate development. In a preliminary report we showed that injection of the monoclonal antibody CSAT, which recognizes the avian beta 1 integrins, causes a lateral separation of both somites and segmental plate tissue from the embryonic axis (Drake and Little, 1991). In this study we addressed the cell biological response to CSAT injection, particularly the cell-ECM interactions involved in maintaining normal somite-axial relationships. A total of 150 stage 7-10 quail embryos have been injected with CSAT and then cultured for varying periods (1-30 hr). CSAT caused somitic cells to behave abnormally. Changes include, rounding-up, extensive blebbing, and formation of retraction fibers. A majority of separated somites were able to assume normal axial position with further time culture. Whether a somite subsequently aligned at the axis was dependent on the amount of CSAT injected and the postinjection culture period. Embryos in which somites remained separated from the axis after relatively long culture intervals (18-24 hr) displayed abnormal sclerotomal cell migrations. In no case did control injected embryos exhibit cellular alterations. Similarly, the injection of RGD-containing peptides had no detectable effect on somitogenesis or somite/segmental plate adhesion to the axis. On the basis of these data, we conclude that beta 1 integrins are necessary for normal somitic cell adhesions to the axis, but not somite segmentation and differentiation.

Amino Acid Sequence↗
PubMed1992

Induction of alpha v beta 3 integrin-mediated attachment to extracellular matrix in beta 1 integrin (CD29)-negative B cell lines.

beta 1 integrin containing complexes have been implicated as the primary adhesion structures in many lymphocyte extracellular matrix (ECM) interactions. However, many B lymphocytes lack surface expression of the beta 1 subunit, implying that this subpopulation of lymphoid cells must employ alternate adhesion structures if they are to maintain an interactive capacity with ECM. An examination of the adherence properties of the beta 1 integrin-negative B cell line JY indicated that these cells exhibit little or no basal adherence to any of the ECM components examined. However, these cells could be induced to adhere to the ECM components fibronectin, laminin, and vitronectin following treatment with PMA. Blocking studies with monoclonal antibodies indicated the alpha v beta 3 integrin complex was involved in the attachment to each of these ligands. However, the adherence to fibronectin displayed a complex pattern of inhibition suggesting the involvement of other ECM receptors. The utilization of the alpha v beta 3 complex was not unique to the JY cell line. Other B cell lines were observed to employ alpha v beta 3, and these lines similarly lacked expression of beta 1 integrin. These results indicate that alpha v beta 3 can act as a lymphoid ECM-adhesion structure which may provide an alternative means for lymphocytes to interact with ECM. Furthermore, these studies provide evidence for the presence of lymphoid-associated alpha v beta 3 integrins with regulatable activity, which contrasts with the constitutive adhesive potential of these complexes when present on other cell types.

Antibodies, Monoclonal↗
PubMed1991

ICAM-2 peptides mediate lymphocyte adhesion by binding to CD11a/CD18 and CD49d/CD29 integrins.

Three fifteen-amino-acid polypeptides designated peptides 1, 2 and 3 were synthesised as likely candidates for mimicking the role of ICAM-2 as a ligand. The ability of each peptide to bind lymphoid cells was tested. Peptide 2 largely mediated cell attachment of unstimulated cells and this binding was only marginally increased by stimulating the cells with phorbol dibutyrate (P(Bu)2). Peptide 3 mediated minimal spontaneous cell attachment, but this binding was significantly enhanced following P(Bu)2 stimulation. Peptide 1 had no effect on cell attachment with or without stimulation. The cell attachment to peptide 2 was both temperature- and cation-dependent. Studies using specific monoclonal antibodies showed that with unstimulated cells, anti-VLA-4 alpha(CD49d) or beta chain (CD29) antibodies (KD4-13 and 4B4) and anti-CD18 (1B4) each partially inhibited the cell binding. Monoclonal antibodies against CD54 (ICAM-1; 84H10 or LB2), MHC class 1 (W6/32) and control mouse IgG had no effect. When anti-CD29 and anti-CD18 monoclonal antibodies were used concurrently, there was almost complete inhibition of the cell attachment. These observations indicated that cell adhesion via ICAM-2 is mediated: (i) predominantly by peptide 2 in unstimulated and P(Bu)2-stimulated cells, and also, to some extent, by peptide 3 in P(Bu)2-stimulated cells and (ii) by binding to both CD11/CD18 and CD49d/CD29 integrins.

Amino Acid Sequence↗
PubMed1992

Are beta 1 integrins involved in Xenopus gastrulation?

The molecular basis of vertebrate gastrulation is poorly understood. Work on urodele amphibians has implicated beta 1-containing integrins, but the limited information available for Xenopus indicates otherwise: peptides containing the RGD sequence do not inhibit gastrulation and induction of cell spreading in presumptive ectodermal cells by activin is not accompanied by an increase in synthesis of integrin beta 1. Here we report that beta 1-containing integrins are, nevertheless, the principal fibronectin receptors in the Xenopus gastrula, although their cell surface levels are low. Antibodies recognizing the external domain of the molecule can, unlike peptides containing the RGD site, block gastrulation when introduced into the blastocoel. These results allow us to propose a model to explain the role of integrin beta 1 in Xenopus gastrulation.

Activins↗
PubMed1992

Laminin in the human embryo implantation: analogy to the invasion by malignant cells.

OBJECTIVE: To explore the possible similarities between the biochemical processes of embryo implantation and malignant invasion. DESIGN: The expression of a basement membrane (BM) glycoprotein laminin, a matrix binding cell surface receptor protein beta 1-integrin, and a BM collagen degrading metalloproteinase type IV collagenase, was studied in cultured human in vitro fertilized embryos. PATIENTS: Eight healthy women suffering from tubal infertility were participating in the IVF program in the Department of Obstetrics and Gynecology in University Hospital of Oulu. Twenty oocytes and 110 pre-embryos that were not transferred for the fertilizations were used in this study. MAIN OUTCOME MEASURES: Fibronectin, laminin, beta 1-integrin, and type IV collagenase immunoreactive proteins were studied in embryos by immunoperoxidase staining, and type IV collagen degrading activity was measured from the culture media of the embryos. RESULTS: Laminin and beta 1-integrin were expressed in the early human embryos before the time of implantation. Type IV collagen degrading activity and the 72 kd-type IV collagenase immunoreactive protein were expressed at the time of implantation. Laminin supported the expression of type IV collagenase. CONCLUSIONS: The expression of laminin, beta 1-integrin, and type IV collagenase in vitro are temporally in good correlation with the time of the implantation in vivo. Laminin and beta 1-integrin can relate to the attachment of the embryos to the uterine BM and type IV collagenase to the degradation of the BM collagen during the implantation. Laminin can augment the process locally.

Adult↗
PubMed1992

Morphoregulatory activities of E-cadherin and beta-1 integrins in colorectal tumour cells.

The cadherin family of adhesion molecules are prime mediators of cell-cell interactions while the integrins predominantly mediate cell-matrix and to a lesser extent cell-cell binding specificity. We have recently shown that a human colon carcinoma cell line (SW1222) organizes into glandular structures, with well defined polarity when cultured in three-dimensional type I collagen gel. The current study indicates that SW1222 cells display high levels of E-cadherin (E-cd, epithelial cadherin) by western blotting and immunohistochemical staining. A monoclonal antibody (HECD-1) specific for human E-cd blocks cell-cell adhesion (100%) and inhibits (up to 75%) the glandular differentiation of SW1222 cells growing in collagen gel. Furthermore the anti-beta 1 integrin monoclonal antibody (mAb13) inhibits the glandular differentiation of SW1222 cells (61%) and their cellular binding to type I collagen (60%). However, no significant inhibition of cell-cell adhesion was demonstrated using mAb13 nor the anti-carcinoembryonic antigen monoclonal antibody (PR3B10). These results are consistent with E-cd being a cell-cell adhesion molecule expressed by SW1222 cells. These data indicate that E-cd and beta 1 integrins mediate cell-cell and cell-collagen interactions required for the induction and maintenance of the glandular differentiation of colorectal tumour cells. Thus the down-regulation or loss of E-cd and beta 1 integrins seen in poorly differentiated colorectal tumours may represent one of the abnormalities underlying their progression towards an undifferentiated phenotype in vivo.

Blotting, Western↗
PubMed1992

Adhesion of rat glomerular epithelial cells to extracellular matrices: role of beta 1 integrins.

Glomerular epithelial cells (GEC) maintain glomerular permselectivity and are a target of immunological glomerular injury, which may lead to proliferation or detachment from extracellular matrix (ECM). We studied adhesion mechanisms in rat GEC in culture, focusing on adhesion molecules of the beta 1 integrin family. At early time points (1 hr after plating of cells into culture wells that had been pre-incubated with purified ECM proteins), adhesion of GEC to collagen I, collagen IV, laminin, and fibronectin was inhibited with anti-beta 1 integrin antibody. The peptide RGDS inhibited adhesion to fibronectin and laminin. Immunoprecipitation studies demonstrated the presence of alpha 2, alpha 3, and beta 1 integrins; the alpha 1, alpha 4, alpha 5, alpha 6, alpha v, and beta 3 subunits were undetectable. Adhesion to all ECM proteins was dependent on divalent cations, but the effects of individual cations varied among substrata. In rat GEC, alpha 2 beta 1 and/or alpha 3 beta 1 integrins appear to mediate adhesion to collagen I, collagen IV, and laminin. The alpha 3 beta 1 integrin is also the likely receptor for fibronectin, interacting through an RGD binding site. Furthermore, single integrins or combinations of integrins appear to have distinct ligand-binding functions that are differentially regulated by divalent cations. Characterization of GEC adhesion molecules may facilitate the understanding of mechanisms of glomerular development, and cell detachment or proliferation in immune glomerular injury.

Amino Acid Sequence↗