Characterization of two novel human small heat shock proteins:: protein kinase-related HspB8 and testis-specific HspB9

被引:95
作者
Kappé, G
Verschuure, P
Philipsen, RLA
Staalduinen, AA
Van de Boogaart, P
Boelens, WC
De Jong, WW
机构
[1] Univ Nijmegen, Dept Biochem 161, NL-6500 HB Nijmegen, Netherlands
[2] NV Organon, NL-5340 BH Oss, Netherlands
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 2001年 / 1520卷 / 01期
关键词
alpha-crystallin; heat shock protein; spermatogenesis; in situ hybridization; gene expression;
D O I
10.1016/S0167-4781(01)00237-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Using search profiles based on the conserved alpha -crystallin domain that is characteristic for small heat shock proteins (sHsps), we traced two new human sHsps. One of these, being the eighth known human sHsp and thus named HspB8, was recently described as a serine-threonine protein kinase (H11), but not identified as an sHsp (C.C. Smith, Y.X. Yu, M. Kulka, L. Aurelian, J. Biol. Chem. 275 (2000)). Northern blotting showed that HspB8/H11 is predominantly transcribed in skeletal muscle and heart, like most other sHsps. The other, named HspB9, is specifically expressed in testis, notably in the spermatogenic cells from late pachytene spermatocyte stage till elongate spermatid stage. While mammalian sHsps are generally highly conserved, mouse HspB9 shows 38% sequence difference with human HspB9, which may confirm its sex-related role. (C) 2001 Elsevier Science B.V. All rights reserved.
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页码:1 / 6
页数:6
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