Insulin Receptor Antiserum and Plant Lectins Mimic the Direct Effects of Insulin on Nuclear Envelope Phosphorylation
Authors:
- 29 July 1983
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 221 (4609) , 462-464
Abstract
Insulin directly inhibits protein phosphorylation in isolated rat liver nuclear envelopes. In the present studies, an antiserum to insulin receptor as well as the plant lectins concanavalin A and phytohemagglutinin mimicked insulin action in isolated nuclear envelopes. These studies suggest that insulin and agents that mimic it may directly regulate nuclear functions.Keywords
This publication has 41 references indexed in Scilit:
- Insulin Stimulation of Nucleoside Triphosphatase Activity in Isolated Nuclear EnvelopesScience, 1982
- Insulin stimulates the release from liver plasma membranes of a chemical modulator of pyruvate dehydrogenaseBiochemical and Biophysical Research Communications, 1981
- Autoantibodies to insulin receptorsMolecular and Cellular Endocrinology, 1981
- Pertinence of nuclear envelope nucleoside triphosphatase activity to ribonucleic acid transportBiochemistry, 1980
- Insulin-receptor antibodies mimic a late insulin effectNature, 1979
- Selective phosphorylation of a nuclear envelope polypeptide by an endogenous protein kinaseBiochemistry, 1979
- Identification of Concanavalin A binding glycoproteins of rat liver cell nuclear membranesBiochemical and Biophysical Research Communications, 1977
- EGTA and proteinase reversal of cellular aggregation of activated lymphocytesNature, 1976
- LIGAND-INDUCED MOVEMENT OF LYMPHOCYTE MEMBRANE MACROMOLECULESJournal of Experimental Medicine, 1972
- FRACTIONATION OF THE NUCLEUS BY DIVALENT CATIONSJournal of Cell Biology, 1972