Sialomucin complex, a heterodimeric glycoprotein complex: Expression as a soluble, secretable form in lactating mammary gland and colon

Edmund A. Rossi, Richard R. McNeer, Shari A. Price-Schiavi, Jan M H Van den Brande, Masanobu Komatsu, John F. Thompson, Coralie A. Carothers Carraway, Nevis L. Fregien, Kermit L. Carraway

Research output: Contribution to journalArticle

103 Citations (Scopus)

Abstract

Ascites 13762 rat mammary adenocarcinoma cells express abundantly on their cell surfaces a heterodimeric glycoprotein complex composed of a sialomucin ascites sialoglycoprotein (ASGP)-I and a transmembrane subunit ASGP-2. The latter, which contains two epidermal growth factor-like domains, binds the receptor tyrosine kinase p185(neu), 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 M(r), antigenicity, and association with ASGP-1. The presence of ASGP-1 in milk suggests that it is a candidate for the uncharacterized high M(r) 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.

Original languageEnglish (US)
Pages (from-to)33476-33485
Number of pages10
JournalJournal of Biological Chemistry
Volume271
Issue number52
DOIs
StatePublished - 1996
Externally publishedYes

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Mucin-4
Sialomucins
Human Mammary Glands
Glycoproteins
Colon
Ascites
Rats
Milk
Membranes
Adenocarcinoma
Breast
Sialoglycoproteins
Physiology
Receptor Protein-Tyrosine Kinases
Mucins
Epidermal Growth Factor
Tumors

ASJC Scopus subject areas

  • Biochemistry

Cite this

Sialomucin complex, a heterodimeric glycoprotein complex : Expression as a soluble, secretable form in lactating mammary gland and colon. / Rossi, Edmund A.; McNeer, Richard R.; Price-Schiavi, Shari A.; Van den Brande, Jan M H; Komatsu, Masanobu; Thompson, John F.; Carothers Carraway, Coralie A.; Fregien, Nevis L.; Carraway, Kermit L.

In: Journal of Biological Chemistry, Vol. 271, No. 52, 1996, p. 33476-33485.

Research output: Contribution to journalArticle

Rossi, EA, McNeer, RR, Price-Schiavi, SA, Van den Brande, JMH, Komatsu, M, Thompson, JF, Carothers Carraway, CA, Fregien, NL & Carraway, KL 1996, 'Sialomucin complex, a heterodimeric glycoprotein complex: Expression as a soluble, secretable form in lactating mammary gland and colon', Journal of Biological Chemistry, vol. 271, no. 52, pp. 33476-33485. https://doi.org/10.1074/jbc.271.52.33476
Rossi, Edmund A. ; McNeer, Richard R. ; Price-Schiavi, Shari A. ; Van den Brande, Jan M H ; Komatsu, Masanobu ; Thompson, John F. ; Carothers Carraway, Coralie A. ; Fregien, Nevis L. ; Carraway, Kermit L. / Sialomucin complex, a heterodimeric glycoprotein complex : Expression as a soluble, secretable form in lactating mammary gland and colon. In: Journal of Biological Chemistry. 1996 ; Vol. 271, No. 52. pp. 33476-33485.
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abstract = "Ascites 13762 rat mammary adenocarcinoma cells express abundantly on their cell surfaces a heterodimeric glycoprotein complex composed of a sialomucin ascites sialoglycoprotein (ASGP)-I and a transmembrane subunit ASGP-2. The latter, which contains two epidermal growth factor-like domains, binds the receptor tyrosine kinase p185(neu), 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 M(r), antigenicity, and association with ASGP-1. The presence of ASGP-1 in milk suggests that it is a candidate for the uncharacterized high M(r) 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.",
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AU - Van den Brande, Jan M H

AU - Komatsu, Masanobu

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