(Q28289349)

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Differential effects of the integrins alpha9beta1, alphavbeta3, and alphavbeta6 on cell proliferative responses to tenascin. Roles of the beta subunit extracellular and cytoplasmic domains

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scholarly article

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Differential effects of the integrins alpha9beta1, alphavbeta3, and alphavbeta6 on cell proliferative responses to tenascin. Roles of the beta subunit extracellular and cytoplasmic domains (English)

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author name string

Y Yokosaki

1

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H Monis

2

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J Chen

3

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D Sheppard

4

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language of work or name

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publication date

27 September 1996

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Journal of Biological Chemistry

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271

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39

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24144-50

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Normal human skin demonstrates marked site-variation of tenascin expression, not correlated to epidermal proliferation (Ki-67 binding)

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The human integrin alpha 8 beta 1 functions as a receptor for tenascin, fibronectin, and vitronectin

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Characterization of multiple adhesive and counteradhesive domains in the extracellular matrix protein cytotactin

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Multiple integrins mediate cell attachment to cytotactin/tenascin

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The alpha v beta 6 integrin promotes proliferation of colon carcinoma cells through a unique region of the beta 6 cytoplasmic domain

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Integrin-dependent activation of MAP kinase: a link to shape-dependent cell proliferation

1 reference

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Role of cell shape in growth control

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Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly

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Paxillin: a cytoskeletal target for tyrosine kinases

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Integrin alpha v beta 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels

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Requirement of vascular integrin alpha v beta 3 for angiogenesis

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Antiintegrin alpha v beta 3 blocks human breast cancer growth and angiogenesis in human skin

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Identifiers

10.1074/JBC.271.39.24144

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