CONSERVATION OF THE CARBOXYL TERMINAL EPITOPE OF MYELIN PROTEOLIPID PROTEIN IN THE TETRAPODS AND LOBE-FINNED FISH

被引：21

作者：

LININGTON, C

WAEHNELDT, TV

机构：

[1] MAX PLANCK INST EXPTL MED, W-3400 GOTTINGEN, GERMANY

[2] UNIV COLL CARDIFF, NEUROL SECT, CARDIFF CF4 4XN, S GLAM, WALES

来源：

JOURNAL OF NEUROCHEMISTRY | 1990年 / 54卷 / 04期

关键词：

Carboxyl terminal; Epitopes; Lobe‐finned fish; Myelin; Proteolipid protein; Tetrapods;

D O I：

10.1111/j.1471-4159.1990.tb01969.x

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：

Immunochemical analysis of the myelin proteolipid protein (PLP) has identified the carboxyl terminal amino acid phenylalanine276 as the only PLP epitope conserved between the PLP components of rat and lungfish, species representing the phylogenetically most widely separated groups that synthesise typical CNS myelin. Immunoblotting using a rabbit antiserum raised against the carboxyl terminal sequence of rat PLP (residues 257–276) identified this epitope on the PLP components of both tetrapod (rat, chicken, lizard, and frog) and lobe‐finned fish (coelacanth and lungfish) CNS myelin, including the DM‐20 isoform of PLP, which is restricted to rat, chicken, and lizard CNS myelin. The conservation of the carboxyl terminus of PLP during evolution suggests this structure may play an important role in maintaining the organisation and function of PLP in the myelin membrane. Copyright © 1990, Wiley Blackwell. All rights reserved

引用

页码：1354 / 1359

页数：6

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