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The synthesis and accumulation of membrane protein 4.1 in Friend erythroleukemia cells
Author(s) -
Benabdallah Khadija,
Boivin Pierre,
Dhermy Didier
Publication year - 1991
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1016/0248-4900(91)90270-w
Subject(s) - biology , fibronectin , protein biosynthesis , microbiology and biotechnology , cellular differentiation , membrane , cell culture , membrane protein , biochemistry , cell , gene , genetics
Summary— The effect of extensive differentiation on the synthesis and accumulation of protein 4.1 were studied on Friend erythroleukemia grown in suspension and on fibronectin coated dishes. Whole membranes of Friend erythroleukemia cells (FELC) contained a protein 4.1a and 4.1b doublet of M r 76 and 74 kDa and two minor bands of M r 105 and 43 Da that cross‐reacted with anti‐human protein 4.1 IgG. These proteins were present even in uninduced cells. the synthesis of protein 4.1 was maximal after 4 days of induction in both suspension culture and in fibronectin‐coated dishes whereas the protein 4.1 continued to accumulate until the seventh day. More protein 4.1 accumulated in cells grown on fibronectin‐coated dishes, at each stage of differentiation, than in cells grown in suspension. The protein 4.1a/4.1b ratio changed during differentiation. The amounts of protein 4.1b increased progressively after induction until the protein 4.1a/4.1b ratio was similar to that of mouse mature erythrocyte. The protein 4.1a/4.1b ratio appears to be an internal marker of erythroid differentiation.