메뉴 건너뛰기




Volumn 4, Issue 5, 2008, Pages 300-308

Effect of exercise training on calpain systems in lean and obese Zucker rats

Author keywords

Calpain; Diabetes; Exercise; Obesity; Skeletal muscle

Indexed keywords

BETA ACTIN; CALPAIN 1; CALPAIN 10; CALPAIN 2;

EID: 51849118739     PISSN: 14492288     EISSN: None     Source Type: Journal    
DOI: 10.7150/ijbs.4.300     Document Type: Article
Times cited : (14)

References (38)
  • 1
    • 0031417390 scopus 로고    scopus 로고
    • Exercise regulation of glucose transport in skeletal muscle
    • Hayashi T, Wojtaszewski JF, Goodyear LJ. Exercise regulation of glucose transport in skeletal muscle. Am J Physiol. 1997;273(6 Pt 1):E1039-51.
    • (1997) Am J Physiol , vol.273 , Issue.6 PART 1
    • Hayashi, T.1    Wojtaszewski, J.F.2    Goodyear, L.J.3
  • 2
    • 15644383939 scopus 로고
    • Insulin resistance in soleus muscle from obese Zucker rats
    • Crettaz M., Prentki M., Zaninetti D., and Jeanrenaud B. Insulin resistance in soleus muscle from obese Zucker rats. Biochem J 1983;86: 525-534.
    • (1983) Biochem J , vol.86 , pp. 525-534
    • Crettaz, M.1    Prentki, M.2    Zaninetti, D.3    Jeanrenaud, B.4
  • 3
    • 0027425174 scopus 로고
    • Effects of exercise training on muscle GLUT-4 protein content and translocation in obese Zucker rats
    • Brozinick JT Jr, Etgen GJ Jr, Yaspelkis BB 3rd, Kang HY, Ivy JL. Effects of exercise training on muscle GLUT-4 protein content and translocation in obese Zucker rats. Am J Physiol. 1993;265: E419-27.
    • (1993) Am J Physiol , vol.265
    • Brozinick Jr, J.T.1    Etgen Jr, G.J.2    Yaspelkis 3rd, B.B.3    Kang, H.Y.4    Ivy, J.L.5
  • 4
    • 0031769061 scopus 로고    scopus 로고
    • Exercise training reduces skeletal muscle membrane arachidonate in the obese (fa/fa) Zucker rat
    • Ayre KJ, Phinney SD, Tang AB, Stern JS. Exercise training reduces skeletal muscle membrane arachidonate in the obese (fa/fa) Zucker rat. J Appl Physiol. 1998;85: 1898-902.
    • (1998) J Appl Physiol , vol.85 , pp. 1898-1902
    • Ayre, K.J.1    Phinney, S.D.2    Tang, A.B.3    Stern, J.S.4
  • 5
    • 22844441436 scopus 로고    scopus 로고
    • Adenosinergic modulation of ventilation in obese zucker rats
    • Lee SD, Nakano H, Farkas GA. Adenosinergic modulation of ventilation in obese zucker rats. Obes Res. 2005;13: 545-55.
    • (2005) Obes Res , vol.13 , pp. 545-555
    • Lee, S.D.1    Nakano, H.2    Farkas, G.A.3
  • 6
    • 0026459873 scopus 로고
    • Insulin resistance in obese Zucker rat (fa/fa) skeletal muscle is associated with a failure of glucose transporter translocation
    • King PA, Horton ED, Hirshman MF, Horton ES. Insulin resistance in obese Zucker rat (fa/fa) skeletal muscle is associated with a failure of glucose transporter translocation. J Clin Invest. 1992;90: 1568-75.
    • (1992) J Clin Invest , vol.90 , pp. 1568-1575
    • King, P.A.1    Horton, E.D.2    Hirshman, M.F.3    Horton, E.S.4
  • 7
    • 0033772073 scopus 로고    scopus 로고
    • Genetic variation in the gene encoding calpain-10 is associated with type 2 diabetes mellitus
    • Horikawa Y, Oda N, Cox NJ, Li X, Orho-Melander M, Hara M, et al. Genetic variation in the gene encoding calpain-10 is associated with type 2 diabetes mellitus. Nat Genet. 2000;26: 163-75.
    • (2000) Nat Genet , vol.26 , pp. 163-175
    • Horikawa, Y.1    Oda, N.2    Cox, N.J.3    Li, X.4    Orho-Melander, M.5    Hara, M.6
  • 8
    • 0036895104 scopus 로고    scopus 로고
    • Variants within the calpain-10 gene on chromosome 2q37 (NIDDM1) and relationships to type 2 diabetes, insulin resistance, and impaired acute insulin secretion among Scandinavian Caucasians
    • Rasmussen SK, Urhammer SA, Berglund L, Jensen JN, Hansen L, Echwald SM, et al. Variants within the calpain-10 gene on chromosome 2q37 (NIDDM1) and relationships to type 2 diabetes, insulin resistance, and impaired acute insulin secretion among Scandinavian Caucasians. Diabetes. 2002;51: 3561-7.
    • (2002) Diabetes , vol.51 , pp. 3561-3567
    • Rasmussen, S.K.1    Urhammer, S.A.2    Berglund, L.3    Jensen, J.N.4    Hansen, L.5    Echwald, S.M.6
  • 9
    • 0017101433 scopus 로고
    • A Ca2+activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme
    • Dayton WR, Reville WJ, Goll DE, Stromer MH. A Ca2+activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme. Biochemistry. 1976;15: 2159-67.
    • (1976) Biochemistry , vol.15 , pp. 2159-2167
    • Dayton, W.R.1    Reville, W.J.2    Goll, D.E.3    Stromer, M.H.4
  • 10
    • 33745920207 scopus 로고    scopus 로고
    • A novel 111/121 diplotype in the Calpain-10 gene is associated with type 2 diabetes
    • Kang ES, Kim HJ, Nam M, Nam CM, Ahn CW, Cha BS, Lee HC. A novel 111/121 diplotype in the Calpain-10 gene is associated with type 2 diabetes. J Hum Genet. 2006; 51(7):629-33
    • (2006) J Hum Genet , vol.51 , Issue.7 , pp. 629-633
    • Kang, E.S.1    Kim, H.J.2    Nam, M.3    Nam, C.M.4    Ahn, C.W.5    Cha, B.S.6    Lee, H.C.7
  • 12
    • 0018833064 scopus 로고
    • Ca-activated neutral protease and its inhibitors: In vitro effect on intact myofibrils
    • Sugita H, Ishiura S, Suzuki K, Imahori K. Ca-activated neutral protease and its inhibitors: in vitro effect on intact myofibrils. Muscle Nerve. 1980;3: 335-9.
    • (1980) Muscle Nerve , vol.3 , pp. 335-339
    • Sugita, H.1    Ishiura, S.2    Suzuki, K.3    Imahori, K.4
  • 13
    • 0033797241 scopus 로고    scopus 로고
    • A calpain-10 gene polymorphism is associated with reduced muscle mRNA levels and insulin resistance
    • Baier LJ, Permana PA, Yang X, Pratley RE, Hanson RL, Shen GQ. A calpain-10 gene polymorphism is associated with reduced muscle mRNA levels and insulin resistance. J Clin Invest. 2000;106: R69-73.
    • (2000) J Clin Invest , vol.106
    • Baier, L.J.1    Permana, P.A.2    Yang, X.3    Pratley, R.E.4    Hanson, R.L.5    Shen, G.Q.6
  • 14
    • 0026911137 scopus 로고
    • Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin?
    • Goll DE, Thompson VF, Taylor RG, Zalewska T. Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? Bioessays. 1992;14: 549-56.
    • (1992) Bioessays , vol.14 , pp. 549-556
    • Goll, D.E.1    Thompson, V.F.2    Taylor, R.G.3    Zalewska, T.4
  • 15
    • 0022509727 scopus 로고
    • Immunogold electron-microscopic localisation of calpain I in skeletal muscle of rats
    • Yoshimura N, Murachi T, Heath R, Kay J, Jasani B, Newman GR. Immunogold electron-microscopic localisation of calpain I in skeletal muscle of rats. Cell Tissue Res. 1986;244: 265-70.
    • (1986) Cell Tissue Res , vol.244 , pp. 265-270
    • Yoshimura, N.1    Murachi, T.2    Heath, R.3    Kay, J.4    Jasani, B.5    Newman, G.R.6
  • 17
    • 0026801930 scopus 로고
    • Gene expression of calpains and their specific endogenous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits
    • Ilian MA, Forsberg NE. Gene expression of calpains and their specific endogenous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits. Biochem J. 1992;287 ( Pt 1):163-71.
    • (1992) Biochem J , vol.287 , Issue.PART 1 , pp. 163-171
    • Ilian, M.A.1    Forsberg, N.E.2
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72: 248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227: 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0001070415 scopus 로고
    • A neutral, calcium-activated proteinase from the soluble fraction of rat brain
    • Guroff G. A neutral, calcium-activated proteinase from the soluble fraction of rat brain. J Biol Chem. 1964;239: 149-155
    • (1964) J Biol Chem , vol.239 , pp. 149-155
    • Guroff, G.1
  • 24
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi H, Ishiura S, Suzuki K. Structure and physiological function of calpains. Biochem J. 1997; 328 (Pt. 3):721-732
    • (1997) Biochem J , vol.328 , Issue.PART. 3 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 26
    • 0034903587 scopus 로고    scopus 로고
    • The calpain family and human disease
    • Huang Y, Wang KK. The calpain family and human disease. Trends Mol Med. 2001;7: 355-62.
    • (2001) Trends Mol Med , vol.7 , pp. 355-362
    • Huang, Y.1    Wang, K.K.2
  • 27
    • 0027988820 scopus 로고
    • Calpain inhibition: An overview of its therapeutic potential
    • Wang KK, Yuen PW. Calpain inhibition: an overview of its therapeutic potential. Trends Pharmacol Sci. 1994;15: 412-9.
    • (1994) Trends Pharmacol Sci , vol.15 , pp. 412-419
    • Wang, K.K.1    Yuen, P.W.2
  • 28
    • 2342645468 scopus 로고    scopus 로고
    • Postmortem proteolysis is reduced in transgenic mice overexpressing calpastatin
    • Mar
    • Kent MP, Spencer MJ, Koohmaraie M. Postmortem proteolysis is reduced in transgenic mice overexpressing calpastatin. J Anim Sci Mar. 2004;82: 794-801.
    • (2004) J Anim Sci , vol.82 , pp. 794-801
    • Kent, M.P.1    Spencer, M.J.2    Koohmaraie, M.3
  • 29
    • 0025266427 scopus 로고
    • Calcium activated neutral protease - structure-function relationship and functional implications
    • Suzuki K, Ohno S. Calcium activated neutral protease - structure-function relationship and functional implications. Cell Struct Funct. 1990;15: 1-6.
    • (1990) Cell Struct Funct , vol.15 , pp. 1-6
    • Suzuki, K.1    Ohno, S.2
  • 32
    • 15944428524 scopus 로고    scopus 로고
    • The calcium-dependent protease calpain causes endothelial dysfunction in type 2 diabetes
    • Stalker TJ, Gong Y, Scalia R. The calcium-dependent protease calpain causes endothelial dysfunction in type 2 diabetes. Diabetes. 2005;54: 1132-40.
    • (2005) Diabetes , vol.54 , pp. 1132-1140
    • Stalker, T.J.1    Gong, Y.2    Scalia, R.3
  • 33
    • 0017379059 scopus 로고
    • A proenzyme of cyclic nucleotide-independent protein kinase and its activation by calcium-dependent neutral protease from rat liver
    • Takai Y, Yamamoto M, Inoue M, Kishimoto A, Nishizuka Y. A proenzyme of cyclic nucleotide-independent protein kinase and its activation by calcium-dependent neutral protease from rat liver. Biochem Biophys Res Commun. 1977;77: 542-50.
    • (1977) Biochem Biophys Res Commun , vol.77 , pp. 542-550
    • Takai, Y.1    Yamamoto, M.2    Inoue, M.3    Kishimoto, A.4    Nishizuka, Y.5
  • 35
    • 4444338479 scopus 로고    scopus 로고
    • Calpain-related diseases
    • Branca D. Calpain-related diseases. Biochem Biophys Res Commun. 2004;322: 1098-104.
    • (2004) Biochem Biophys Res Commun , vol.322 , pp. 1098-1104
    • Branca, D.1
  • 37
    • 15544381276 scopus 로고    scopus 로고
    • Exercise-induced increase in skeletal muscle vasodilatory responses in obese Zucker rats
    • Xiang L, Naik J, Hester RL. Exercise-induced increase in skeletal muscle vasodilatory responses in obese Zucker rats. Am J Physiol Regul Integr Comp Physiol. 2005;288: R987-91.
    • (2005) Am J Physiol Regul Integr Comp Physiol , vol.288
    • Xiang, L.1    Naik, J.2    Hester, R.L.3
  • 38
    • 1342327871 scopus 로고    scopus 로고
    • Exercise training reverses insulin resistance in muscle by enhanced recruitment of GLUT-4 to the cell surface
    • Etgen GJ Jr, Jensen J, Wilson CM, Hunt DG, Cushman SW, Ivy JL. Exercise training reverses insulin resistance in muscle by enhanced recruitment of GLUT-4 to the cell surface. Am J Physiol. 1997;272: E864-9.
    • (1997) Am J Physiol , vol.272
    • Etgen Jr, G.J.1    Jensen, J.2    Wilson, C.M.3    Hunt, D.G.4    Cushman, S.W.5    Ivy, J.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.