Identification of pp120, an endogenous substrate for the hepatocyte insulin receptor tyrosine kinase, as an integral membrane glycoprotein of the bile canalicular domain

R. N. Margolis, S. I. Taylor, D. Seminara, Ann Louise Hubbard

Research output: Contribution to journalArticle

Abstract

An endogenous membrane-bound substrate of the insulin receptor β-subunit tyrosine kinase in liver, pp120, has been identified as HA4, a 110-kDa membrane glycoprotein localized primarily to the bile canalicular domain of the hepatocyte. HA4 has been implicated in bile salt transport and cell adhesion. Monoclonal antibodies to HA4 were used to identify it as a substrate of the insulin receptor kinase. Anti-pp120 and anti-HA4 were found to cross-react, and phosphopeptide maps for each of the corresponding antigens were identical. The identification of the pp120 as HA4 serves to link insulin action through the receptor tyrosine kinase activity to bile metabolism and raises questions pertaining to the intracellular site(s) of action of the insulin receptor.

Original languageEnglish (US)
Pages (from-to)7256-7259
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number19
StatePublished - 1988
Externally publishedYes

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Focal Adhesion Kinase 1
Insulin Receptor
Membrane Glycoproteins
Bile
Hepatocytes
Phosphopeptides
Receptor Protein-Tyrosine Kinases
Bile Acids and Salts
Cell Adhesion
Phosphotransferases
Monoclonal Antibodies
Insulin
Antigens
Membranes
Liver
insulin receptor tyrosine kinase

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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title = "Identification of pp120, an endogenous substrate for the hepatocyte insulin receptor tyrosine kinase, as an integral membrane glycoprotein of the bile canalicular domain",
abstract = "An endogenous membrane-bound substrate of the insulin receptor β-subunit tyrosine kinase in liver, pp120, has been identified as HA4, a 110-kDa membrane glycoprotein localized primarily to the bile canalicular domain of the hepatocyte. HA4 has been implicated in bile salt transport and cell adhesion. Monoclonal antibodies to HA4 were used to identify it as a substrate of the insulin receptor kinase. Anti-pp120 and anti-HA4 were found to cross-react, and phosphopeptide maps for each of the corresponding antigens were identical. The identification of the pp120 as HA4 serves to link insulin action through the receptor tyrosine kinase activity to bile metabolism and raises questions pertaining to the intracellular site(s) of action of the insulin receptor.",
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year = "1988",
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T1 - Identification of pp120, an endogenous substrate for the hepatocyte insulin receptor tyrosine kinase, as an integral membrane glycoprotein of the bile canalicular domain

AU - Margolis, R. N.

AU - Taylor, S. I.

AU - Seminara, D.

AU - Hubbard, Ann Louise

PY - 1988

Y1 - 1988

N2 - An endogenous membrane-bound substrate of the insulin receptor β-subunit tyrosine kinase in liver, pp120, has been identified as HA4, a 110-kDa membrane glycoprotein localized primarily to the bile canalicular domain of the hepatocyte. HA4 has been implicated in bile salt transport and cell adhesion. Monoclonal antibodies to HA4 were used to identify it as a substrate of the insulin receptor kinase. Anti-pp120 and anti-HA4 were found to cross-react, and phosphopeptide maps for each of the corresponding antigens were identical. The identification of the pp120 as HA4 serves to link insulin action through the receptor tyrosine kinase activity to bile metabolism and raises questions pertaining to the intracellular site(s) of action of the insulin receptor.

AB - An endogenous membrane-bound substrate of the insulin receptor β-subunit tyrosine kinase in liver, pp120, has been identified as HA4, a 110-kDa membrane glycoprotein localized primarily to the bile canalicular domain of the hepatocyte. HA4 has been implicated in bile salt transport and cell adhesion. Monoclonal antibodies to HA4 were used to identify it as a substrate of the insulin receptor kinase. Anti-pp120 and anti-HA4 were found to cross-react, and phosphopeptide maps for each of the corresponding antigens were identical. The identification of the pp120 as HA4 serves to link insulin action through the receptor tyrosine kinase activity to bile metabolism and raises questions pertaining to the intracellular site(s) of action of the insulin receptor.

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