Characterization of the cysteine-rich calcium-binding S100A3 protein from human hair cuticles

被引：17

作者：

Kizawa, K

Troxler, H

Kleinert, P

Inoue, T

Toyoda, M

Morohashi, M

Heizmann, CW

机构：

[1] Univ Zurich, Dept Pediat, Div Clin Chem & Biochem, CH-8032 Zurich, Switzerland

[2] Kanebo Ltd, Basic Res Lab, Odawara 2500002, Japan

[3] Toyama Med & Pharmaceut Univ, Fac Med, Dept Dermatol, Toyama 9300194, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2002年 / 299卷 / 05期

关键词：

S100A3; purification; hair cuticle; 2D gel electrophoresis; electrospray mass spectrometry; calcium; EF-hand;

D O I：

10.1016/S0006-291X(02)02744-4

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：

S100A3, a unique protein among all members of the calcium-binding S100 family, is specifically expressed at the inner endocuticle of human hair fibers. Upon hair damage, S100A3 is released from hair fibers and possibly destabilizes the hair tissue architecture. This study describes the purification and characterization of native S100A3 isolated from human hair fibers. We extracted native S100A3 from cuticles and purified the protein by anion-exchange chromatography. The results of 2D gel electrophoresis showed that cuticle S100A3 has a slightly lower isoelectric point compared to the recombinant protein. Tandem mass spectrometry of the peptides resulting from endoproteinase digest of cuticle S100A3 revealed that the N-terminal methionine is replaced with an acetyl group. This is the first report on biochemical characteristics of S100A3 in hair cuticle. (C) 2002 Elsevier Science (USA). All rights reserved.

引用

页码：857 / 862

页数：6

共 19 条

[1] 6 S100 GENES ARE CLUSTERED ON HUMAN CHROMOSOME-1Q21 - IDENTIFICATION OF 2 GENES-CODING FOR THE 2 PREVIOUSLY UNREPORTED CALCIUM-BINDING PROTEIN-S100D AND PROTEIN-S100E [J].