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Lack of protein 4.1a in red blood cells of the hereditarily anemic Belgrade laboratory ( b/b ) rat
Author(s) -
Lušić Marina,
Zarić Jelena,
Ðurković Aleksandra,
Glišin Vladimir,
Popović Zvezdana
Publication year - 1999
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19991001)75:1<56::aid-jcb6>3.0.co;2-j
Subject(s) - gene isoform , red blood cell , in vivo , membrane protein , life span , biology , membrane , chemistry , microbiology and biotechnology , biochemistry , medicine , gene , evolutionary biology
We have demonstrated that the red blood cell (RBC) membrane of the hereditarily anemic Belgrade laboratory ( b/b ) rat contains protein 4.1b isoform, only. The evidence are given that the synthesis of protein 4.1 in the b/b rat reticulocytes is the same as in normal rat. When haemolytic anaemia was induced in normal rat by in vivo phenyhydrazine treatment the same phenomenon, i.e., the absence of protein 4.1a in the RBC membrane was observed. The increase of 4.1a isoform was monitored in RBCs during the recovery of normal rat after phenyhydrazine treatment. Hence, the portion of membrane protein 4.1a isoform is increasing during rat RBC aging. Likewise, when the RBC life span is prolonged (but not normalised) in the b/b rats by iron‐dextran treatment protein 4.1a is present in small portion in the RBC membrane. All these data indicate that the lack of protein 4.1a isoform in the b/b rat is due to the presence of young RBCs in the circulation. J. Cell. Biochem. 75:56–63, 1999. © 1999 Wiley‐Liss, Inc.