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Stable expression of VLA‐4 and increased maturation of the β 1 ‐integrin precursor after transfection of CHO cells with α 4m cDNA
Author(s) -
Jaspers Martine,
de Meirsman Catherine,
Schollen Els,
Vekemans Sylvie,
Cassiman Jean-Jacques
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01054-4
Subject(s) - transfection , chinese hamster ovary cell , microbiology and biotechnology , complementary dna , g alpha subunit , biology , hamster , cell culture , interleukin 10 receptor, alpha subunit , beta (programming language) , alpha (finance) , integrin , protein subunit , cell , biochemistry , gene , genetics , medicine , construct validity , nursing , computer science , patient satisfaction , programming language
A full‐length cDNA coding for the murine α 4 integrin subunit (α 4m ) was transfected into CHO‐K1 cells and cell lines that expressed VLA‐4 at their surface as a result of the association of transfected α 4m with endogenous hamster β 1 were selected. Functionality of the expressed α 4m β 1 was shown by adhesion assays on VCAM‐1 and antibody (anti‐VCAM‐ 1) inhibition. Pulse chase experiments indicated that transfection of the murine α 4 cDNA into CHO cells led to an increase in maturation and a decrease in degradation of the β 1 precursor subunit compared to control CHO‐K1 cells. This was supported by FACS analysis, using an anti‐hamster β 1 monoclonal antibody, which showed that more β 1 subunit was expressed at the surface of these stably transfected α 4m expressing cells. These results support the hypothesis that degradation of precursor β 1 is at least partly determined by the quantity of α subunits available intracellulary for heterodimer formation.