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Volumn 26, Issue 6, 2010, Pages 577-585

The effect of hot-tub therapy on serum Hsp70 level and its benefit on diabetic rats: A preliminary report

Author keywords

Antioxidant capacity; Diabetic complications; HDL functionality; Hot tub therapy; Hsp70; Protein folding

Indexed keywords

ADVANCED GLYCATION END PRODUCT; GLUCOSE; GLYCOSYLATED HEMOGLOBIN; HEAT SHOCK PROTEIN 70; INSULIN; LUCIFERASE; STREPTOZOCIN;

EID: 77955644253     PISSN: 02656736     EISSN: 14645157     Source Type: Journal    
DOI: 10.3109/02656736.2010.485594     Document Type: Article
Times cited : (38)

References (42)
  • 1
    • 0029560077 scopus 로고
    • The pathological implications of proteins glyca-tion
    • Brownlee M. The pathological implications of proteins glyca-tion. Clin Inv Med 1995;18:275-281.
    • (1995) Clin Inv Med , vol.18 , pp. 275-281
    • Brownlee, M.1
  • 2
  • 3
    • 18944375783 scopus 로고    scopus 로고
    • Glucose, advanced glycation end products, and diabetes complications: What is new and what works
    • Peppa M, Uribarri J, Vlassara H. Glucose, advanced glycation end products, and diabetes complications: What is new and what works. Clin Diabetes 2003;21:4,186.
    • (2003) Clin Diabetes , vol.21 , Issue.4 , pp. 186
    • Peppa, M.1    Uribarri, J.2    Vlassara, H.3
  • 4
    • 0142029114 scopus 로고    scopus 로고
    • Novel inhibitors of advanced glycation endproducts
    • Rahbar S, Figarola JL. Novel inhibitors of advanced glycation endproducts. Arch Biochem Biophys 2003;419:63-79.
    • (2003) Arch Biochem Biophys , vol.419 , pp. 63-79
    • Rahbar, S.1    Figarola, J.L.2
  • 5
    • 0036860156 scopus 로고    scopus 로고
    • Effects of inhibition of glycation and oxidative stress on the development of diabetic nephropathy in rats
    • Agardh CD, Stenram U, Torffvit O, Agardh E. Effects of inhibition of glycation and oxidative stress on the development of diabetic nephropathy in rats. J Diabetes Complications 2002;16:395-400.
    • (2002) J Diabetes Complications , vol.16 , pp. 395-400
    • Agardh, C.D.1    Stenram, U.2    Torffvit, O.3    Agardh, E.4
  • 6
    • 0026323337 scopus 로고
    • Aminoguanidine treatment inhibits the development of experimental diabetic retinopathy
    • Hammes HP, Martin S, Federlin K, Geisen K, Brownlee M. Aminoguanidine treatment inhibits the development of experimental diabetic retinopathy. Proc Natl Acad Sci 1991;88:11555-11558.
    • (1991) Proc Natl Acad Sci , vol.88 , pp. 11555-11558
    • Hammes, H.P.1    Martin, S.2    Federlin, K.3    Geisen, K.4    Brownlee, M.5
  • 7
    • 0028061311 scopus 로고
    • Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell
    • Craig EA, Weissman JS, Horwich AL. Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell. Cell 1994;78:365-372.
    • (1994) Cell , vol.78 , pp. 365-372
    • Craig, E.A.1    Weissman, J.S.2    Horwich, A.L.3
  • 8
    • 23344446694 scopus 로고    scopus 로고
    • Endogenous extra-cellular heat shock protein 72: Releasing signal(s) and function
    • Fleshner M, Johnson JD. Endogenous extra-cellular heat shock protein 72: Releasing signal(s) and function. Int J Hyperthermia 2005;21:457-471.
    • (2005) Int J Hyperthermia , vol.21 , pp. 457-471
    • Fleshner, M.1    Johnson, J.D.2
  • 10
    • 0035914213 scopus 로고    scopus 로고
    • Characteristic changes of stress protein expression in streptozotocin-induced diabetic rats
    • Yamagish N, Nakayama K, Wakatsuki T, Hatayama T. Characteristic changes of stress protein expression in streptozotocin-induced diabetic rats. Life Sci 2001;69: 2603-2609.
    • (2001) Life Sci , vol.69 , pp. 2603-2609
    • Yamagish, N.1    Nakayama, K.2    Wakatsuki, T.3    Hatayama, T.4
  • 11
    • 0036227062 scopus 로고    scopus 로고
    • Decreased expression of heat shock protein 72 in skeletal muscle of patients with type 2 diabetes correlates with insulin resistance
    • Kurucz I, Morva A, Vaag A, Eriksson KF, Huang X, Groop L, Koranyi L. Decreased expression of heat shock protein 72 in skeletal muscle of patients with type 2 diabetes correlates with insulin resistance. Diabetes 2002;51:1102-1109.
    • (2002) Diabetes , vol.51 , pp. 1102-1109
    • Kurucz, I.1    Morva, A.2    Vaag, A.3    Eriksson, K.F.4    Huang, X.5    Groop, L.6    Koranyi, L.7
  • 12
    • 14844356006 scopus 로고    scopus 로고
    • Loss of defense against stress: Diabetes and heat shock proteins
    • Hooper PL, Hopper JJ. Loss of defense against stress: Diabetes and heat shock proteins. Diabetes Thechnol Ther 2005;7:204-208.
    • (2005) Diabetes Thechnol Ther , vol.7 , pp. 204-208
    • Hooper, P.L.1    Hopper, J.J.2
  • 14
    • 0028580077 scopus 로고
    • Animal models in diabetes research
    • Mendez JD, Ramos GHB. Animal models in diabetes research. Arch Med Res 1994;25:367-375.
    • (1994) Arch Med Res , vol.25 , pp. 367-375
    • Mendez, J.D.1    Ghb, R.2
  • 15
    • 11844260682 scopus 로고    scopus 로고
    • Manipulating heat shock protein expression in laboratory animals
    • Tolson JK, Roberts SM. Manipulating heat shock protein expression in laboratory animals. Methods 2005;35:149-157.
    • (2005) Methods , vol.35 , pp. 149-157
    • Tolson, J.K.1    Roberts, S.M.2
  • 16
    • 0036327153 scopus 로고    scopus 로고
    • Whole-body hyperthermia-induced thermotolerance is associated with the induction of Heat Shock Protein 70 in mice
    • King Y-T, Lin C-S, Lin J-H, Lee W-C. Whole-body hyperthermia-induced thermotolerance is associated with the induction of Heat Shock Protein 70 in mice. J Experiment Biol 2002;205:273-278.
    • (2002) J Experiment Biol , vol.205 , pp. 273-278
    • King, Y.-T.1    Lin, C.-S.2    Lin, J.-H.3    Lee, W.-C.4
  • 18
    • 0034713819 scopus 로고    scopus 로고
    • Involvement of cytokines in the mechanism of whole-body hyperthermia-induced cardioprotection
    • Yamashita N, Hoshida S, Otsu K, Taniguchi N, Kuzuya T, Hori M. Involvement of cytokines in the mechanism of whole-body hyperthermia-induced cardioprotection. Circulation 2000;102:452-457.
    • (2000) Circulation , vol.102 , pp. 452-457
    • Yamashita, N.1    Hoshida, S.2    Otsu, K.3    Taniguchi, N.4    Kuzuya, T.5    Hori, M.6
  • 20
    • 0015348189 scopus 로고
    • Estimation of the concentration of low-density lipoprotein cholesterol in plasma without use of the preparative ultracentrifuge
    • Fridewald WJ, Levy RJ, Fredrikson DS. Estimation of the concentration of low-density lipoprotein cholesterol in plasma without use of the preparative ultracentrifuge. Clin Chem 1972;18:499-502.
    • (1972) Clin Chem , vol.18 , pp. 499-502
    • Fridewald, W.J.1    Levy, R.J.2    Fredrikson, D.S.3
  • 21
    • 0036972669 scopus 로고    scopus 로고
    • Advanced glycation end-products and advanced oxidation protein products in patients with diabetes mellitus
    • Kalousova M, Skrha J, Zima T. Advanced glycation end-products and advanced oxidation protein products in patients with diabetes mellitus. Physiol Res 2002;51: 597-604.
    • (2002) Physiol Res , vol.51 , pp. 597-604
    • Kalousova, M.1    Skrha, J.2    Zima, T.3
  • 22
    • 0030586361 scopus 로고    scopus 로고
    • The ferric reducing ability of plasma (FRAP) as a measure of antioxidant power: The FRAP assay
    • Benzie IF, Stain JJ. The ferric reducing ability of plasma (FRAP) as a measure of antioxidant power: The FRAP assay. Anal Biochem 1996;239:70-76.
    • (1996) Anal Biochem , vol.239 , pp. 70-76
    • Benzie, I.F.1    Stain, J.J.2
  • 23
    • 0021365056 scopus 로고
    • Nonenzymatic glycosyla-tion of human serum albumin alters its conformation and function
    • Shaklai N, Garlick RL, Bunn HF. Nonenzymatic glycosyla-tion of human serum albumin alters its conformation and function. J Biol Chem 1984;259:3812-3817.
    • (1984) J Biol Chem , vol.259 , pp. 3812-3817
    • Shaklai, N.1    Garlick, R.L.2    Bunn, H.F.3
  • 24
    • 0028151509 scopus 로고
    • The ATP hydrolysis dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ, and GrpE
    • Szabo A, Langer T, Schroder H, Flanagan J, Bukau B, Hartl U. The ATP hydrolysis dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ, and GrpE. Proc Natl Acad Sci USA 1994;91:10345-10349.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schroder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, U.6
  • 25
    • 38349009152 scopus 로고    scopus 로고
    • The improvement effect of L-Lys as a chemical chaperone on STZ-induced diabetic rats, protein structure and function
    • Jafarnejad A, Bathaie SZ, Nakhjavani M, Hassan MZ, Banasadegh S. The improvement effect of L-Lys as a chemical chaperone on STZ-induced diabetic rats, protein structure and function. Diabetes Metab Res Rev 2008;24:64-73.
    • (2008) Diabetes Metab Res Rev , vol.24 , pp. 64-73
    • Jafarnejad, A.1    Bathaie, S.Z.2    Nakhjavani, M.3    Hassan, M.Z.4    Banasadegh, S.5
  • 26
    • 38749136625 scopus 로고    scopus 로고
    • Investigation of the mechanisms involved in the high-dose and long-term acetyl salicylic acid therapy of type i diabetic rats
    • Jafarnejad A, Bathaie SZ, Nakhjavani M, Hassan MZ. Investigation of the mechanisms involved in the high-dose and long-term acetyl salicylic acid therapy of type I diabetic rats. J Pharmacol Exp Ther 2008;324:850-857.
    • (2008) J Pharmacol Exp Ther , vol.324 , pp. 850-857
    • Jafarnejad, A.1    Bathaie, S.Z.2    Nakhjavani, M.3    Hassan, M.Z.4
  • 27
    • 38349081325 scopus 로고    scopus 로고
    • Effect of spermine on lipid profile and HDL functionality in the streptozotocin-induced diabetic rat model
    • Jafarnejad A, Bathaie SZ, Nakhjavani M, Hassan MZ. Effect of spermine on lipid profile and HDL functionality in the streptozotocin-induced diabetic rat model. Life Sci 2008;82:301-307.
    • (2008) Life Sci , vol.82 , pp. 301-307
    • Jafarnejad, A.1    Bathaie, S.Z.2    Nakhjavani, M.3    Hassan, M.Z.4
  • 28
    • 0033575998 scopus 로고    scopus 로고
    • Hot-tub therapy for type 2 diabetes mellitus
    • Hooper PL. Hot-tub therapy for type 2 diabetes mellitus. N Engl J Med 1999;341:924-925.
    • (1999) N Engl J Med , vol.341 , pp. 924-925
    • Hooper, P.L.1
  • 29
    • 39549093999 scopus 로고    scopus 로고
    • Fever-range whole body hyperthermia prevents the onset of type 1 diabetes in non-obese diabetic mice
    • Capitano ML, Ertel BR, Repasky EA, Ostberg JR. Fever-range whole body hyperthermia prevents the onset of type 1 diabetes in non-obese diabetic mice. Int J Hyperthermia 2008;24:141-149.
    • (2008) Int J Hyperthermia , vol.24 , pp. 141-149
    • Capitano, M.L.1    Ertel, B.R.2    Repasky, E.A.3    Ostberg, J.R.4
  • 31
    • 0033000493 scopus 로고    scopus 로고
    • Halothane, an inhalational anesthetic agent, increases folding stability of serum albumin
    • Tanner JW, Eckenhoff RG, Liebman PA. Halothane, an inhalational anesthetic agent, increases folding stability of serum albumin. Biochim Biophys Acta 1999;1430:46-56.
    • (1999) Biochim Biophys Acta , vol.1430 , pp. 46-56
    • Tanner, J.W.1    Eckenhoff, R.G.2    Liebman, P.A.3
  • 32
    • 13244253861 scopus 로고    scopus 로고
    • Anesthesia and post-mortem interval profoundly influence the regulatory serine phosphorylation of glycogen synthase kinase-3 in mouse brain
    • Li X, Friedman AB, Roh M-S, Jope RS. Anesthesia and post-mortem interval profoundly influence the regulatory serine phosphorylation of glycogen synthase kinase-3 in mouse brain. J Neurochem 2005;92:701-704.
    • (2005) J Neurochem , vol.92 , pp. 701-704
    • Li, X.1    Friedman, A.B.2    Roh, M.-S.3    Jope, R.S.4
  • 33
    • 33745059628 scopus 로고    scopus 로고
    • Tissue physiology and the response to heat
    • Horsman MR. Tissue physiology and the response to heat. Int J Hyperthermia 2006;22:197-203.
    • (2006) Int J Hyperthermia , vol.22 , pp. 197-203
    • Horsman, M.R.1
  • 34
    • 0028575781 scopus 로고
    • Heat shock and recovery protects pancreatic islets from warm ischemic injury
    • Perdrizet GA, Rewinski MJ, Schweizer RT, Scharp DW. Heat shock and recovery protects pancreatic islets from warm ischemic injury. Transplant Proc 1994;26:3477-3478.
    • (1994) Transplant Proc , vol.26 , pp. 3477-3478
    • Perdrizet, G.A.1    Rewinski, M.J.2    Schweizer, R.T.3    Scharp, D.W.4
  • 35
  • 36
    • 7744222195 scopus 로고    scopus 로고
    • Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability
    • Arispe N, Doh M, Simakova O, Kurganov B, De Maio A. Hsc70 And Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability. FASEB J 2004;18:1636-1645.
    • (2004) FASEB J , vol.18 , pp. 1636-1645
    • Arispe, N.1    Doh, M.2    Simakova, O.3    Kurganov, B.4    De Maio, A.5
  • 38
    • 33845913216 scopus 로고    scopus 로고
    • Intracellular and extracellular functions of heat shock proteins: Repercussions in cancer therapy
    • Schmitt E, Gehrmann M, Brunet M, Multhoff G, Garrido C. Intracellular and extracellular functions of heat shock proteins: Repercussions in cancer therapy. J Leukoc Biol 2007;81:15-27.
    • (2007) J Leukoc Biol , vol.81 , pp. 15-27
    • Schmitt, E.1    Gehrmann, M.2    Brunet, M.3    Multhoff, G.4    Garrido, C.5
  • 39
    • 34848859541 scopus 로고    scopus 로고
    • Heat shock protein 70 (Hsp70): Membrane location, export and immunological relevance
    • Multhoff G. Heat shock protein 70 (Hsp70): Membrane location, export and immunological relevance. Methods 2007;43:229-237.
    • (2007) Methods , vol.43 , pp. 229-237
    • Multhoff, G.1
  • 40
    • 34248358968 scopus 로고    scopus 로고
    • Extracellular heat shock protein 70 has novel functional effects on sea urchin eggs and coelomocytes
    • Browne CL, Swan JB, Rankin EE, Calvert H, Griffiths S, Tytell M. Extracellular heat shock protein 70 has novel functional effects on sea urchin eggs and coelomocytes. J Exp Biol 2007;210:1275-1287.
    • (2007) J Exp Biol , vol.210 , pp. 1275-1287
    • Browne, C.L.1    Swan, J.B.2    Rankin, E.E.3    Calvert, H.4    Griffiths, S.5    Tytell, M.6
  • 41
    • 33845382806 scopus 로고
    • Nonparametric estimation from incomplete observations
    • Kaplan EL, Meier P. Nonparametric estimation from incomplete observations. J Am Stat Assoc 1958;53: 457-481.
    • (1958) J Am Stat Assoc , vol.53 , pp. 457-481
    • Kaplan, E.L.1    Meier, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.