Potential role of N-myristoyltransferase in pathogenic conditions

Canadian Journal of Physiology and Pharmacology

Volumn 82, Issue 10, 2004, Pages 849-859

  Sharma, Rajendra K ^a  

^a UNIVERSITY OF SASKATCHEWAN   (Canada)

Author keywords

Calpains; Diabetes; Ischemic heart; N myristoyltransferase; Vanadate

Indexed keywords

ENZYME INHIBITOR; INSULIN; N ACETYLLEUCYLLEUCYLMETHIONINAL; ORTHOVANADIC ACID; PROTEIN N MYRISTOYLTRANSFERASE; UNCLASSIFIED DRUG; VANADIC ACID;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; CELLULAR DISTRIBUTION; CONFERENCE PAPER; DIABETES MELLITUS; ENZYME ACTIVITY; ENZYME LOCALIZATION; HEART MUSCLE ISCHEMIA; IMMUNOHISTOCHEMISTRY; INSULIN DEPENDENT DIABETES MELLITUS; INSULIN RESPONSE; ISCHEMIA; NON INSULIN DEPENDENT DIABETES MELLITUS; NONHUMAN; PATHOPHYSIOLOGY; PRIORITY JOURNAL; RAT; REPERFUSION INJURY; STREPTOZOCIN DIABETES;

ACYLTRANSFERASES; ANIMALS; DIABETES MELLITUS, EXPERIMENTAL; DISEASE MODELS, ANIMAL; GLYCOPROTEINS; HUMANS; MYOCARDIAL REPERFUSION INJURY; RATS;

EID: 13544263368     PISSN: 00084212     EISSN: None     Source Type: Journal    
DOI: 10.1139/y04-099     Document Type: Conference Paper

References (53)

1. 2-terminal blocking group of calcineurin B as myristic acid. FEBS Lett. 150: 314-318.
2. Arthur, G.D., and Belcastsro, A.N. 1997. A calcium stimulated cysteine protease involved in isoproterenol induced cardiac hypertrophy. Mol. Cell. Biochem. 176: 241-248.
3. Boutin, J.A. 1997. Myristoylation. Cell. Signalling, 9: 15-35.
4. Boutin, J.A., Ferry, G., Ernould, A.P., Maes, P., Remond, G., and Vincent, M. 1993. Myristoyl-CoA:protein N-myristoyltransferase activity in cancer cells. Purification and characterization of a cytosolic isoform from the murine leukemia cell line L1210. Eur. J. Biochem. 214: 853-867.
5. src but does not affect tyrosine protein kinase activity. J. Virol. 58: 468-474.
6. 2 terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle. Proc. Natl. Acad. Sci. USA, 79: 6128-6131.
7. Croall, D.E., and Demartino, G.N. 1991. Calcium activated neutral protease (calpain) system: structure, function and regulation. Physiol. Rev. 71: 813-847.
8. src myristoylation and membrane association and for cell transformation. Mol. Cell. Biol. 4: 1834-1842.
9. Farazi, T.A., Waksman, J.I., and Gordon, J.I. 2001. The biology and enzymology of protein N-myristoylation. J. Biol. Chem. 276: 9501-9504.
10. Feder, D., and Bishop, J.M. 1990. Purification and enzymatic characterization of pp60c-src from human platelets. J. Biol. Chem. 265: 8205-8211.
11. Fryer, R.M., Schultz, J.E.L.J., Hsu, A.K., and Gross, G.J. 1998. Pretreatment with tyrosine kinase inhibitors partially attenuates ischemic preconditioning in rat hearts. Am. J. Physol. 275: H2009-H2015.
12. 2+ dependent porteolysis? Circ. Res. 78: 455-465.
13. Iizuka, K., Kawaguchi, H., and Kitabatake, A. 1993. Effects of thiol protease inhibitors on fodrin degradation during hypoxia in cultured myocytes. J. Mol. Cell. Cardiol. 25: 1101-1109.
14. Imajoh, S., Kawasaki, H., and Suzuki, K. 1986. The amino terminal hydrophobic region of the small subunit of calcium-activated neutral protease (CANP) is essential for its activation by phosphatidylinositol. J. Biochem. (Tokyo), 99: 1281-1284.
15. Kakkar, R., Wang, X., Radhi, J.M., Rajala, R.V.S., Wang, R., and Sharma, R.K. 2001. Decreased expression of high molecular weight calmodulin-binding protein and its correlation in the apoptosis in ischemia-reperfused rat heart. Cell Calcium, 29: 59-71.
16. src prevents both myristoylation and morphological transformation. Proc. Natl. Acad. Sci. USA, 82: 4625-4628.
17. Kamps, M.P., Buss, J.E., and Sefton, B.M. 1986. Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known polypeptides substrates without inducing transformation. Cell, 45: 105-112.
18. Kennedy, M.T., Brockman, H., and Rusnak, F. 1996. Contribution of myristoylation to calcineurin structure/function. J. Biol. Chem. 271: 26517-26521.
19. Khandelwal, R.L., and Pugazhenthi, S. 1995. In vivo effects of vanadate on hepatic glycogen metabolism and lipogenic enzymes in insulin-dependent and insulin-resistant diabetic animals. Mol. Cell. Biochem. 153: 95-102.
20. King, M.J., and Sharma, R.K. 1992. Demonstration of multiple forms of bovine brain myristoyl CoA:protein N-myristoyltransferase. Mol. Cell. Biochem. 113: 77-81.
21. King, M.J., and Sharma, R.K. 1993. Identification, purification and characterization of a membrane-associated N-myristoyltransferase inhibitor protein from bovine brain. Biochem. J. 291: 635-639.
22. King, M.J., and Sharma, R.K. 1995. Differential activation of bovine brain N-myristoyltransferase(s) by a cytosolic activator. Biochem. Biophys. Res. Commun. 212: 580-588.
23. King, M.J., Pugazhenthi, S., Khandelwal, R.L., and Sharma, R.K. 1993a. Elevated N-myristoyltransferase activity is reversed by sodium orthovanadate in streptozotocin-induced diabetic rat. Biochim. Biophys. Acta, 1165: 259-262.
24. King, M.J., Pugazhenthi, S., Khandelwal, R.L., and Sharma, R.K. 1993e. Membrane-associated N-myristoyltransferase activity is reduced in obese (fa/fa) Zucker rat liver. Biochem. Biophys. Res. Commun. 196: 665-670.
25. Klarland, J.K. 1985. Transformation of cells by an inhibitor of phosphatases acting on phosphotyrosine in proteins. Cell, 41: 707-717.
26. Li, S., Ke, S., and Budde, R.J.A. 1996. The C-terminal SRC kinase (CSK) is widely expressed, active in HT-29 cells that contain activated SRC, and its expression is downregulated in butyrate-treated SW 620 cells. Cell Biol. Int. 20: 723-729.
27. Liauw, S., and Steinberg, T.A. 1996. Dephosphorylation of catalytic subunit of cAMP-dependent protein kinase at Thr-197 by a cellular protein phosphatase and by purified protein phosphatase-2A. J. Biol. Chem. 271: 258-263.
28. Macara, I.G., Kustin, K., and Cantley, L.C. 1980. Glutathione reduces cytoplasmic vanadate mechanism and physiological implications. Biochim. Biophys. Acta, 629: 95-106.
29. Magnusson, B.A., Raju, R.V.S., and Sharma, R.K. 1995. Increased N-myristoyltransferase activity observed in rat and human co-Ionic tumors. J. Natl. Cancer Inst. 87: 1630-1635.
30. Maki, M., Hatanaka, M., Takano, E., and Murachi, T. 1990. Intra-cellular calcium-dependent proteolysis. Edited by R.L. Melgren and T. Murachi. CRC Press Inc., Boca Raton, Fla. pp. 37-54.
31. McIlhinney, R.A.J., and McGlone, K. 1990. Characterization of a myristoyl CoA: glycylpeptide N-myristoyltransferase activity in rat brain. Subcellular and regional distribution. J. Neurochem. 54: 110-117.
32. Melloni, E., Averna, M., Salamino, F., Sparatore, B., Minafra, R., and Pntremoli, S. 2000. Acyl-CoA-binding protein is a potent m-calpain activator. J. Biol. Chem. 275: 82-86.
33. Miyazaki, Y., Gross, R.W., Sobel, B.E., and Saffits, J.E. 1990. Selective turnover of sarcolemmal phospholipids with lethal cardiac myocyte injury. Am. J. Physiol. 259: C325-C331.
34. Oda, A., Druker, B.J., Ariyoshi, H., Smith, M., and Salzman, B.W. 1993. pp60Src is an endogenous substrate for calpain in human blood platelets. J. Biol. Chem. 268: 12 603-12 608.
35. Oda, Y., Renaux, B., Bjorge, J., Saifeddine, M., Fujita, D.J., and Hollenberg, M.D. 1999. c-Src is a major cytosolic tyrosine kinase in vascular tissue. Can. J. Physiol. Pharmacol. 77: 606-617.
36. Pasha, M.K., Dimmock, J.R., Hollenberg, M.D., Sharma, R.K. 2002. Enhanced activity of human N-myristoyltransferase by dimethyl sulfoxide and related solvents in the presence of serine containing peptide substrates. Biochem. Pharmacol. 64: 1461-1467.
37. Ping, P., Zhang, J., Zheng, Y.T., Li, R.C., Dawn, B., Tang, X.L., Takano, H., Balafanova, Z., and Bolli, R. 1999. Demonstration of selective protein kinase C-dependent activation of Src and Lck tyrosine kinase during ischemic preconditioning in conscious rabbits. Circ. Res. 85: 542-550.
38. Pugazhenthi, S., and Khandelwal, R.L. 1990. Insulin-like effects of vanadate on hepatic glycogen metabolism in nondiabetic and straptozotocine- induced diabetic rats. Diabetes, 39: 821-827.
39. Pugazhenthi, S., Khandelwal, R.L., and Angel, J.F. 1991a. Insulin-like effect of vanadate on malic enzyme and glucose-6-phosphate dehydrogenase activities in streptozotocin-induced diabetic rat liver. Biochim. Biophys. Acta, 1083: 310-312.
40. Pugazhenthi, S., Angel, J.F., and Khandelwal, R.L. 1991b. Long-term effects of vanadate treatment of glycogen metabolizing and lipogenic enzymes of liver in genetically diabetic (db/db) mice. Metabolism, 40: 941-946.
41. Rajala, R.V., Datla, R.S., Moyana, T.N., Kakkar, R., Carlsen, S.A., and Sharma, R.K. 2000a. N-Myristoyltransferase. Mol. Cell. Biochem. 204: 135-155.
42. Rajala, R.V.S., Radhi, J.M., Kakkar, R., Datla, R.S.S., and Sharma, R.K. 2000b. Increased expression of N-myristoyltransferase in gallbladder carcinomas. Cancer, 88: 1992-1999.
43. Rajala, R.V.S., Datla, R.S.S., Carlsen, S.A., Anderson, D.H., Qi, Z., Qang, J.H., and Sharma, R.K. 2001. Phosphorylation of human N- myristoyltransferase by N-myristoylated SRC family tyrosine kinase members. Biochem. Biophys. Res. Commun. 288: 233-239.
44. Rajala, R.V.S., Kakkar, R., Radhi, J.M., Wang, X., Wang, R., Datla, R.S.S., Kanthan, R., and Sharma, R.K. 2002. Altered expression and localization of N-myristoyltransferase in experimentally induced rat model of ischemia reperfusion. J. Cell. Biochem. 86: 509-519.
45. Raju, R.V.S., and Sharma, R.K. 1997. Demonstration and purification of a myristoyl-CoA binding protein from bovine cardiac muscle. Life Sci. 60: 2145-2153.
46. Raju, R.V.S., Moyana, T.N., and Sharma, R.K. 1997. N-Myristoyltransferase overexpression in human colorectal adenocarcinomas. Exp. Cell Res. 235: 145-154.
47. Raju, R.V.S., Kakkar, R., Datla, R.S.S., Radhi, J.M., and Sharma, R.K. 1998. Myristoyl-CoA:protein-myristoyltransferase from bovine cardiac muscle. Molecular cloning, kinetic analysis, and in vitro proteolytic cleavage by m-calpain. Exp. Cell Res. 241: 23-35.
48. Resh, M.D. 1999. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochem. Biophys. Acta, 1451: 1-16.
49. Resh, M.D., and Ling, H.P. 1990. Identification of a 32 K plasma membrane protein that binds to the myristoylated amino-terminal sequence of pp60v-src. Nature (London), 346: 84-86.
50. Tompa, P., Baki, A., Schad, E., and Friedich, P. 1996. The calpain cascade: calpain activates m-calpain. J. Biol. Chem. 271: 33 161-33 164.
51. VanBilsen, M., Van der Vusse, G.J., Willemsen, P.H.M., Coumans, W.A, Roeman, T.H., and Reneman, R.S. 1989. Lipid alterations in isolated working rat hearts during ischemia and reperfusion: its relation to myocardial damage. Circ. Res. 64: 304-314.
52. Yoshida, K., Sorimachi, Y., Fujiwara, M., and Hironaka, K. 1995a. Calpain is implicated in rat myocardial injury after ischemia and reperfusion. Jpn. Circ. J. 59: 40-48.
53. Yoshida, K., Inui, M., Harada, K., Saido, T.C., Sorimachi, Y., Ishihara, T., Kawashima, S., and Sobue, K. 1995b. Reperfusion of rat heart after brief ischemia induces proteolysis of calspectin (nonerythroid spectrin or fodrin) by calpain. Circ. Res. 77: 603-610.