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Journal of Cell Science, Vol 93, Issue 1 85-94, Copyright © 1989 by Company of Biologists

JOURNAL ARTICLES

A Ca2(+)-sensitive glycoprotein, GP90, associated with the cytoskeleton from brain and gizzard

DJ Moss and CA White
Department of Biophysics, Cell and Molecular Biology, King's College, London, UK.

We describe here the expression during development, tissue distribution and molecular properties of GP90: a major concanavalin A (ConA)-binding glycoprotein present in the neuronal membrane skeleton from chicken brain. GP90 is co-isolated with, and has a similar developmental profile to contactin (previously called GP130). In whole brain, GP90 undergoes rapid synthesis between embryonic days 10 and 12. Unlike contactin, it is not restricted to nervous tissue and is quite abundant in gizzard, where there are two antigenically related proteins of 100K and 90K (K = 10(3) Mr). In both brain and gizzard GP90 and (GP100) are enriched in the membrane skeleton fraction. Trypsinization of live cells suggest that GP90 from gizzard is related to GP100 by the removal of a polypeptide chain. GP90 from both neurones and gizzard cells is protected from proteolysis by the presence of extracellular Ca2+. In the absence of Ca2+ a soluble fragment of approximately 70K can be released from the surface of cells indicating that a large fraction of GP90 is extracellular. Deglycosylation of GP90 from brain using endoglycosidase F demonstrates the presence of at least five carbohydrate chains and a polypeptide chain of approximately 80K. Immunofluorescence studies show that GP90 is exposed on the surface of cultured neurones, gizzard cells and most glial cells with the exception of Schwann cells. It is observed in clusters or patches even when cells are prefixed, suggesting this may be the normal distribution of GP90.


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[Abstract] [PDF]


© The Company of Biologists Ltd 1989