DISSOCIATION OF NEURITE-PROMOTING ACTIVITY AND PROTEASE-INHIBITING FUNCTION OF ALPHA-2-MACROGLOBULIN IN CULTURE

被引：12

作者：

MORI, T ^{[1
]}

MIYAMOTO, Y ^{[1
]}

IIJIMA, N ^{[1
]}

KITABATAKE, K ^{[1
]}

KOHSAKA, S ^{[1
]}

机构：

[1] NATL INST NEUROSCI,DEPT NEUROCHEM,TOKYO,JAPAN

来源：

BRAIN RESEARCH | 1991年 / 567卷 / 02期

关键词：

ALPHA-2-MACROGLOBULIN; NEURON; NEURITE-PROMOTING ACTIVITY; PROTEASE INHIBITOR;

D O I：

10.1016/0006-8993(91)90820-L

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

The relationship between the neurite-promoting effect and the protease-inhibiting function of alpha(2)-macroglobulin (alpha(2)M) was examined in a culture of dissociated neurons from embryonic rat neocortical tissue. The neurite-promoting effect of various protease inhibitors (soybean trypsin inhibitor, alpha(1)-antitrypsin, aprotinin, phenylmethanesulfonyl fluoride, leupeptin, antipain, human alpha(2)M and purified rat alpha(2)M) was investigated. At lower concentrations, only alpha(2)M significantly promoted neurite outgrowth. Furthermore, alpha(2)M-trypsin complexes, which had lost their protease-inhibiting function and exposed their receptor-recognition site, promoted neurite outgrowth more efficiently than native alpha(2)M. These results indicate the possibility that the neurite-promoting effect of alpha(2)M is mediated by its receptor-binding activity but is not directly related to its protease-inhibiting function.

引用

页码：355 / 357

页数：3

共 19 条

[1] THE HUMAN ALPHA-2-MACROGLOBULIN RECEPTOR - IDENTIFICATION OF A 420-KD CELL-SURFACE GLYCOPROTEIN SPECIFIC FOR THE ACTIVATED CONFORMATION OF ALPHA-2-MACROGLOBULIN [J].