Integrin (the CSAT antigen): functionality requires oligomeric integrity.

Buck, Clayton A.; Shea, Elizabeth; Duggan, K; Horwitz, Alan E

doi:10.1083/jcb.103.6.2421

Cited by 154 publications

(82 citation statements)

References 28 publications

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“…This is consistent with in vitro studies which strongly suggest that one major determinant of vessel morphogenesis is cell-ECM interaction (Folkman and Haudenchild, 1980;Montesano et al, 1983;Kubota et al, 1988;Grant et al, 19891, and with the fact that the space between the splanchnic mesoderm and the endoderm is rich in ECM. Our immunolabeling studies (Drake et al, 1990) and the work of others Thiery, 1982, 1987;Krotoski et al, 1986) have shown that this area contains collagens, and in-its ability to perturb the binding function of these integrins (Buck et al, 1986). This antibody has been used successfully by several laboratories to analyze morphogenetic processes such as neural crest migration (Bronner-Fraser, 1986), myoblast movements laminin, and fibronectin.…”

Section: Vasculogenesis In Vitro and In Vivomentioning

confidence: 99%

“…Control antibodies included "G," a mouse monoclonal antibody, and purified nonimmune mouse IgGzb (the same subclass as CSAT). The monoclonal antibody "G' recognizes avian PI-integrins, but unlike CSAT, does not perturb ligand binding (Buck et al, 1986). This antibody has been used as a CSAT control in a number of studies (Bronner-Fraser, 1986;Jaffredo et al, 1988;.…”

Section: Antibody Preparationmentioning

confidence: 99%

“…Two control antibodies were used throughout this study: The first was the mouse monoclonal antibody, "G," that recognizes an extracellular epitope on chicken PI-integrins ( n = 26), but does not perturb integrin function (Buck et al, 1986). The second control was a nonimmune mouse IgG,,, the same subclass as CSAT ( n = 10).…”

Section: Control Antibodiesmentioning

confidence: 99%

“…These heterodimeric, membrane-spanning proteins are known to recognize an extensive list of ECM ligands. The mouse monoclonal antibody, CSAT, recognizes all known members of the p1 subfamily of avian integrins (Buck et al, 1986;Buck and Horwitz, 1987). Immunolocalization studies show that CSAT-reactive p,-integrins are present on the basal surface of most avian mesodermally derived epithelia (Krotoski et al, 1986); and the studies of Fujimoto and Singer (1988) described the distribution of P,-integrins on chicken aortic and capillary endothelial cells.…”

Section: Introductionmentioning

confidence: 99%

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Antibodies to β₁‐integrins cause alterations of aortic vasculogenesis, in vivo

Drake

Davis

Little

1992

Developmental Dynamics

121

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Vasculogenesis is the de novo formation of blood vessels from mesoderm. This process occurs very early in development and provides a convenient system for studying morphogenesis in higher vertebrates. The cell-extracellular matrix (ECM) interactions that occur during dorsal aortic vasculogenesis were examined using the monoclonal antibody, CSAT, a reagent known to neutralize the ligand-binding activity of avian p,-integrins. We injected CSAT into quail embryos during a period of active vasculogenesis (4-10 somites). The CSAT antibodies, but not controls, had a marked and reproducible effect on aortic vessel formation. Vasculogenesis appeared to be arrested at the stage when slender cord-like assemblies of angioblasts rearrange to form tubules. Indeed, aortic primordia near the site of CSAT injection did not form patent vessels.

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Section: Vasculogenesis In Vitro and In Vivomentioning

confidence: 99%

Section: Antibody Preparationmentioning

confidence: 99%

Section: Control Antibodiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Antibodies to β₁‐integrins cause alterations of aortic vasculogenesis, in vivo

Drake

Davis

Little

1992

Developmental Dynamics

121

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“…Ligand binding is dependent upon divalent cations (Gailit and Ruoslahti, 1988). The ligand recognised by integrins depends upon the particular cc-and ,Bsubunits within the complex, and requires both subunits (Buck et al, 1986). Endothelial integrins are involved in adhesion to extracellular matrix (ECM) molecules and in maintaining the integrity of the monolayer.…”

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confidence: 99%

Beta-1 Integrins mediate tumour cell adhesion to quiescent endothelial cells in vitro

Price

Coombe²,

Murray³

1996

Br J Cancer

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Summary Metastatic spread of some solid tumours is thought to depend upon the adhesion of tumour cells to the vascular endothelium followed by extravasation into surrounding tissues. We investigated the role of ,B1 integrins in the adhesion of the breast adenocarcinoma cell line MDA-MB-231 and the melanoma cell line RPMI-7951 to quiescent human umbilical vein endothelial cells (HUVEC) (Honn and Tang, 1992). These transmembrane glycoproteins are composed of two non-covalently associated subunits termed a and fi. There are at least 14 a-subunits (150-200 kDa) and eight P-subunits (90-210 kDa). The cxsubunits can associate with more than one type of f-unit, leading to a wide range of integrin dimers (Hynes, 1992;Albelda and Buck, 1990). Ligand binding is dependent upon divalent cations (Gailit and Ruoslahti, 1988). The ligand recognised by integrins depends upon the particular cc-and ,Bsubunits within the complex, and requires both subunits (Buck et al., 1986). Endothelial integrins are involved in adhesion to extracellular matrix (ECM) molecules and in maintaining the integrity of the monolayer. Endothelial cells express f,l, f3 and fl5 chains. The #1 integrins, which are expressed on a wide range of cell types, dimerise with acs 1-6 and thereby mediate cellular adhesion to laminin, collagen and fibronectin (Dejana, 1993). Integrins are also expressed on a variety of tumour cells, and changes in their expression may play a role in malignant progression and metastasis (Albelda, 1993;Juliano and Varner, 1993).In addition to mediating adhesion to extracellular matrix components, beta-l integrins have also been reported to play a role in tumour cell-endothelial cell adhesion. Lauri et al. Tumour cell/endothelial cell adhesion assay Tumour cell adhesion was measured as previously described (Price et al., 1995). Briefly, HUVEC were grown on 96-well gelatin-coated plates until confluent. Subconfluent tumour cells were suspended with 10 mM EDTA (pH 7.0) and incubated in this solution for 1 h at 37°C. The released tumour cells were washed three times in Medium 199 supplemented with 0.1% bovine serum albumin (BSA) (assay medium) and then fluorescence labelled by incubation in 40 ,ug ml-' carboxy-fluorescein diacetate (CFDA; Sigma) in the same medium for 30 min at 37°C. After three washes in assay medium, cells were resuspended to give 1 x 106 cells ml-', and 50 p1 of cell suspension was added to each well of washed HUVEC monolayers. The plates were incubated for 30 min at 37°C to allow adhesion before washing the wells three times with phosphate-buffered saline (PBS

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Apologies to John Donne

Goldsmith¹

1987

Arch Dermatol

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No molecule is an island, entire of itself; each molecule is a piece of the continent, a part of the main. If a cell be washed away by the sea, the body is less. Any cell's defect diminishes the whole, because it is involved in the whole.Life requires the effective interactions of tens of thousands of different molecules for reproduction, growth, movement, and adhesion. Adhesion occurs between cells of the organism, between cells and extracellular molecules within the organism, and between the organism and the external environment. Adhesion can be permanent, or relatively permanent, and at times must be a more transient phenomenon. The passage of epidermal cells through the epidermis during differentiation illustrates the importance of the control of adhesion in normally functioning skin. Blistering and hyperkeratotic diseases are examples of the importance of adhesion in dermatologic diseases. Adhesion of cells to the extra\x=req-\ cellular molecules in the dermis is of major functional importance to cells in the dermis.In Ecclesiastes 12:12, Koheleth admonishes, "Of making many books there is no end" (and anticipat¬ ing the needs of residents, "Much study is a weari¬ ness of the flesh"). For the modern biologist, the exhilaration of identifying and naming new mole¬ cules will not have an end for many years and will be the subject of many articles and books. In the December 1986 issue of the Journal of Cell Biology, there are two articles related to cell adhesion and dermal organization.Integrin is a molecular complex functioning in cell adhesion of chicken fibroblasts to extracellular matrix. The complex was previously called CSAT (cell substrate attachment complex), and I suspect that integrin, which has some zip to it, will be a name that will stick to this attachment complex. Molecules that are functionally similar to integrin exist on the membrane of mammalian cells, suggesting that what is found in chicks will have more general relevance. Fibroblast integrin interacts with the matrix mole¬ cules laminin and fibronectin. One of the molecular constituents of the integrin complex, band three, spans the cell membrane and would be an important link between the cytoskeleton of the fibroblast and the extracellular matrix. Integrin also binds to a cytoplasmic protein, talin, which connects cytoskele¬ ton to the cell membrane. Integrin is composed of three proteins, and the question asked by Buck et al1 was whether the entire three molecule complex was necessary for binding to fibronectin, laminin, and talin, or whether individual components of the com¬ plex could bind. Buck and coworkers developed a monoclonal antibody to band three of integrin and could dissociate integrin into band three and a mixture of the proteins from bands one and two. Neither of the fractions could bind by themselves to fibronectin, laminin, or talin. When the integrin was reconstituted, it was able to bind to the fibronectin, laminin, and talin. The authors' conclusion was that integrity of the complex was required for the func¬ tional in...

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Integrin (the CSAT antigen): functionality requires oligomeric integrity.

Cited by 154 publications

References 28 publications

Antibodies to β₁‐integrins cause alterations of aortic vasculogenesis, in vivo

Antibodies to β₁‐integrins cause alterations of aortic vasculogenesis, in vivo

Beta-1 Integrins mediate tumour cell adhesion to quiescent endothelial cells in vitro

Apologies to John Donne

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Integrin (the CSAT antigen): functionality requires oligomeric integrity.

Cited by 154 publications

References 28 publications

Antibodies to β1‐integrins cause alterations of aortic vasculogenesis, in vivo

Antibodies to β1‐integrins cause alterations of aortic vasculogenesis, in vivo

Beta-1 Integrins mediate tumour cell adhesion to quiescent endothelial cells in vitro

Apologies to John Donne

Contact Info

Product

Resources

About

Antibodies to β₁‐integrins cause alterations of aortic vasculogenesis, in vivo

Antibodies to β₁‐integrins cause alterations of aortic vasculogenesis, in vivo