Role for myelin-associated glycoprotein as a functional tenascin-R receptor.

Abstract:

:The expression of the immunoglobulin superfamily member myelin-associated glycoprotein (MAG) and the extracellular matrix glycoprotein tenascin-R (TN-R) by oligodendrocytes overlaps in time and space. The two molecules can be neurite outgrowth-inhibitory or -promoting depending on the neuronal cell type and the environment in which they are presented. Here we show that the two molecules directly bind to each other in vitro and that binding sites on TN-R localize to two domains, the fibrinogen domain and the epidermal growth factor-like repeat domain with the N-terminal cysteine-rich stretch. We further show by a functional assay, namely the repulsion of MAG-transfected Chinese hamster ovary cells (CHO) cells from a TN-R substrate, that MAG is part of the signalling pathway of TN-R for cell repulsion. When coated as a uniform substrate, MAG was inhibitory for neurite outgrowth of hippocampal and cerebellar neurons in vitro, when compared to poly-L-lysine, while TN-R enhanced neurite outgrowth. When added to MAG, TN-R neutralized the neurite outgrowth-inhibitory effects of MAG, presumably by blocking the neurite outgrowth-inhibitory domain of MAG.

journal_name

J Neurosci Res

authors

Yang H,Xiao ZC,Becker B,Hillenbrand R,Rougon G,Schachner M

doi

10.1002/(SICI)1097-4547(19990315)55:6<687::AID-JNR

keywords:

subject

Has Abstract

pub_date

1999-03-15 00:00:00

pages

687-701

issue

6

eissn

0360-4012

issn

1097-4547

pii

10.1002/(SICI)1097-4547(19990315)55:6<687::AID-JNR

journal_volume

55

pub_type

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