Phosphoprotein target for insulin and its antagonists

Details Phosphoprotein target for insulin and its antagonists Phosphoprotein target for insulin and its antagonists

2005-04-26

2005-04-26

Carlson, Karen Cochrane (Department: 1653)

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Reexamination Certificate

active

06884575

ABSTRACT:
The invention provides methods for diagnosing and treating individuals with insulin resistance.

REFERENCES:
Wang et al., “Insulin And Insulin Antagonists Evoke Phosphorylation Of P20 at Serine 157 and Serine 16 Respectively in Rat Skeletal Muscle”, FEBS Letters 462 (1999) 25-30.
Wang et al., “Amylin Evokes Phosphorylation of P20 in Rat Skeletal Muscle”, FEBS Letters 457 (1999) 149-152.
Wang et al., “Phosphorylation of P20 Is Associated with the Actions of Insulin in Rat Skeletal and Smooth Muscle”, Biochem. J. (1999) 344, 971-976 (Printed in Great Britain).
Wang et al., “Alteration in Phosphorylation of P20 Is Associated with Insulin Resistance”, Diabetes, vol. 50, Aug. 2001, 1821-1827.
Andrews, R.C. and Walker, B.R. (1999). “Glucocorticoids and insulin resistance: old hormones, new targets,”Clin. Sci. 96:513-523.
Beall, A.C. et al. (1997). “Cyclic nucleotide-dependent vasorelaxation is associated with the phosphorylation of a small heat shock-related protein,”J. Biol. Chem. 272:11283-11287.
Bergman, R.N. et al. (1985). “Assessment of insulin sensitivity in vivo,”Endocrine Review6:45-86.
Bjornholm, M. et al. (1997). “Insulin receptor susbstrate-1 phosphorylation and phosphatidylinositol 3-kinase activity in skeletal muscle from NIDDM subjects after in vivo insulin stimulation,”Diabetes46:524-527.
Bjorntorp, P. (1999). “Neuroendocrine perturbations as a cause of insulin resistance,”Diabet/Metab Res. Rev. 15:427-441.
Boden, G. (1998). “Free fatty acids (FFA), a link between obesity and insulin resistance,”Front. Biosci. 3:D169-D175.
Brophy, C.M. et al. (1999). “The small heat shock-related protein-20 is an actin-associated protein,”J. Vasc. Surg. 29:326-333.
Castle, A.L. (1998), “Amylin influences insulin-stimulated glucose metabolism by two independent mechanisms,”Am. J. Physiol. 274:E6-E12.
Christopoulos, G. et al. (1999). “Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product,”Mol. Pharmacol. 56:235-242.
Condorelli, G. et al. (1998). “PED/PEA-15 gene controls glucose transport and is overexpressed in type 2 diabetes mellitus,”ENMO J17:3858-3866.
Cooper, G.J.S. (1994). “Amylin compared with calcitonin gene-related peptide: structure, biology, and relevance to metabolic disease,”Endocr. Rev. 15:163-201.
Cooper, G.J.S. et al. (1998). “Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle,”Proc. Natl. Acad. Sci. USA85:7763-7766.
DeFronzo, R.A. (1997). “Pathogenesis of type 2 diabetes: metabolic and molecular implications for identifying diabetes genes,”Diabet. Rev. 5:177-269.
Dimitriadis, G. et al. (1997). “Effects of glucocorticoid excess on the sensitivity of glucose transport and metabolism to insulin in rat skeletal muscle,”Biochem. J.321:707-712.
Enoki, S. et al. (1992). “Plasma islet amyloid polypeptide levels in obesity, impaired glucose tolerance and non-insulin-dependent diabetes mellitus,”Diabet. Res. Clin. Prac.15:97-102.
Fodor, S.P.A. et al. (1991). “Light-directed, spatially addressable parallel chemical synthesis,”Science251:767-773.
Folli, F. (1993). “Regulation of phosphatidylinositol 3-kinase activity in liver and muscle of animal models of insulin-resistant and insulin-deficient diabetes mellitus,”J. Clin. Invest.92:1787-1794.
Frontoni, S et al. (1991). “In vivo insulin resistance induced by amylin primarily through inhibition of insulin-stimulated glycogen synthesis in skeletal muscle,”Diabetes40:568-573.
Gebre-Medhin, S. et al. (1998). “Increased insulin secretion and glucose tolerance in mice lacking islet amyloid polypeptide (amylin),”Biochern. Biophys. Res. Commun.250:271-277.
Gennaro, A.R. (Ed.)(1995). Remington Pharmaceutical Sciences 19th Ed. Mack Publishing (Table of Contents) pp. xv-xvi.
Giorgino, F. (1993). “Glucocorticoid regulation of insulin receptor and substrate IRS-1 tyrosine phosphorylation in rat skeletal muscle in vivo,”J. Clin. Invest91:2020-2030.
Gold, L. (1995). “Oligonucleotides as research, diagnostic, and therapeutic agents,”J. Biol. Chem.270:13581-13584.
Hettiarachchi, M. et al. (1997). “Rat amylin (8-37) enhances insulin action and alters lipid metabolism in normal and insulin resistant rats,”Am. J. Physiol.273:E859-E867.
Hunter, S.J. and Garvey, W.T. (1998). “Insulin action and insulin resistance: diseases involving defects in insulin receptors, signal transduction, and the glucose transport effector system,”Am. J. Med.105:331-345.
Inaguma, Y. et al. (1996). “cDNA cloning of a 20-kDa protein (p20) highly homologous to small heat shock proteins: developmental and physiological changes in rat hindlimb muscles,”Gene178(1-2):145-150.
Kahn, B.B. (1998). “Type 2 diabetes: When insulin secretion fails to compensate for insulin resistance,”Cell92:593-596.
Kahn, C.R. (1994). “Insulin action, diabetogenes, and the cause of type II diabetes,”Diabetes43:1066-1084.
Kao, A.W. (1999). “Aldolase mediates the association of F-actin with the insulin-responsive glucose transporter GLUT4,”J. Biol. Chem.274:17742-17747.
Kato, K. (1994). “Purification and characteristization of a 20-kDa protein that is highly homologous to alpha B crystallin,”J. Biol. Chem.269:15302-15309.
Lam, K.S. (1997) “Application of combinatorial library methods in cancer research and drug discovery,”Anticancer Drug Des.12:145-167.
Leighton, B. and Cooper, G.J. (1988). “Pancreatic amylin and calcitonin gene-related peptide cause resistance to insulin in skeletal muscle in vitro,”Nature335:632-635.
Molina, J.M. et al. (1990). “Induction of insulin resistance in-vivo by amylin and calcitonin gene-related peptide,”Diabetes39:260-265.
Moller, D.E. and Flier, J.S. (1991). “Insulin resistance—mechanisms, syndromes, and implications,”N. Engl. J. Med.325:938-948.
Moller, D.E. et al. (1996). “Candidate genes for insulin resistance,”Diabet. Care19:396-400.
Moyers, J.S. et al. (1996). “Overexpression of Rad inhibits glucose uptake in cultured muscle and fat cells,”J. Biol. Chem.271:23111-23116.
Niwa, M. et al. (2000). “Small molecular weight heat shock-related protein, HSP20, exhibits an anti-platelet activity by inhibiting receptor-mediated calcium influx,”Life Sci.66:L7-L12.
Oakes, N.D. et al. (1997). “Mechanisms of liver and muscle insulin resistance induced by chronic high-fat feeding,”Diabetes46:1768-1774.
Peraldi, P. and Spiegelman, B. (1998). “TNF-alpha and insulin resistance: Summary and future prospects,”Mol. Cell Biochem.182:169-175.
Pieber, T.R. et al. (1993). “Amylin-insulin relationships in insulin resistance with and without diabetic hyperglycemia,”Am. J. Physiol.265:E446-E453.
Reaven, G.M. (1995). “Pathophysiology of insulin resistance in human disease,”Physiol. Rev.75:473-486.
Reaven, G.M. and Miller, R.G. (1979). “An attempt to define the nature of chemical diabetes using a multidimensional analysis,”Diabetologia16:17-24.
Robinson, R. et al. (1993). “Glucose transport in L6 myoblasts overexpressing GLUT1 and GLUT4,”J. Biol. Chem.268:22119-22126.
Suh, N. et al. (1995). “Discovery of natural product chemopreventive agents utilizing HL-60 cell differentiation as a model,”Anticancer Res.15(2):233-239.
Tsakiridis, T. et al. (1994). “Disassembly of the actin network inhibits insulin-dependent stimulation of glucose transport and prevents recruitment of glucose transporters to the plasma membrane,”J. Biol. Chem.269:29934-29942.
Turner, D.M. (1996). “Natural product sour

Affiliated with

Also associated with

Rating

Phosphoprotein target for insulin and its antagonists does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Phosphoprotein target for insulin and its antagonists, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Phosphoprotein target for insulin and its antagonists will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3425224