Localization of m-calpain and calpastatin and studies of their association in pulmonary smooth muscle endoplasmic reticulum

Biochimica et Biophysica Acta - General Subjects

Volumn 1770, Issue 9, 2007, Pages 1297-1307

  Samanta, Krishna ^a   Kar, Pulak ^a   Ghosh, Biswarup ^a   Chakraborti, Tapati ^a   Chakraborti, Sajal ^a  

^a UNIVERSITY OF KALYANI   (India)

Author keywords

Calpain calpastatin association; Calpastatin; Endoplasmic reticulum; m calpain; Pulmonary artery; Smooth muscle

Indexed keywords

CALPAIN; CALPASTATIN; CASEIN; CYSTEINE PROTEINASE INHIBITOR; M CALPAIN; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTERY MUSCLE; ARTICLE; CONTROLLED STUDY; COW; CYTOSOL; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME SUBUNIT; IMMUNOPRECIPITATION; LUNG ARTERY; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN LOCALIZATION; REGULATORY MECHANISM; ROUGH ENDOPLASMIC RETICULUM; WESTERN BLOTTING; ZYMOGRAPHY;

ANIMALS; CALCIUM-BINDING PROTEINS; CALPAIN; CARBONATES; CASEINS; CATTLE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPLASMIC RETICULUM; MUSCLE, SMOOTH, VASCULAR; PULMONARY ARTERY;

BOVINAE;

EID: 34547844232     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2007.06.010     Document Type: Article

References (59)

1. Goll D.E., Thompson V.F., Li H., Wei W., and Cong J. The calpain system. Physiol. Rev. 83 (2003) 731-801
2. Edelstein C.L., Weider W.D., Yaqoob M.M., Gengaro P.E., Burke T.J., and Schrier R.W. The role of cysteine proteases in hypoxia-induced renal proximal tubular injury. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 7662-7666
3. Edelstein C.L., Yaqoob M.M., Alkhunaizi A., Gengaro P., Nemenoff R.A., Wang K.K.W., and Schrier R.W. Modulation of hypoxia-induced calpain activity in rat renal proximal tubules. Kidney Int. 50 (1996) 150-1157
4. Fraser A., and Evan G. A licence to kill. Cell 85 (1996) 781-784
5. Juin P., Pelletier M., Oliver L., Tremblais K., Gregoire M., Mefiah K., and Vallette F.M. Induction of caspase-3 like activity by calcium in normal cytosolic extracts triggers nuclear apoptosis in a cell free system. J. Biol. Chem. 273 (1998) 17559-17564
6. Barr F.E. Calpain: a new target in pulmonary hypertension. Crit. Care Med. 33 (2005) 623-628
7. Ariyoshi H., Okahara K., Sakon M., Kambayashi J., Kawashima S., Kawasaki T., and Monden M. Possible involvement of m-calpain in vascular smooth muscle cell proliferation. Arterioscler. Thromb. Vasc. Biol. 18 (1998) 493-498
8. 2+-calpain and caspase-3 dependent pathways. Pharmacol. Res. 48 (2003) 571-578
9. Eva S., Una F., and Afshin S. Caspase -12 and ER- stress-mediated apoptosis the story so far. Ann. N. Y. Acad. Sci. 1010 (2003) 186-194
10. Michalak M., Cobett E.F., Mesaeli N., Nakamura K., and Opas M. Calreticulin: one protein, one gene, many functions. Biochem. J. 344 (1999) 281-292
11. Barnoy S., Zipser Y., Glaser T., Grimberg Y., and Kosower N.S. Association of calpain (Ca dependent thiol protease) with its endogenous inhibitor calpastatin in myoblasts. J. Cell. Biochem. 74 (1999) 522-531
12. Slman R., Flood G.G., Thinakarani G., and Neumer R.W. Endoplasmic reticulum stress-induced protease activation in cortical neurons. J. Biol. Chem. 276 (2001) 44736-44742
13. Hood J.L., Brooks W.H., and Roszman T.L. Subcellular mobility of the calpain/calpastatin network: an organelle transient. BioEssays 28 (2006) 850-859
14. Chakraborti S., Mandal A., Das S., and Chakraborti T. Role of MMP-2 in PKC-δ-mediated inhibition of Na-dependent Ca uptake in microsomes of pulmonary smooth muscle: Involvement of a pertussis toxin sensitive protein. Mol. Cell. Biochem. 280 (2005) 107-117
15. Belafanova Z., Bolli R., Zhang Z., Zheng Y., Pass J.M., Bhatnagar A., Tang Z.-L., Wang O., Cardwell E., and Ping P. Nitric oxide (NO) induces nitration of protein kinase Cε (PKCε), facilitating PKCε-RACK2 interactions: a novel mechanism of NO triggered activation of PKCε. J. Biol. Chem. 277 (2002) 15021-15027
16. Hood J.L., Brooks W.H., and Roszman T.L. Differential compartmentalization of the calpain/calpastatin network with the endoplasmic reticulum and Golgi apparatus. J. Biol. Chem. 278 (2004) 43126-43135
17. Duffy J.D., Schwartz S.M., Lyons J.M., et al. calpain inhibition decreases endothelin-1 levels and pulmonary hypertension after cardiopulmonary bypass with deep hypothemic circulatory arrest. Cri. Care. Med. 33 (2005) 623-628
18. 2+ATPase by superoxide radical in microsomes of pulmonary smooth muscle. Biochem. J. 31 (1996) 7885-7890
19. Mandal M., Mandal A., Das S., Chakraborti S., and Chakraborti T. Identification, purification and partial characterization of tissue inhibitor of matrix metalloprotease-2 in bovine pulmonary artery smooth muscle. Mol. Cell. Biochem. 254 (2003) 275-287
20. Phung T.L., Roncone A., deMesy Jensen K.L., Sparks C.E., and Sparks J.D. Phosphoinositide 3-kinase activity is necessary for insulin-dependent inhibition of apolipoprotein B secretion by rat hepatocytes and localizes to the endoplasmic reticulum. J. Biol. Chem. 272 (1997) 30693-30702
21. Fujiki Y., Hubbard A.L., Fowler S., and Lazarow P.B. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93 (1982) 97-102
22. Baudhuin P. Morphometry of subcellular fractions. Methods Enzymol. 32 Part B (1974) 3-20
23. Karmakar S., Ghosh A.N., Dey D., Nair G.B., and Ganguly U. Ultrastructural changes in HeLa cells associated with enteroadherent Escherichia coli isolated from infants with diarrhoea in Calcutta. J. Diarrhoeal Dis. Res. 12 (1994) 274-278
24. Towbin H., Staehlin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 4350-4354
25. Raser K.J., Posner A., and Wang K.K.W. Casein zymography: a method to study μ-calpain, m-calpain, and their inhibitory agents. Arch. Biochem. Biophys. 319 (1995) 211-216
26. Hood J.L., Logan B.B., Sinai A.P., Brooks W.H., and Roszman T.L. Association of the calpain/calpastatin network with subcellular organelles. Biochem. Biophys. Res. Commun. 310 (2003) 1200-1212
27. Garcia M., Bondada V., and Geddes J.W. Mitochondrial localization of μ calpain. Biochem. Biophys. Res. Commun. 338 (2005) 1241-1247
28. Eskelinen E.L. Role of lamp-1 and lamp-2 in lysosomes and autophagy. Mol. Aspects Med. 27 (2006) 495-502
29. Baer H.P., and Vriend R.A. Cytosolic enzyme leakage from isolated smooth muscle preparation. Can. J. Physiol. Pharmacol. 63 (1985) 164-165
30. Kim H.K., Kim E.G., and Schuman E. Measurement of dendrite mRNA transport using ribosomal markers. Biochem. Biophys. Res. Commun. 328 (2005) 895-900
31. Nishimura T., and Goll D.E. Binding of calpain fragments to calpastatin. J. Biol. Chem. 266 (1991) 11842-11850
32. Strobl S., Fernandez-Catalan C., Braun M., Huber R., Masumoto H., Nakagawa K., Irie A., Sorimachi H., Bourenkow G., Bartunik H., Suzuki K., and Bode W. The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 588-592
33. 2+-regulated phospholipid-binding domain. Biochem. Biophys. Res. Commun. 280 (2001) 1333-1339
34. 2+ sensitivity and implications for the role of the C(2)-like domain. J. Biol. Chem. 276 (2001) 7404-7407
35. 2 C2 domain specify targeting to Golgi and ER in live cells. Mol. Biol. Cell 15 (2004) 371-383
36. Xie X., Dwyer M.D., Swenson L., Parker M.H., and Botfield M.C. Crystal structure of calcium-free human sorcin: a member of the penta-EF-hand protein family. Protein Sci. 10 (2001) 2419-2425
37. Schwarz-Benmeir N., Glaser T., Barnoy S., and Kosower N.S. Calpstatin in erythrocytes of young and old individuals. Biochem. J. 304 (1994) 365-370
38. Nixon R.A., Saito K.I., Grynspan F., Griffin W.R., atayama S.K., Honda T., Mohan P.S., Shea T.B., and Beerman M. Calcium-activated neutral proteinase system in aging and Alzheimer's disease. Ann. N. Y. Acad. Sci. 747 (1994) 77-91
39. Barnoy S., Glaser T., and Kosower N.S. The role of calpastatin (the specific calpain inhibitor) in myoblast differentiation and fusion. Biochem. Biophys. Res. Commun. 220 (1996) 933-938
40. Mellgren R.L., Song K., and Mericle M.T. m-Calpain requires DNA for activity on nuclear proteins at low calcium concentrations. J. Biol. Chem. 268 (1993) 653-657
41. Salamino F., Averna M., Tedesco I., De Tullio R., Melloni E., and Pontremoli S. Modulation of rat brain calpastatin efficiency by post translational modifications. FEBS Lett. 412 (1997) 433-438
42. Melloni E., Michetti M., Salamino F., and Pontremoli S. Molecular and functional properties of a calpain activator protein specific for μ-isoforms. J. Biol. Chem. 273 (1998) 12827-12831
43. Yuexian S., Melnikov V.Y., Schrier R.W., and Edelstein C.L. Downregulation of the calpain inhibitor protein calpastatin by caspases during renal ischemia-reperfusion. Am. J. Physiol. 279 (2000) F509-F517
44. 2+ requiring forms of calcium-activated neutral proteases. Biochemistry 28 (1989) 449-455
45. Vandenabeele P., Orrenius S., and Zhivotovsky B. Serin protease and calpains fulfill important supporting roles in the apoptotic tragedy of the cellular opera. Cell Death Differ. 12 (2005) 1219-1224
46. Ilian M.A., and Foresberg N.E. Gene Expression of calpains and their specific endogenous inhibitor calpastatin, in skeletal muscle of fed and fasted rabbits. Biochem. J. 287 (1992) 163-171
47. Shields D.C., Tyor W.R., Deibler G.E., Hogan E.L., and Banik N.L. Increased calpain expression in activated glial and inflammatory cells in experimental allergic encephalomyelitis. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 5768-5772
48. Kawasaki H., Emori Y., and Suzuki K. Calpastatin has two distinct sites for interaction with calpain-Effect of calpastatin fragments on the binding of calpain to membranes. Arch. Biochem. Biophys. 305 (1993) 467-472
49. Koohmaraie M. Effect of pH, temperature, and inhibitors on autolysis and catalytic activity of bovine skeletal muscle μ-calpain. J. Anim. Sci. 70 (1992) 3071-3080
50. Nishihara H., Nakagawa Y., Ishikawa H., Ohba M., Shimizu K., and Nakamura T. Matrix vesicles and media vesicle as nonclassical pathways for the secretion of m-calpain from MC3T3-E1 cells. Biochem. Biophys. Res. Commun. 285 (2001) 845-853
51. Yoshizawa T., Sorimachi H., Tomioka S., Ishiura S., and Suzuki K. A catalytic subunit of calpain possesses full proteolytic activity. FEBS Lett. 358 1 (1995) 101-103
52. Suzuki K., Sorimachi H., Yoshizawa T., Kinbara K., and Ishiura S. Calpain: novel family members, activation, and physiologic function. Biol. Chem. 376 9 (1995) 523-529
53. Tam L.Y., Loo T.W., Clarke D.M., and Reithmeier A.F. Identification of an internal topogenic signal sequence in human Band 3, the erythrocyte anion exchanger. J. Biol. Chem. 269 (1994) 32542-32550
54. Joliot A., Maizel A., Rosenberg D., Trembleau A., Dupas S., Volovitch M., and Prochiantz A. Identification of a signal sequence necessary for the unconventional secretion of Engrailed homeoprotein. Curr. Biol. 8 (1998) 856-863
55. Ouzzine M., Magdalou J., Burchell B., and Fournel-Gigleux S. An internal signal sequence mediates the targeting and retention of the human UDP-glucuronosyltransferase 1A6 to the endoplasmic reticulum. J. Biol. Chem. 274 (1999) 31401-31409
56. Beaudoin F., and Napier J. Targeting and membrane-insertion of a sunflower oleosin in vitro and in Saccharomyces cerevisiae: the central hydrophobic domain contains more than one signal sequence, and directs oleosin insertion into the endoplasmic reticulum membrane using anchor sequence mechanism. Planta 215 (2002) 293-303
57. Ashby M.C., and Tepikin A.V. ER calcium and the functions of intracellular organelles. Cell 12 (2001) 11-17
58. Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B.A., and Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403 (2000) 98-103
59. Nakagawa T., and Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J. Cell Biol. 150 (2000) 887-894