The role of membrane glycoprotein plasma cell antigen 1 ectonucleotide pyrophosphatase phosphodiesterase 1 in the pathogenesis of insulin resistance and related abnormalities (1197 views)
Endocrine Reviews (ISSN: 0163-769x), 2008 Feb; 29(1): 62-75.
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Paper type: Journal Article,
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Keywords: Cell Membrane Protein, Ectonucleotide Pyrophosphatase Phosphodiesterase 1, Insulin Receptor, Membrane Glycoprotein Plasma Cell Antigen 1, Protein Tyrosine Kinase, Unclassified Drug, Adipose Tissue, Binding Affinity, Cardiovascular System Examination, Enzyme Activation, Fibroblast, Human, Insulin Binding, Insulin Resistance, Non Insulin Dependent Diabetes Mellitus, Nonhuman, Obesity, Pathogenesis, Priority Journal, Protein Binding, Protein Expression, Protein Function, Protein Phosphorylation, Protein Polymorphism, Protein Structure, Review, Transgenic Mouse, Wild Type, Animals, Diabetes Complications, Disease Models, Female, Gene Expression, Phosphoric Diester Hydrolases, Polycystic Ovary Syndrome, Genetic, Quaternary, Variation (genetics),
Affiliations:
*** IBB - CNR ***
Department of Medicine and Diabetes Center, University of California, San Francisco, CA 94115, United States
Division of Cardiovascular Medicine, Stanford University School of Medicine, Stanford, CA 94305, United States
Diabetes Center, Columbia University, New York, NY 10032, United States
Department of Clinical Sciences, Sapienza University, 00198 Rome, Italy
Research Unit of Diabetes and Endocrinology, Scientific Institute Casa Sollievo Della Sofferenza, 71013 San Giovanni Rotondo, Italy
Endocrinologia, Ospedale Garibaldi, University of Catania, 95122 Catania, Italy
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Maddux, B.A., Goldfine, I.D., Membrane glycoprotein PC-1 inhibition of insulin receptor function occurs via direct interaction with the receptor α-subunit (2000) Diabetes, 49, pp. 13-19
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Reaven, G. M., Role of insulin resistance in human disease (1988) Diabetes, 37, pp. 1595-1607
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Maddux, B. A., Sbraccia, P., Kumakura, S., Sasson, S., Youngren, J. F., Fisher, A., Spencer, S., Goldfine, I., Membrane glycoprotein PC-1 and insulin resistance in non-insulin-dependent diabetes mellitus (1995) Nature, 373, pp. 448-451
Goding, J. W., Grobben, B., Slegers, H., Physiological and pathophysiological functions of the ecto-nucleotide pyrophosphatase/ phosphodiesterase family (2003) Biochim Biophys Acta, 1638, pp. 1-19
Goding, J. W., Terkeltaub, R., Maurice, M., Deterre, P., Sali, A., Belli, S. I., Ecto-phosphodiesterase/pyrophosphatase of lymphocytes and non-lymphoid cells: Structure and function of the PC-1 family (1998) Immunol Rev, 161, pp. 11-26
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Weedon, M. N., Shields, B., Hitman, G., Walker, M., McCarthy, M. I., Hattersley, A. T., Frayling, T. M., No evidence of association of ENPP1 variants with type 2 diabetes or obesity in a study of 8, 089 U. K. Caucasians (2006) Diabetes, 55, pp. 3175-3179
Harris, M. I., Flegal, K. M., Cowie, C. C., Eberhardt, M. S., Goldstein, D. E., Little, R. R., Wiedmeyer, H. M., Byrd-Holt, D. D., Prevalence of diabetes, impaired fasting glucose, and impaired glucose tolerance in U. S. adults (1998) The Third National Health and Nutrition Examination Survey, 1988-1994. Diabetes Care, 21, pp. 518-524
Willer, C. J., Bonnycastle, L. L., Conneely, K. N., Duren, W. L., Jackson, A. U., Scott, L. J., Narisu, N., Boehnke, M., Screening of 134 single nucleotide polymorphisms (SNPs) previously associated with type 2 diabetes replicates association with 12 SNPs in nine genes (2007) Diabetes, 56, pp. 256-264
Bruning, J. C., Gautam, D., Burks, D. J., Gillette, J., Schubert, M., Orban, P. C., Klein, R., Kahn, C. R., Role of brain insulin receptor in control of body weight and reproduction (2000) Science, 289, pp. 2122-2125
Swinburn, B. A., Nyomba, B. L., Saad, M. F., Zurlo, F., Raz, I., Knowler, W. C., Lillioja, S., Ravussin, E., Insulin resistance associated with lower rates of weight gain in Pima Indians (1991) J Clin Invest, 88, pp. 168-173
Nicklas, B. J., van Rossum, E. F., Berman, D. M., Ryan, A. S., Dennis, K. E., Shuldiner, A. R., Genetic variation in the peroxisome proliferator-activated receptor- 2 gene (Pro12Ala) affects metabolic responses to weight loss and subsequent weight regain (2001) Diabetes, 50, pp. 2172-2176
Clausen, J. O., Hansen, T., Bjorbaek, C., Echwald, S. A., Urhammer, S. A., Rasmussen, S., Andersen, C. B., Pedersen, O., Insulin resistance: Interactions between obesity and a common variant of insulin receptor substrate-1 (1995) Lancet, 346, pp. 397-402
Yip, C. C., Ottensmeyer, P., Three-dimensional structural interactions of insulin and its receptor (2003) J Biol Chem, 278, pp. 27329-27332
Luo, R. Z., Beniac, D. R., Fernandes, A., Yip, C. C., Ottensmeyer, F. P., Quaternary structure of the insulin-insulin receptor complex (1999) Science, 285, pp. 1077-1080
Maddux, B. A., Goldfine, I. D., Membrane glycoprotein PC-1 inhibition of insulin receptor function occurs via direct interaction with the receptor -subunit (2000) Diabetes, 49, pp. 13-19
Endocrine Reviews (ISSN: 0163-769x), 2008 Feb; 29(1): 62-75.
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Paper type: Journal Article,
Impact factor: 18.562, 5-year impact factor: 24.444
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-39149099952&partnerID=40&md5=8056751abdb7902ef7b5396be51e9351
Keywords: Cell Membrane Protein, Ectonucleotide Pyrophosphatase Phosphodiesterase 1, Insulin Receptor, Membrane Glycoprotein Plasma Cell Antigen 1, Protein Tyrosine Kinase, Unclassified Drug, Adipose Tissue, Binding Affinity, Cardiovascular System Examination, Enzyme Activation, Fibroblast, Human, Insulin Binding, Insulin Resistance, Non Insulin Dependent Diabetes Mellitus, Nonhuman, Obesity, Pathogenesis, Priority Journal, Protein Binding, Protein Expression, Protein Function, Protein Phosphorylation, Protein Polymorphism, Protein Structure, Review, Transgenic Mouse, Wild Type, Animals, Diabetes Complications, Disease Models, Female, Gene Expression, Phosphoric Diester Hydrolases, Polycystic Ovary Syndrome, Genetic, Quaternary, Variation (genetics),
Affiliations:
*** IBB - CNR ***
Department of Medicine and Diabetes Center, University of California, San Francisco, CA 94115, United States
Division of Cardiovascular Medicine, Stanford University School of Medicine, Stanford, CA 94305, United States
Diabetes Center, Columbia University, New York, NY 10032, United States
Department of Clinical Sciences, Sapienza University, 00198 Rome, Italy
Research Unit of Diabetes and Endocrinology, Scientific Institute Casa Sollievo Della Sofferenza, 71013 San Giovanni Rotondo, Italy
Endocrinologia, Ospedale Garibaldi, University of Catania, 95122 Catania, Italy
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The role of membrane glycoprotein plasma cell antigen 1 ectonucleotide pyrophosphatase phosphodiesterase 1 in the pathogenesis of insulin resistance and related abnormalities
Insulin resistance is a major feature of most patients with type 2 diabetes mellitus (T2D). A number of laboratories have observed that membrane glycoprotein plasma cell antigen 1 (PC-1) [ ectonucleotide pyrophosphatase phosphodiesterase 1] is either overexpressed or overactive in muscle, adipose tissue, fibroblasts, and other tissues of insulin-resistant individuals, both nondiabetic and diabetic. Moreover, in cultured cells in vitro and in transgenic mice in vivo, PC-1 overexpression impairs insulin stimulation of insulin receptor (IR) activation and downstream signaling. PC-1 binds to the connecting domain of the IR alpha-subunit that is located in residues 485-599. The connecting domain transmits insulin binding the alpha- subunit to activation of tyrosine kinase activation in the beta- subunit. When PC-1 is overexpressed, it inhibits insulin-induced IR beta- subunit tyrosine kinase activity. In addition, a polymorphism of PC-1 ( K121Q) in various ethnic populations is closely associated with insulin resistance, T2D, and cardio-and nephrovascular diseases. The product of this polymorphism has a 2- to 3-fold increased binding affinity for the IR and is more potent than the wild-type PC-1 protein ( K121K) in inhibiting the IR. These data suggest therefore that PC-1 is a candidate protein that may play a role in human insulin resistance and T2D by its overexpression, its overactivity, or both.
Insulin resistance is a major feature of most patients with type 2 diabetes mellitus (T2D). A number of laboratories have observed that membrane glycoprotein plasma cell antigen 1 (PC-1) [ ectonucleotide pyrophosphatase phosphodiesterase 1] is either overexpressed or overactive in muscle, adipose tissue, fibroblasts, and other tissues of insulin-resistant individuals, both nondiabetic and diabetic. Moreover, in cultured cells in vitro and in transgenic mice in vivo, PC-1 overexpression impairs insulin stimulation of insulin receptor (IR) activation and downstream signaling. PC-1 binds to the connecting domain of the IR alpha-subunit that is located in residues 485-599. The connecting domain transmits insulin binding the alpha- subunit to activation of tyrosine kinase activation in the beta- subunit. When PC-1 is overexpressed, it inhibits insulin-induced IR beta- subunit tyrosine kinase activity. In addition, a polymorphism of PC-1 ( K121Q) in various ethnic populations is closely associated with insulin resistance, T2D, and cardio-and nephrovascular diseases. The product of this polymorphism has a 2- to 3-fold increased binding affinity for the IR and is more potent than the wild-type PC-1 protein ( K121K) in inhibiting the IR. These data suggest therefore that PC-1 is a candidate protein that may play a role in human insulin resistance and T2D by its overexpression, its overactivity, or both.
The role of membrane glycoprotein plasma cell antigen 1 ectonucleotide pyrophosphatase phosphodiesterase 1 in the pathogenesis of insulin resistance and related abnormalities
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The role of membrane glycoprotein plasma cell antigen 1 ectonucleotide pyrophosphatase phosphodiesterase 1 in the pathogenesis of insulin resistance and related abnormalities
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 28.878
View Export to BibTeX Export to EndNote
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Breast Cancer Res Tr Kluwer Academic Publishers (ISSN: 0167-6806), 1993; 25(1): 73-82.
Impact Factor: 2.43
View Export to BibTeX Export to EndNote
Papa V, Reese CC, Brunetti A, Vigneri R, Siiteri PK, Goldfine ID
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Cancer Res (ISSN: 0008-5472, 1538-7445, 1538-7445electronic), 1990 Dec 15; 50(24): 7858-7862.
Impact Factor: 8.426
View Export to BibTeX Export to EndNote
Trischitta V, Brunetti A, Chiavetta A, Benzi L, Papa V, Vigneri R
Defects in insulin-receptor internalization and processing in monocytes of obese subjects and obese NIDDM patients (314 views)
Diabetesdiabetes (ISSN: 0012-1797), 1989 Dec; 38(12): 1579-1584.
Impact Factor: 8.675
View Export to BibTeX Export to EndNote
Pezzino V, Papa V, Trischitta V, Brunetti A, Goodman PA, Treutelaar MK, Williams JA, Maddux BA, Vigneri R, Goldfine ID
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Am J Physiol Endocrinol Metab (ISSN: 0002-9513), 1989 Sep; 257(3): N/D-N/D.
Impact Factor: 3.116
View Export to BibTeX Export to EndNote
Trischitta V, Wong KY, Brunetti A, Scalisi R, Vigneri R, Goldfine ID
Endocytosis, recycling, and degradation of the insulin receptor. Studies with monoclonal antireceptor antibodies that do not activate receptor kinase (316 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 1989 Mar 25; 264(9): 5041-5046.
Impact Factor: 6.963
View Export to BibTeX Export to EndNote
21 Records (17 excluding Abstracts).
Total impact factor: 141.737 (128.267 excluding Abstracts).
Total 5 year impact factor: 130.386 (123.767 excluding Abstracts).
Total impact factor: 141.737 (128.267 excluding Abstracts).
Total 5 year impact factor: 130.386 (123.767 excluding Abstracts).
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