Role of PC-1 in the etiology of insulin resistance.

作者: IRA D. GOLDFINE , BETTY A. MADDUX , JACK F. YOUNGREN , VINCENZO TRISCHITTA , LUCIA FRITTITTA

DOI: 10.1111/J.1749-6632.1999.TB07797.X

关键词:

摘要: : Defects in insulin receptor tyrosine kinase activity have been demonstrated tissues from resistant subjects, but mutations the gene are rare. Therefore, other molecules that capable of modulating most likely play a major role resistance. In cultured fibroblasts an patient with Type 2 diabetes, we first identified membrane glycoprotein PC-1 as inhibitor activity. is overexpressed both and without diabetes. large class II exoprotein whose function unknown. Studies muscle fat two primary for activation, reveal elevated levels inversely correlated decreased action vivo vitro. Transfection expression cells demonstrate overexpression produces impairments activity, subsequent cellular responses to insulin. These studies indicate, therefore, factor etiology resistance, potential new therapeutic target antidiabetic therapy.

参考文章(63)
B Obermaier-Kusser, M F White, D E Pongratz, Z Su, B Ermel, C Muhlbacher, H U Haring, A defective intramolecular autoactivation cascade may cause the reduced kinase activity of the skeletal muscle insulin receptor from patients with non-insulin-dependent diabetes mellitus. Journal of Biological Chemistry. ,vol. 264, pp. 9497- 9504 ,(1989) , 10.1016/S0021-9258(18)60559-9
M F Buckley, K A Loveland, W J McKinstry, O M Garson, J W Goding, Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. Journal of Biological Chemistry. ,vol. 265, pp. 17506- 17511 ,(1990) , 10.1016/S0021-9258(18)38193-6
Y. Oda, M.D. Kuo, S.S. Huang, J.S. Huang, The plasma cell membrane glycoprotein, PC-1, is a threonine-specific protein kinase stimulated by acidic fibroblast growth factor. Journal of Biological Chemistry. ,vol. 266, pp. 16791- 16795 ,(1991) , 10.1016/S0021-9258(18)55370-9
I.R. van Driel, J.W. Goding, Plasma cell membrane glycoprotein PC-1. Primary structure deduced from cDNA clones. Journal of Biological Chemistry. ,vol. 262, pp. 4882- 4887 ,(1987) , 10.1016/S0021-9258(18)61278-5
Barry J. Goldstein, Pei-Ming Li, Wendi Ding, Faiyaz Ahmad, Wei-Ren Zhang, Regulation of insulin action by protein tyrosine phosphatases. Vitamins and Hormones Series. ,vol. 54, pp. 67- 96 ,(1998) , 10.1016/S0083-6729(08)60922-X
Ira D. Goldfine, Giuseppe Damante, Martha R. Stampfer, Francesco Giorgino, Riccardo Vigneri, Giovanni Milazzo, Antonino Belfiore, Chin Sung, Insulin Receptor Expression and Function in Human Breast Cancer Cell Lines Cancer Research. ,vol. 52, pp. 3924- 3930 ,(1992)
C Arrieumerlou, P Deterre, L Gelman, G Bismuth, J Goding, J M Tixier, S Ktorza, H Gary-Gouy, C Schmitt, V Berthelier, Coordinated regulation in human T cells of nucleotide-hydrolyzing ecto-enzymatic activities, including CD38 and PC-1. Possible role in the recycling of nicotinamide adenine dinucleotide metabolites. Journal of Immunology. ,vol. 157, pp. 1381- 1388 ,(1996)
Cristiana Stefan, Willy Stalmans, Mathieu Bollen, Growth-related expression of the ectonucleotide pyrophosphatase PC-1 in rat liver. Hepatology. ,vol. 28, pp. 1497- 1503 ,(1998) , 10.1002/HEP.510280608
James W Goding, Robert Terkeltaub, Michele Maurice, Philippe Deterre, Adnan Sali, Sabina I. Belli, Ecto-phosphodiesterase/pyrophosphatase of lymphocytes and non-lymphoid cells: structure and function of the PC-1 family. Immunological Reviews. ,vol. 161, pp. 11- 26 ,(1998) , 10.1111/J.1600-065X.1998.TB01568.X