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Selective increase of α 2 ‐integrin sub‐unit expression on human carcinoma cells upon EGF‐receptor activation
Author(s) -
Krensel Kirstin,
Lichtner Rosemarie B.
Publication year - 1999
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/(sici)1097-0215(19990209)80:4<546::aid-ijc11>3.0.co;2-9
Subject(s) - integrin , fibronectin , a431 cells , microbiology and biotechnology , cell culture , cell adhesion , biology , a549 cell , cell , epidermal growth factor , epidermoid carcinoma , collagen receptor , chemistry , extracellular matrix , cell cycle , carcinoma , biochemistry , oncogene , genetics
The effects of chronic EGF exposure on expression of the α 2 β 1 collagen and α 5 β 1 fibronectin receptor in a pair of human carcinoma cell lines (A431 and A549) with differential responses to EGF in a short‐term ECM‐cell adhesion assay were investigated. Treatment with EGF at 10 ng/ml for 24 hr increased on both cell lines the expression of the α 2 ‐ but not the β 1 ‐ or α 5 ‐integrin sub‐units, and concomitantly cellular adhesion was increased on collagen IV but not on fibronectin. Increased collagen adhesion of A549 cells could be blocked by α 2 ‐ and β 1 ‐integrin‐sub‐unit antibodies down to control levels, while it was blocked by α 2 ‐integrin‐sub‐unit antibody only by 60% and completely by the β 1 ‐integrin‐sub‐unit antibody on A431 cells. EGF induced disparate shifts in cell morphologies (dome‐like structures, A431, vs. spindle‐like fibroblastoid, A549) with concomitant opposite changes in the expression/localization of E‐cadherin in cell‐cell contacts. This could be taken as an indication for cell‐type‐specific differential changes in the ratio of cell‐ECM vs. cell‐cell contacts. The EGF‐induced up‐regulation of the α 2 β 1 integrin was instrumental in increasing collagen adhesion of A549 but only partly in the case of A431 cells, in which cells the α 2 β 1 integrin may have additional functions besides serving as cell‐ECM receptor. Int. J. Cancer 80:546–552, 1999. © 1999 Wiley‐Liss, Inc.