Identification and characterization of phospholipase A2 inhibitors from the serum of the Japanese rat snake, Elaphe climacophora

被引：30

作者：

Shirai, Ryoichi ^{[1
]}

Toriba, Michihisa ^{[2
]}

Hayashi, Kyozo ^{[1
]}

Ikeda, Kiyoshi ^{[1
]}

Inoue, Seiji ^{[1
]}

机构：

[1] Osaka Univ Pharmaceut Sci, Biochem Lab, Osaka 5691094, Japan

[2] Japan Snake Inst, Gunma 3792301, Japan

来源：

TOXICON | 2009年 / 53卷 / 06期

关键词：

Phospholipase A(2); PLA(2); Phospholipase A(2) inhibitor; PLI; Colubridae; cDNA sequence; AGKISTRODON-BLOMHOFFII-SINITICUS; AMINO-ACID-SEQUENCE; BLOOD-PLASMA; TRIMERESURUS-FLAVOVIRIDIS; MYOTOXIN INHIBITOR; NONVENOMOUS SNAKE; SUBUNITS; MOLECULAR-CLONING; CHINESE MAMUSHI; CDNA CLONING;

D O I：

10.1016/j.toxicon.2009.02.001

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Two distinct phospholipase A(2) (PLA(2)) inhibitory proteins (PLIs) were purified from the serum of the Japanese rat snake, Elaphe climacophora. The 150-kDa inhibitor, a trimer of a 50-kDa subunit, specifically inhibited the basic PLA(2) purified from the venom of Gloydius brevicaudus, whereas the 120-kDa one composed of two distinct 25-kDa subunits, A and B, inhibited both the acidic and basic PLA(2)S of G. brevicaudus. On the basis of their amino acid sequences, these inhibitors were assigned as PLI beta and PLI gamma, respectively. A PLI alpha homolog (PLI alpha-like protein; PLI alpha-LP) having an apparent molecular weight of 50-kDa and composed of 15-kDa subunits was also purified from the E climacophora serum. This homolog was immunoreactive with antibody raised against the G. brevicaudus PLI alpha, but lacked in the inhibitory activity toward the acidic and basic PLA(2)s. The cDNAs encoding PLI alpha-LP, PLI beta, PLI gamma-A, and PLI gamma-B were cloned from liver RNA, and their nucleotide sequences were compared with those of other venomous and non-venomous snakes. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：685 / 692

页数：8

共 26 条

[1] Inhibition of crotoxin binding to synaptosomes by a receptor-like protein from Crotalus durissus terrificus (the South American rattlesnake) [J].

dos Santos, RMM ;

Oliveira, LC ;

Estevao-Costa, MI ;

de Lima, ME ;

Santoro, MM ;

Fortes-Dias, CL .

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2005, 1717 (01) :27-33

[2] Snake inhibitors of phospholipase A2 enzymes [J].

Dunn, RD ;

Broady, KW .

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS, 2001, 1533 (01) :29-37

[3]

Inoue S, 1997, BIOCHEM MOL BIOL INT, V41, P529

[4]

INOUE S, 1991, J BIOL CHEM, V266, P1001

[5]

Kini RM, 2003, TOXICON, V42, P827, DOI 10.1016/j.toxicon.2003.11.002

[6] Receptors for a growing family of secreted phospholipases A2 [J].

Lambeau, G ;

Lazdunski, M .

TRENDS IN PHARMACOLOGICAL SCIENCES, 1999, 20 (04) :162-170

[7] Biochemical characterization and pharmacological properties of a phospholipase A(2) myotoxin inhibitor from the plasma of the snake Bothrops asper [J].

Lizano, S ;

Lomonte, B ;

Fox, JW ;

Gutierrez, JM .

BIOCHEMICAL JOURNAL, 1997, 326 :853-859

[8] Two phospholipase A2 inhibitors from the plasma of Cerrophidion (Bothrops) godmani which selectively inhibit two different group-II phospholipase A2 myotoxins from its own venom:: isolation, molecular cloning and biological properties [J].

Lizano, S ;

Angulo, Y ;

Lomonte, B ;

Fox, JW ;

Lambeau, G ;

Lazdunski, M ;

Gutiérrez, JM .

BIOCHEMICAL JOURNAL, 2000, 346 :631-639

[9]

MORI A, 1988, Snake, V20, P98

[10] Structural elements of Trimeresurus flavoviridis serum inhibitors for recognition of its venom phospholipase A2 isozymes [J].

Nobuhisa, I ;

Chiwata, T ;

Fukumaki, Y ;

Hattori, S ;

Shimohigashi, Y ;

Ohno, M .

FEBS LETTERS, 1998, 429 (03) :385-389

← 1 2 3 →