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Journal ArticleDOI

Integrins: a family of cell surface receptors.

Richard O. Hynes
- 27 Feb 1987 - 
- Vol. 48, Iss: 4, pp 549-554
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TLDR
This brief review of sequence data from embryogenesis, thrombosis, and lymphocyte help and killing is summarized and attempts to clarify the relationships among the members of this family of cell surface receptors.
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This article is published in Cell.The article was published on 1987-02-27. It has received 4229 citations till now. The article focuses on the topics: Integrin & Cell adhesion.

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Specific interaction between gangliotriaosylceramide (Gg3) and sialosyllactosylceramide (GM3) as a basis for specific cellular recognition between lymphoma and melanoma cells.

TL;DR: A specific interaction between AA12 cells and B16 cells based on Gg3-GM3 interaction is reported, suggesting a possible role of glycosphingolipids in defining the specificity of cell-cell interactions.
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Interactions of a neuronal cell line (PC12) with laminin, collagen IV, and fibronectin: identification of integrin-related glycoproteins involved in attachment and process outgrowth.

TL;DR: The interactions of a neuron-like rat pheochromocytoma cell line, PC12, with ECM protein-coated substrates are studied and three prominent cell surface glycoproteins of 120, 140, and 180 kD under nonreducing conditions are identified.
Journal ArticleDOI

Cell surface distribution of fibronectin and vitronectin receptors depends on substrate composition and extracellular matrix accumulation.

TL;DR: The accumulation of FNR at extracellular matrix contacts implies that this receptor might also function in the process of cellular migration along fibronectin-containing matrix cables, and that FNR might also recognize substrates coated with purified ligands.
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Distinct functions of integrin alpha and beta subunit cytoplasmic domains in cell spreading and formation of focal adhesions

TL;DR: The integrin beta 3 subunit cytoplasmic domain is necessary and sufficient for initiation of cell spreading and focal adhesion formation and the beta 3 cytopLasmicdomain is required for the transmission of intracellular contractile forces to fibrin gels.
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Alterations in Integrin Receptor Expression on Chemically Transformed Human Cells: Specific Enhancement of Laminin and Collagen Receptor Complexes

TL;DR: A critical role is indicated for the alpha 6/beta 1 laminin receptor in the invasion of HOS cells through basement membranes and chemical transformation of nontumorigenic human cells to highly tumorigenic cells is associated with an altered pattern of integrin expression which may play a direct role in the increased capacity of these cells to bind and invade through basement membrane.
References
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Journal ArticleDOI

Arg-Gly-Asp: a versatile cell recognition signal.

Erkki Ruoslahti, +1 more
- 28 Feb 1986 - 
TL;DR: The RGD sequence as a basic unit of a widespread cellular recognition system is established and the same peptides also inhibit the attachment of fibroblasts to a number of other proteins, including vitronectin.
Journal ArticleDOI

Interaction of plasma membrane fibronectin receptor with talin—a transmembrane linkage

TL;DR: The interaction of the purified CSAT antigen with these cytoskeletal components is investigated, and an interaction specifically between theCSAT antigen and talin is demonstrated.
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Leukocyte adhesion deficiency: an inherited defect in the Mac-1, LFA-1, and p150,95 glycoproteins.

TL;DR: Recognition of the molecular pathogenesis of this disorder has allowed rich insights into the role of cellular adherence reactions in inflammation and host defense.
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Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor

TL;DR: Affinity chromatography on wheat germ agglutinin-Sepharose showed that the 140 kd protein is a glycoprotein and, in combination with the fibronectin fragment chromatography, gave highly enriched preparations of the 140Kd protein.
Journal ArticleDOI

Platelet membrane glycoprotein IIb/IIIa: member of a family of Arg-Gly-Asp--specific adhesion receptors

TL;DR: The results establish the existence of a family of adhesion receptors that recognize the sequence Arg-Gly-Asp, which corresponds to the cell adhesion site in fibronectin and is also present in the alpha chain of fibrinogen.
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