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Titolo:
Does post-translational modification influence chaperone-like activity of alpha-crystallin? I. Study on phosphorylation
Autore:
Kamei, A; Hamaguchi, T; Matsuura, N; Masuda, K;
Indirizzi:
Meijo Univ, Fac Pharmaceut Sci, Dept Biochem, Tenpaku Ku, Aichi 4688503, Japan Meijo Univ Aichi Japan 4688503 Biochem, Tenpaku Ku, Aichi 4688503, Japan Suntory Inst Bioorgan Res, Shimamoto, Osaka 6188503, Japan Suntory Inst Bioorgan Res Shimamoto Osaka Japan 6188503 ka 6188503, Japan
Titolo Testata:
BIOLOGICAL & PHARMACEUTICAL BULLETIN
fascicolo: 1, volume: 24, anno: 2001,
pagine: 96 - 99
SICI:
0918-6158(200101)24:1<96:DPMICA>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
C-TERMINAL REGION; A-CRYSTALLIN; HUMAN LENS; MOLECULAR CHAPERONE; B-CRYSTALLIN; POSTTRANSLATIONAL MODIFICATIONS; PROTEIN; IDENTIFICATION; BOVINE; SITES;
Keywords:
bovine lens; alpha-crystallin; post-translational modification; phosphorylation; chaperone-like activity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Kamei, A Meijo Univ, Fac Pharmaceut Sci, Dept Biochem, Tenpaku Ku, 150 Yagotoyama, Aichi 4688503, Japan Meijo Univ 150 Yagotoyama Aichi Japan 4688503 chi 4688503, Japan
Citazione:
A. Kamei et al., "Does post-translational modification influence chaperone-like activity of alpha-crystallin? I. Study on phosphorylation", BIOL PHAR B, 24(1), 2001, pp. 96-99

Abstract

It is difficult to isolate derivatives of alpha -crystallin nlith only onetype of post-translational modification, because this protein is subjectedto several different types of modification. In the present study using bovine lens proteins, we isolated mono-phosphoralated alphaB-crystallin with no other post-translational modifications, Using this material, we demonstrated that mono-phosphorylation reduced the activity of alphaB-crystallin by approximately 30%. Our results confirmed that investigation of the correlation between chaperone-like activities of alpha -crystallin and post-translational modification is important to understand the mechanism of cataract formation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:41:11