Literature DB >> 3292271

Regulation of proteins in the VLA cell substrate adhesion family: influence of cell growth conditions on VLA-1, VLA-2, and VLA-3 expression.

E Fingerman1, M E Hemler.   

Abstract

Cell quiescence resulting from culture of normal human fibroblasts in low serum (0.5%) was associated with a subsequent gradual increase in the expression of the cell-surface glycoprotein VLA-1, and a corresponding decrease in the expression of extracellular matrix adhesion receptors VLA-2 and VLA-3. Quantitation using either flow cytometry or immunoprecipitation showed that both the VLA-1/VLA-2 and VLA-1/VLA-3 ratios increased 10- to 28-fold and were still rising when cells remained quiescent for 20-30 days. Although induced by cell quiescence, changes in the levels of VLA-1, VLA-2, and VLA-3 continued to occur well after cell proliferation had stopped and thus do not directly correlate with cell cycle transition events. Despite prolonged serum deprivation resulting in elevated VLA-1/VLA-2 and VLA-1/VLA-3 ratios, growth-arrested cells remained viable and were fully capable of proliferating when restimulated. The increases in VLA-1/VLA-2 and VLA-1/VLA-3 ratios observed on quiescent cells were readily reversible, since after restimulation with 10% serum, these ratios quickly returned within 1-2 days to a level near that found on normal exponentially grown cells. Elevation of VLA-1/VLA-2 and VLA-1/VLA-3 ratios is generally associated with quiescence and is not due just to serum deprivation since density arrest of cells at confluence had similar effects on these ratios.

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Year:  1988        PMID: 3292271     DOI: 10.1016/0014-4827(88)90031-6

Source DB:  PubMed          Journal:  Exp Cell Res        ISSN: 0014-4827            Impact factor:   3.905


  8 in total

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Authors:  M V Agrez; R C Bates; A W Boyd; G F Burns
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2.  Comparative evaluation of integrin alpha- and beta-chain expression in colorectal carcinoma cell lines and in their tumours of origin.

Authors:  K Koretz; S Brüderlein; C Henne; T Fietz; M Laqué; P Möller
Journal:  Virchows Arch       Date:  1994       Impact factor: 4.064

3.  Coexpression of two fibronectin receptors, VLA-4 and VLA-5, by immature human erythroblastic precursor cells.

Authors:  M Rosemblatt; M H Vuillet-Gaugler; C Leroy; L Coulombel
Journal:  J Clin Invest       Date:  1991-01       Impact factor: 14.808

4.  Differential expression of beta 1 integrins in nonneoplastic smooth and striated muscle cells and in tumors derived from these cells.

Authors:  G Mechtersheimer; T Barth; A Quentmeier; P Möller
Journal:  Am J Pathol       Date:  1994-06       Impact factor: 4.307

5.  Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations.

Authors:  M J Elices; L A Urry; M E Hemler
Journal:  J Cell Biol       Date:  1991-01       Impact factor: 10.539

6.  Human smooth muscle VLA-1 integrin: purification, substrate specificity, localization in aorta, and expression during development.

Authors:  V M Belkin; A M Belkin; V E Koteliansky
Journal:  J Cell Biol       Date:  1990-11       Impact factor: 10.539

7.  Molecular cloning and expression of the cDNA for alpha 3 subunit of human alpha 3 beta 1 (VLA-3), an integrin receptor for fibronectin, laminin, and collagen.

Authors:  Y Takada; E Murphy; P Pil; C Chen; M H Ginsberg; M E Hemler
Journal:  J Cell Biol       Date:  1991-10       Impact factor: 10.539

8.  The primary structure of the VLA-2/collagen receptor alpha 2 subunit (platelet GPIa): homology to other integrins and the presence of a possible collagen-binding domain.

Authors:  Y Takada; M E Hemler
Journal:  J Cell Biol       Date:  1989-07       Impact factor: 10.539

  8 in total

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