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(Received for publication, April 4, 1996, and in revised form, October 17, 1996)
From the Dorrance H. Hamilton Research Laboratories, Division of
Endocrinology, Diabetes and Metabolic Diseases, Department of Medicine,
Jefferson Medical College of Thomas Jefferson University,
Philadelphia, Pennsylvania 19107
The receptor-type protein-tyrosine phosphatase
LAR (for
Volume 272, Number 1,
Issue of January 3, 1997
pp. 448-457
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
eukocyte common
ntigen-
elated) has been implicated as a
physiological regulator of the insulin receptor. To demonstrate a
functional interaction between LAR and the insulin receptor, we
incubated CHO cells overexpressing the human insulin receptor with an
antibody to the extracellular domain of LAR and found a 47% decrease
in insulin receptor autophosphorylation and kinase activity. A physical association between LAR and the insulin receptor was then shown by
immunoprecipitation of LAR from cell lysates and immunoblotting with
antibody to the insulin receptor, or vice versa. Up to
11.8% of the LAR protein in the lysates of CHO cells overexpressing both the insulin receptor and LAR co-immunoprecipitated with the insulin receptor. The LAR/insulin receptor association was related to
the level of LAR or insulin receptor overexpression and was increased
6.5-fold by chemical cross-linking and 3.9-fold by treatment with
insulin, suggesting that receptor activation influences the affinity of
LAR for the insulin receptor. In insulin-stimulated rat liver, LAR was
temporally enriched in endosomes with the insulin receptor, and
incubation of endosomes with neutralizing LAR antibodies decreased
insulin receptor dephosphorylation in situ by 28%
(p = 0.01 versus control). These data
provide more direct evidence of a role for LAR in the physiological
regulation of insulin action at the receptor level.
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