Novel specific chemotactic receptor for S100L protein on guinea pig eosinophils

被引：50

作者：

Komada, T

Araki, R

Nakatani, K

Yada, I

Naka, M

Tanaka, T

机构：

[1] MIE UNIV,SCH MED,DEPT MOLEC & CELLULAR PHARMACOL,TSU,MIE 514,JAPAN

[2] MIE UNIV,SCH MED,DEPT THORAC & CARDIOVASC SURG,TSU,MIE 514,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1996年 / 220卷 / 03期

关键词：

D O I：

10.1006/bbrc.1996.0496

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：

We isolated a new chemotactic protein from bovine lung, and its partial protein sequence analysis indicated that this protein was identical with S100L, one member of the Ca2+-binding S100 protein family. The chemotactic activity of S100L on guinea pig eosinophils is observed at 0.1nM protein concentration, and the effects appear mediated by a novel specific surface receptor. We characterized the receptor for S100L on guinea pig eosinophils. Scatchard analyses of the data that [I-125]S100L bound to S100L receptor indicate the presence of two receptor populations on eosinophils with a Kd value of 3.3 x 10(-11)M and 1.1 x 10(-9)M. Thus, S100L protein has the most potent chemotactic activity on guinea pig eosinophils of all the chemotactic proteins. (C) 1996 Academic Press, Inc.

引用

页码：871 / 874

页数：4

共 17 条

[1] CARDIAC S-100A0 PROTEIN - PURIFICATION BY A SIMPLE PROCEDURE AND RELATED IMMUNOCYTOCHEMICAL AND IMMUNOCHEMICAL STUDIES [J].