ENDOPEPTIDASE-24.11 CLEAVES A CHEMOTACTIC FACTOR FROM ALPHA-CALCITONIN GENE-RELATED PEPTIDE

被引：22

作者：

DAVIES, D

MEDEIROS, MS

KEEN, J

TURNER, AJ

HAYNES, LW

机构：

[1] UNIV LEEDS,DEPT BIOCHEM & MOLEC BIOL,LEEDS LS2 9JT,W YORKSHIRE,ENGLAND

[2] UNIV BRISTOL,DEPT ZOOL,BRISTOL BS8 1UG,AVON,ENGLAND

来源：

BIOCHEMICAL PHARMACOLOGY | 1992年 / 43卷 / 08期

基金：

英国惠康基金;

关键词：

D O I：

10.1016/0006-2952(92)90706-O

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

The sequence of rat alpha-calcitonin gene-related peptide (CGRP-alpha) contains the tetrapeptide eosinophil granulocyte chemotactic factor Val32-Gly-Ser-Glu35. Peptide fragments formed following hydrolysis of rat CGRP-alpha in vitro by endopeptidase-24.11 were identified. The tetrapeptide fragment was generated following cleavage at a substrate recognition site unusual for this enzyme (-Glu-Ala-). Chemotactic activity of rat CGRP-alpha was increased following hydrolysis. Furthermore. rat CGRP-beta, which lacks the tetrapeptide sequence and is completely devoid of chemotactic activity, displayed low but measurable activity after hydrolysis. Val-Gly-Ser-Glu was identified as the principle fragment with chemotactic activity in rat CGRP-alpha. The results show that the chemotactic activity of the neuropeptide rat CGRP-alpha towards eosinophil polymorphonuclear leukocytes is increased following its hydrolysis in vitro by endopeptidase 24.11 through the formation of a previously identified eosinophil chemotactic tetrapeptide.

引用

页码：1753 / 1756

页数：4

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