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Digitale Medien

Focal adhesion kinase is abundant in developing blood vessels and elevation of its phosphotyrosine content in vascular smooth muscle cells is a rapid response to angiotensin II (1994)

Polte, Thomas R. ; Hanks, Steven K. ; Naftilan, Allen J.

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 55 (1994), S. 106-119

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ISSN: 0730-2312

Schlagwort(e): protein-tyrosine kinase ; embryogenesis ; extracellular matrix ; fibronectin ; Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie , Chemie und Pharmazie , Medizin

Notizen: Focal adhesion kinase (FAK) is a structurally unique nonreceptor protein-tyrosine kinase that localizes to focal adhesion plaques. Regulation of its activity has been implicated in diverse signaling pathways, including those mediated by extracellular matrix/integrin interactions, G-protein coupled receptors for mitogenic neuropeptides, and certain oncogene products. To gain evidence for specific processes in which FAK may be involved in vivo, a study was initiated to determine its expression pattern during mouse development. FAK expression was detected in early embryos and appeared to be distributed throughout all cell types at about the time of neurulation. Subsequent to neural tube closure, expression became particularly abundant in the developing vasculature. This included expression in the medial layer of arteries populated by smooth muscle cells. In vitro studies using cultured rat aortic vascular smooth muscle cells demonstrate that FAK phosphotyrosine content is dramatically elevated in response to plating cells onto the adhesive glycoprotein, fibronectin. Also, enhanced tyrosine phosphorylation of FAK is observed in these cells upon stimulation with the vasoconstrictor angiotensin II. Thus, in vascular smooth muscle cells, like fibroblasts, FAK appears to play a role in signaling mechanisms induced by extracellular matrix components as well as G-protein coupled receptor agonists. The combined results of this study suggest that signaling through FAK may play an important role in blood vessel morphogenesis and function. © 1994 Wiley-Liss, Inc.

Zusätzliches Material: 7 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/jcb.240550113

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Digitale Medien

Signaling through focal adhesion kinase (1997)

Hanks, Steven K. ; Polte, Thomas R.

New York, NY : Wiley-Blackwell

BioEssays 19 (1997), S. 137-145

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ISSN: 0265-9247

Schlagwort(e): Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie , Medizin

Notizen: Focal adhesion kinase (FAK) is a nonreceptor protein-tyrosine kinase implicated in controlling cellular responses to the engagement of cell-surface integrins, including cell spreading and migration, survival and proliferation. Aberrant FAK signaling may contribute to the process of cell transformation by certain oncoproteins, including v-Src. Progress toward elucidating the events leading to FAK activation following integrin-mediated cell adhesion, as well as events downstream of FAK, has come through the identification of FAK phosphorylation sites and interacting proteins. A signaling partnership is formed between FAK and Src-family kinases, leading to tyrosine phosphorylation of FAK and associated ‘docking’ proteins Cas and paxillin. Subsequent recruitment of proteins containing Src homology 2 domains, including Grb2 and c-Crk, to the complex is likely to trigger adhesion-induced cellular responses, including changes to the actin cytoskeleton and activation of the Ras-MAP kinase pathway.

Zusätzliches Material: 3 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/bies.950190208

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