1. Purification, characterization and cytokine release function of a novel Arg-49 phospholipase A(2) from the venom of Protobothrops mucrosquamatus.
- Author
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Wei JF, Li T, Wei XL, Sun QY, Yang FM, Chen QY, Wang WY, Xiong YL, and He SH
- Subjects
- Amino Acid Sequence, Animals, Anti-Bacterial Agents pharmacology, Arginine, Base Sequence, Humans, Molecular Sequence Data, Molecular Weight, Monocytes drug effects, Monocytes immunology, Phospholipases A isolation & purification, Rats, Rats, Wistar, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, T-Lymphocytes drug effects, T-Lymphocytes immunology, Crotalid Venoms enzymology, Cytokines metabolism, Phospholipases A chemistry, Phospholipases A pharmacology
- Abstract
Group IIA phospholipase A(2) (PLA(2)) are major components in Viperidae/Crotalidae venom. In the present study, a novel PLA(2) named promutoxin with Arg at the site 49 has been purified from the venom of Protobothrops mucrosquamatus by chromatography. It consists of 122 amino acid residues with a molecular mass of 13,656 Da assessed by MALDI-TOF. It has the structural features of snake venom group IIA PLA(2)s, but has no PLA(2) enzymatic activity. Promutoxin shows higher amino acid sequence identity to the K49 PLA(2)s (72-95%) than to D49 PLA(2)s (52-58%). Promutoxin exhibits potent myotoxicity in the animal model with as little as 1 microg of promutoxin causing myonecrosis and myoedema in the gastrocnemius muscle of mice. Promutoxin is also able to stimulate the release of IL-12, TNFalpha, IL-6 and IL-1beta from human monocytes, and induce IL-2, TNFalpha and IL-6 release from T cells, indicating that this snake venom group IIA PLA(2) is actively involved in the inflammatory process in man caused by snake venom poisoning.
- Published
- 2006
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