Insulin induces α1B-adrenergic receptor phosphorylation and desensitization
- 3 September 2004
- journal article
- research article
- Published by Elsevier in Life Sciences
- Vol. 75 (16) , 1937-1947
- https://doi.org/10.1016/j.lfs.2004.03.025
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- The Phosphoinositide 3-Kinase PathwayScience, 2002
- Akt Mediates Sequestration of the β2-Adrenergic Receptor in Response to InsulinJournal of Biological Chemistry, 2002
- Insulin Stimulates Phosphorylation of the β2-Adrenergic Receptor by the Insulin Receptor, Creating a Potent Feedback Inhibitor of Its Tyrosine KinaseJournal of Biological Chemistry, 2002
- Insulin Stimulates Sequestration of β-Adrenergic Receptors and Enhanced Association of β-Adrenergic Receptors with Grb2 via Tyrosine 350Journal of Biological Chemistry, 1998
- Crosstalk: phosphorylation of α1b‐adrenoceptors induced through activation of bradykinin B2 receptorsFEBS Letters, 1998
- The β-Adrenergic Receptor Is a Substrate for the Insulin Receptor Tyrosine KinaseJournal of Biological Chemistry, 1996
- Phosphorylation of Tyrosyl Residues 350/354 of the β-Adrenergic Receptor Is Obligatory for Counterregulatory Effects of InsulinJournal of Biological Chemistry, 1995
- Species heterogeneity of hepatic α1-adrenoceptors: α1A-, α1B- and α1C-subtypesBiochemical and Biophysical Research Communications, 1992
- α1-Adrenoceptor subtypes in aorta (α1A) and liver (α1B)European Journal of Pharmacology: Molecular Pharmacology, 1991
- Insulin-like effect of epidermal growth factor in isolated rat hepatocytesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1986