Wide distribution of cysteine-rich secretory proteins in snake venoms: Isolation and cloning of novel snake venom cysteine-rich secretory proteins

被引：118

作者：

Yamazaki, Y ^{[1
]}

Hyodo, F ^{[1
]}

Morita, T ^{[1
]}

机构：

[1] Meiji Pharmaceut Univ, Dept Biochem, Tokyo 2048588, Japan

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2003年 / 412卷 / 01期

关键词：

snake venom; cysteine-rich secretory proteins; cloning; purification; distribution;

D O I：

10.1016/S0003-9861(03)00028-6

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：

Cysteine-rich secretory proteins (CRISPs) are found in epididymis and granules of mammals, and they are thought to function in sperm maturation and in the immune system. Recently, we isolated and obtained clones for novel snake venom proteins that are classified as CRISP family proteins. To elucidate the distribution of snake venom CRISP family proteins, we evaluated a wide range of venoms for immuno-cross-reactivity. Then we isolated, characterized, and cloned genes for three novel CRISP family proteins (piscivorin, ophanin, and catrin) from the venom of eastern cottonmouth (Agkistrodon piscivorus piscivorus), king cobra (Ophiophagus hannah), and western diamondback rattlesnake (Crotalus atrox). Our results show the wide distribution of snake venom CRISP family proteins among Viperidae and Elapidae from different continents, indicating that CRISP family proteins compose a new group of snake venom proteins. (C) 2003 Elsevier Science (USA). All rights reserved.

引用

页码：133 / 141

页数：9

共 46 条

[1]

ATODA H, 1991, J BIOL CHEM, V266, P14903

[2] Purification and characterization of a chymotrypsin inhibitor from the venom of Ophiophagus hannah (King Cobra) [J].

Chang, LS ;

Chung, C ;

Huang, HB ;

Lin, SR .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2001, 283 (04) :862-867

[3] Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the elapid snake Bungarus fasciatus [J].

Chen, CP ;

Hsu, CH ;

Su, NY ;

Lin, YC ;

Chiou, SH ;

Wu, SH .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (48) :45079-45087

[4] A novel hydrophobic omega-conotoxin blocks molluscan dihydropyridine-sensitive calcium channel [J].

Fainzilber, M ;

Lodder, JC ;

vanderSchors, RC ;

Li, KW ;

Yu, ZH ;

Burlingame, AL ;

Geraerts, WPM ;

Kits, KS .

BIOCHEMISTRY, 1996, 35 (26) :8748-8752

[5] Experimentally based model of a complex between a snake toxin and the α7 nicotinic receptor [J].

Fruchart-Gaillard, C ;

Gilquin, B ;

Antil-Delbeke, S ;

Le Novère, N ;

Tamiya, T ;

Corringer, PJ ;

Changeux, JP ;

Ménez, A ;

Servent, D .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (05) :3216-3221

[6] Crystal structure of flavocetin-A, a platelet glycoprotein Ib-binding protein, reveals a novel cyclic tetramer of C-type lectin-like heterodimers [J].

Fukuda, K ;

Mizuno, H ;

Atoda, H ;

Morita, T .

BIOCHEMISTRY, 2000, 39 (08) :1915-1923

[7]

Furie B.C., 1976, Methods Enzymol, V45, P191

[8] TRANSCRIPTS FOR CYSTEINE-RICH SECRETORY PROTEIN-1 (CRISP-1, DE/AEG) AND THE NOVEL RELATED CRISP-3 ARE EXPRESSED UNDER ANDROGEN CONTROL IN THE MOUSE SALIVARY-GLAND [J].

HAENDLER, B ;

KRATZSCHMAR, J ;

THEURING, F ;

SCHLEUNING, WD .

ENDOCRINOLOGY, 1993, 133 (01) :192-198

[9] Recent studies on dendrotoxins and potassium ion channels [J].

Harvey, AL .

GENERAL PHARMACOLOGY-THE VASCULAR SYSTEM, 1997, 28 (01) :7-12

[10] Twenty years of dendrotoxins [J].

Harvey, AL .

TOXICON, 2001, 39 (01) :15-26

← 1 2 3 4 5 →