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Lack of protein 4.1a in red blood cells of the hereditarily anemic Belgrade laboratory ( b/b ) rat

Lack of protein 4.1a in red blood cells of the hereditarily anemic Belgrade laboratory ( b/b ) rat 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Cellular Biochemistry Wiley

Lack of protein 4.1a in red blood cells of the hereditarily anemic Belgrade laboratory ( b/b ) rat

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Publisher
Wiley
Copyright
Copyright © 1999 Wiley‐Liss, Inc.
ISSN
0730-2312
eISSN
1097-4644
DOI
10.1002/(SICI)1097-4644(19991001)75:1<56::AID-JCB6>3.3.CO;2-A
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Journal of Cellular Biochemistry – Wiley

Published: Oct 1, 1999

Keywords: RBC membrane; protein 4.1; RBC aging; b/b rat

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