Insulin Receptor Phosphorylation May not be a Prerequisite for Acute Insulin Action

An antiserum to the insulin receptor mimicked insulin's acute actions on glucose transport, phosphorylation of integral membrane proteins, and internalization of the insulin receptor in isolated rat adipose cells. These insulinomimetic actions of the antiserum occurred without the equivalent in...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1984-03, Vol.223 (4642), p.1301-1304
Main Authors: Simpson, Ian A., Hedo, José A.
Format: Article
Language:English
Subjects:
3-O-Methylglucose
Adipose Tissue - cytology
Animals
Antiserum
Bicarbonates
Biological and medical sciences
Biological Transport
Cell Membrane - metabolism
Cell membranes
Cell physiology
Diabetes
Diabetes research
Endocrinology, Experimental
Fundamental and applied biological sciences. Psychology
Gels
Hormonal regulation
Immune Sera
Insulin
Insulin - metabolism
Insulin - pharmacology
Internalization
Membrane Proteins - metabolism
Methylglucosides - metabolism
Microsomes
Molecular and cellular biology
Phosphorylation
Physiological aspects
Rats
Receptor, Insulin - immunology
Receptor, Insulin - metabolism
Receptors
Serum albumins
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Summary:An antiserum to the insulin receptor mimicked insulin's acute actions on glucose transport, phosphorylation of integral membrane proteins, and internalization of the insulin receptor in isolated rat adipose cells. These insulinomimetic actions of the antiserum occurred without the equivalent increase in phosphorylation of the β subunit of the insulin receptor observed with insulin. Thus, a role of receptor phosphorylation in acute insulin action is now questioned.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.6367041