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J. Biol. Chem., Vol. 265, Issue 15, 8505-8510, 05, 1990
ZQ Sheng, SR Hull and KL Carraway
Cell surfaces of metastatic 13762 ascites rat mammary adenocarcinoma cells
are covered with a sialomucin complex composed of the high Mr sialomucin
ASGP-1 (approximately 600,000) and a concanavalin A-binding, integral
membrane glycoprotein ASGP-2 (120,000). Antibodies prepared against ASGP-2
and deglycosylated ASGP-1 react on immunoblots of ascites cells or their
isolated microvilli with the Mr = 120,000 species and the high Mr
sialomucin, respectively. No cross-reactivity was observed. Under complex
dissociating conditions, anti-ASGP-2 immunoprecipitated primarily
components of Mr = 120,000 and about 400,000 from lysates of cells labeled
for 1 h with mannose, glucosamine, and threonine. Under similar conditions,
anti-ASGP-1 immunoprecipitated the Mr = 400,000 component and a second
major labeled component of about 330,000. Pulse-chase labeling with 35S-
labeled amino acids followed by immunoprecipitation with anti-ASGP-2
indicated a precursor-product relationship for the Mr = 400,000 component,
designated pSMC-1 (precursor, sialomucin complex), and ASGP- 2. Similar
pulse-chase analyses of threonine-labeled cells using anti- ASGP-1 showed
equivalent amounts of immunoprecipitated pSMC-1 and pSMC- 2, both of which
disappeared with kinetics similar to those observed for pSMC-1
immunoprecipitated with anti-ASGP-2. A precursor-product relationship of
both pSMC-1 and pSMC-2 to ASGP-1 was suggested by combined precipitations
with anti-ASGP-1 and peanut agglutinin, which precipitates ASGP-1
specifically. Immunoblot and lectin blot analyses indicated that pSMC-1 and
pSMC-2 from the immunoprecipitates bind anti- ASGP-2, anti-ASGP-1, and
concanavalin A. Moreover, these three components can also be labeled with
mannose; the mannose was removed from 30-min pulse-labeled anti-ASGP-2
immunoprecipitates by incubation with endo-beta-N-acetylglucosaminidase H,
indicating the presence of only high mannose N-linked oligosaccharides in
pSMC-1. One-dimensional peptide maps of 35S-labeled pSMC-1 and Mr = 120,000
ASGP-2 showed several corresponding bands. These results indicate that both
ASGP-1 and ASGP-2 can be synthesized from a common high Mr precursor. We
propose that complex is formed from pSMC-1 by proteolytic cleavage to yield
Mr = 120,000 ASGP-2 plus the precursor to ASGP-1 early in the transit
pathway from the endoplasmic reticulum to the cell surface.
Biosynthesis of the cell surface sialomucin complex of ascites 13762 rat mammary adenocarcinoma cells from a high molecular weight precursor
Department of Cell Biology, University of Miami School of Medicine, Florida 33101.
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