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Volume 272, Number 2, Issue of January 10, 1997 pp. 821-827
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Synaptic Membrane Glycoproteins gp65 and gp55 Are New Members of the Immunoglobulin Superfamily

(Received for publication, September 4, 1996, and in revised form, October 23, 1996)

Kristina Langnaese , Philip W. Beesley and Eckart D. Gundelfinger

From the Department of Neurochemistry and Molecular Biology, Federal Institute for Neurobiology, D-39008 Magdeburg, Germany and the  Division of Biochemistry, School of Biological Sciences, Royal Holloway University of London, Egham, Surrey TW20 0EX, United Kingdom

Glycoproteins gp65 and gp55 are major components of synaptic membranes prepared from rat forebrain. Both are recognized by the monoclonal antibody SMgp65. We have used SMgp65 to screen a rat brain cDNA expression library. Two sets of overlapping cDNAs that contain open reading frames of 397 and 281 amino acids were isolated. The deduced proteins are members of the immunoglobulin (Ig) superfamily containing three and two Ig domains, respectively. The common part has ~40% sequence identity with neurothelin/basigin. The identity of the proteins as gp65 and gp55 was confirmed by production of new antisera against a common recombinant protein fragment. These antisera immunoprecipitate gp65 and gp55. Furthermore, expression of gp65 and gp55 cDNAs in human 293 cells treated with tunicamycin results in the production of unglycosylated core proteins of identical size to deglycosylated gp65 and gp55. Northern analysis revealed that gp65 transcripts are brain-specific, whereas gp55 is expressed in most tissues and cell lines examined. The tissue distribution was confirmed at the protein level though the pattern of glycosylation of gp55 varies between tissues. In situ hybridization experiments with a common and a gp65-specific probe suggest differential expression of gp65 and gp55 transcripts in the rat brain.

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