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(Received for publication, February 9, 1996, and in revised form, September 3, 1996)
From the Departments of Ascites 13762 rat mammary
adenocarcinoma cells express abundantly on their cell surfaces a
heterodimeric glycoprotein complex composed of a sialomucin ascites
sialoglycoprotein (ASGP)-1 and a transmembrane subunit ASGP-2. The
latter, which contains two epidermal growth factor-like domains, binds
the receptor tyrosine kinase p185neu, suggesting that the
complex is bifunctional as well as heterodimeric. Immunoblot analyses
using monoclonal antibodies prepared against the complex demonstrate
high levels of expression in rat lactating mammary gland and colon.
Immunolocalization studies with anti-ASGP-2 indicate that ASGP-2 is
present in these two tissues in the apical regions of secretory
epithelial cells. Both mammary gland and colon contain a soluble,
secretable form of ASGP-2, which is not found in the ascites cells;
milk and mammary gland also have the membrane form. Immunoblot analyses
using a COOH-terminal-specific polyclonal antibody indicate that the
soluble form of ASGP-2 is missing its COOH-terminal domains. Both the
soluble and membrane forms of ASGP-2 are similar to the
membrane-associated form from the 13762 adenocarcinoma with respect to
Mr, antigenicity, and association with ASGP-1.
The presence of ASGP-1 in milk suggests that it is a candidate for the
uncharacterized high Mr milk mucin, MUCX.
ASGP-2 expression is up-regulated in mammary gland during pregnancy,
because it is undetectable in virgin and early pregnant rats but
abundant in the gland from late pregnant and lactating animals.
However, compared with the lactating mammary gland, the 13762 ascites
cells overexpress ASGP-2 by more than 100-fold, which may contribute to
their malignancy. These combined results indicate that sialomucin
complex is a unique secreted product in the mammary gland and colon,
whose behavior is different from that in the mammary ascites tumors,
and which may play important roles in mammary and intestinal
physiology.
Volume 271, Number 52,
Issue of December 27, 1996
pp. 33476-33485
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
EXPRESSION AS A SOLUBLE, SECRETABLE FORM IN LACTATING MAMMARY
GLAND AND COLON
,
,
,
,
,
and
Cell Biology and Anatomy,
§ Pediatrics, and 
Biochemistry and Molecular
Biology, University of Miami School of Medicine,
Miami, Florida 33101
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