This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Copyright Permission Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Goldstein, B. J. Articles by Dudley, A. L. Search for Related Content PubMed PubMed Citation Articles by Goldstein, B. J. Articles by Dudley, A. L.

The Rat Insulin Receptor: Primary Structure and Conservation of Tissue-Specific Alternative Messenger RNA Splicing

Research Division, Joslin Diabetes Center and Department of Medicine, Brigham and Women's Hospital, Harvard Medical School Boston Massachusetts 02215

Address requests for reprints to: Dr. Barry J. Goldstein, Joslin Diabetes Center, Research Division, One Joslin Place, Boston, Massachusetts 02215.

Abstract

To investigate whether alterations in the polypeptide structure of the insulin receptor might explain the heterogeneity observed in its properties between species and in different tissues, we obtained the complete primary structure of the rat liver insulin receptor precursor by cDNA cloning and sequencing. The rat proreceptor contains 1357 amino acids and has 95.2% identity with deduced polypeptide sequences reported for the human insulin receptor precursor. In addition, the rat liver insulin receptor cDNA was similar to the form of the human insulin receptor mRNA that contains Exon 11 in its coding region, which undergoes tissue-specific alternative splicing. Using the polymerase chain reaction to amplify a cDNA segment corresponding to this region in several rat tissues, the splicing pattern of sequences homologous to Exon 11 was found to be highly conserved, providing further evidence that these two forms of the insulin receptor may serve important functional or regulatory roles. These studies have also identified subtle variations in the primary structure of the insulin receptor which may influence its properties between species.

FOOTNOTES

This work was supported by NIH Grant DK-31036 and a Pilot and Feasibility Award from the Joslin Diabetes Endocrinology Research Center (DERC) Grant DK-36836.

^* Recipient of a research award from The Medical Foundation of Boston.

Received for publication November 7, 1989. Revision received November 7, 1989. Accepted for publication November 16, 1989.

This article has been cited by other articles:

				C. Nevado, M. Benito, and A. M. Valverde Role of Insulin Receptor and Balance in Insulin Receptor Isoforms A and B in Regulation of Apoptosis in Simian Virus 40-immortalized Neonatal Hepatocytes Mol. Biol. Cell, March 1, 2008; 19(3): 1185 - 1198. [Abstract] [Full Text] [PDF]

				R Serrano, M Villar, C Martinez, J M Carrascosa, N Gallardo, and A Andres Differential gene expression of insulin receptor isoforms A and B and insulin receptor substrates 1, 2 and 3 in rat tissues: modulation by aging and differentiation in rat adipose tissue J. Mol. Endocrinol., February 1, 2005; 34(1): 153 - 161. [Abstract] [Full Text] [PDF]

				R. V. S. Rajala and R. E. Anderson Interaction of the Insulin Receptor {beta}-Subunit with Phosphatidylinositol 3-Kinase in Bovine ROS Invest. Ophthalmol. Vis. Sci., December 1, 2001; 42(13): 3110 - 3117. [Abstract] [Full Text] [PDF]

				M. S. Chacko and M. L. Adamo Double-Stranded Ribonucleic Acid Decreases C6 Rat Glioma Cell Numbers: Effects on Insulin-Like Growth Factor I Gene Expression and Action Endocrinology, October 1, 2000; 141(10): 3546 - 3555. [Abstract] [Full Text] [PDF]

				D. M. Ney, D. J. Huss, M. B. Gillingham, K. R. Kritsch, E. M. Dahly, J. L. Talamantez, and M. L. Adamo Investigation of Insulin-Like Growth Factor (IGF)-I and Insulin Receptor Binding and Expression in Jejunum of Parenterally Fed Rats Treated with IGF-I or Growth Hormone Endocrinology, October 1, 1999; 140(10): 4850 - 4860. [Abstract] [Full Text]

				L. G. Sparrow, N. M. McKern, J. J. Gorman, P. M. Strike, C. P. Robinson, J. D. Bentley, and C. W. Ward The Disulfide Bonds in the C-terminal Domains of the Human Insulin Receptor Ectodomain J. Biol. Chem., November 21, 1997; 272(47): 29460 - 29467. [Abstract] [Full Text] [PDF]

				S. Bortoli, M. Amessou, M. Collinet, B. Desbuquois, and S. Lopez Vanadate, But Not Insulin, Inhibits Insulin Receptor Gene Expression in Rat Hepatoma Cells Endocrinology, November 1, 1997; 138(11): 4821 - 4829. [Abstract] [Full Text] [PDF]

				H. K. Kole, A. S. Liotta, S. Kole, J. Roth, C. Montrose-Rafizadeh, and M. Bernier A Synthetic Peptide Derived from a COOH-terminal Domain of the Insulin Receptor Specifically Enhances Insulin Receptor Signaling J. Biol. Chem., December 6, 1996; 271(49): 31619 - 31626. [Abstract] [Full Text] [PDF]

				L. A. Sechi, C. A. Griffin, G. Giacchetti, L. Zingaro, C. Catena, E. Bartoli, and M. Schambelan Abnormalities of Insulin Receptors in Spontaneously Hypertensive Rats Hypertension, April 1, 1996; 27(4): 955 - 961. [Abstract] [Full Text]

				A. Kosaki, T. S. Pillay, L. Xu, and N. J. G. Webster The B Isoform of the Insulin Receptor Signals More Efficiently Than the A Isoform in HepG2 Cells J. Biol. Chem., September 1, 1995; 270(35): 20816 - 20823. [Abstract] [Full Text] [PDF]