Axonal proteins involved in myelination: characterization of a collagen-like protein.
Axonal proteins involved in myelination: characterization of a collagen-like protein.
复制标题
参与髓鞘形成的轴突蛋白：胶原蛋白样蛋白的表征。
DOI：
10.1159/000111239
复制
发表时间：
1997
影响因子：
2.9
通讯作者：
Rome,LH
中科院分区：
文献类型：
--
作者：
Raval-Fernandes,S;Sawant,LA;Aebersold,RH;Ducret,A;Rome,LH
An anti-axolemma monoclonal antibody, designated G21.3, has been isolated in order to understand molecular mechanisms involved in myelination. Both biochemical and morphological studies showed that the monoclonal antibody inhibits myelin production by oligodendrocytes in cerebellar slice cultures. On Western blots of axolemma preparations, the antibody recognized 140- and 120-kD proteins. The present study involves the isolation and characterization of the G21.3 antigen. The G21.3-immunoreactive proteins of 140 and 120 kD were purified from the adult rat sciatic nerve and amino acid sequencing of these proteins revealed significant homology to αI and αII chains of collagen type I. Biochemical and Western blot analysis using pure collagen, collagen I antibody and collagenase D suggest that the antigen isolated from sciatic nerve is collagen. However, immunofluorescence studies using the G21.3 antibody, collagen I antibody, collagenase D and Northern blot analysis using a collagen probe do not fully support the view that the G21.3 antigen in the CNS is also a collagen. We conclude that the G21.3 antigen is a collagenlike protein involved in CNS myelination.
