메뉴 건너뛰기




Volumn 44, Issue 1, 1998, Pages 15-20

Basal synthesis of heat shock protein 70 increases with age in rat kidneys

Author keywords

Heat shock protein 70; Pentosidine

Indexed keywords

HEAT SHOCK PROTEIN 70; MESSENGER RNA; RIBOSOME RNA;

EID: 0031986063     PISSN: 0304324X     EISSN: None     Source Type: Journal    
DOI: 10.1159/000021977     Document Type: Article
Times cited : (31)

References (37)
  • 1
    • 0001806571 scopus 로고
    • The stress response, function of the proteins, and perspectives
    • Morimoto RI, Tissières R, Georgopulos C (eds): Cold Spring Harbor, Cold Spring Harbor Press
    • Morimoto RI, Tissières R, Georgopulos C: The stress response, function of the proteins, and perspectives; in Morimoto RI, Tissières R, Georgopulos C (eds): Stress Proteins in Biology and Medicine. Cold Spring Harbor, Cold Spring Harbor Press, 1990, pp 1-36.
    • (1990) Stress Proteins in Biology and Medicine , pp. 1-36
    • Morimoto, R.I.1    Tissières, R.2    Georgopulos, C.3
  • 2
    • 0027135501 scopus 로고
    • The function of heat shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell DA, Lindquist S: The function of heat shock proteins in stress tolerance: Degradation and reactivation of damaged proteins. Annu Rev Genet 1993;27:437-496.
    • (1993) Annu Rev Genet , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 3
    • 0025737837 scopus 로고
    • Heat shock: The role of transient inducible responses in cell damage, transformation and differentiation
    • Morimoto RI: Heat shock: The role of transient inducible responses in cell damage, transformation and differentiation. Cancer Cells 1991; 3:295-301.
    • (1991) Cancer Cells , vol.3 , pp. 295-301
    • Morimoto, R.I.1
  • 4
    • 0028272883 scopus 로고
    • Biology of disease. Pathogenic effects of advanced glycosylation: Biochemical, biologic and clinical implications of diabetes and aging
    • Vlassara H, Bucala R, Striker L: Biology of disease. Pathogenic effects of advanced glycosylation: Biochemical, biologic and clinical implications of diabetes and aging. Lab Invest 1994; 70:138-151.
    • (1994) Lab Invest , vol.70 , pp. 138-151
    • Vlassara, H.1    Bucala, R.2    Striker, L.3
  • 6
    • 0024462566 scopus 로고
    • Diminished heat-shock protein synthesis following mitogen stimulation of lymphocytes from aged donors
    • Faassen AA, O'Leary JJ, Rodysill KJ, Bergh N, Hallgren HM: Diminished heat-shock protein synthesis following mitogen stimulation of lymphocytes from aged donors. Exp Cell Res 1989;183:326-334.
    • (1989) Exp Cell Res , vol.183 , pp. 326-334
    • Faassen, A.A.1    O'Leary, J.J.2    Rodysill, K.J.3    Bergh, N.4    Hallgren, H.M.5
  • 7
    • 0027390857 scopus 로고
    • Metallothionein expression and stress responses in aging human diploid fibroblasts
    • Luce MC, Schyberg JP, Bunn CL: Metallothionein expression and stress responses in aging human diploid fibroblasts, Exp Gerontol 1993;28:17-38.
    • (1993) Exp Gerontol , vol.28 , pp. 17-38
    • Luce, M.C.1    Schyberg, J.P.2    Bunn, C.L.3
  • 8
    • 0025738386 scopus 로고
    • Aging affects expression of 70 kDa heat shock proteins in Drosophila
    • Niedzwiecki A, Kongpachith AM, Fleming JE: Aging affects expression of 70 kDa heat shock proteins in Drosophila. J Biol Chem 1991;266: 9332-9338.
    • (1991) J Biol Chem , vol.266 , pp. 9332-9338
    • Niedzwiecki, A.1    Kongpachith, A.M.2    Fleming, J.E.3
  • 9
    • 0025836691 scopus 로고
    • Molecular events involved in transcriptional activation of heat shock genes become progressively refractory to heat stimulation during aging of human diploid fibroblasts
    • Liu AY-C, Choi H-S, Lee Y-K, Chen KY: Molecular events involved in transcriptional activation of heat shock genes become progressively refractory to heat stimulation during aging of human diploid fibroblasts. J Cell Physiol 1991; 149:560-566.
    • (1991) J Cell Physiol , vol.149 , pp. 560-566
    • Liu, A.Y.-C.1    Choi, H.-S.2    Lee, Y.-K.3    Chen, K.Y.4
  • 10
    • 0024022149 scopus 로고
    • Aging results in an unusual expression of Drosophila heat shock proteins
    • Fleming JE, Walton JK, Dubitsky R, Bensch G: Aging results in an unusual expression of Drosophila heat shock proteins. Proc Natl Acad Sci USA 1988;85:4099-4103.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4099-4103
    • Fleming, J.E.1    Walton, J.K.2    Dubitsky, R.3    Bensch, G.4
  • 11
    • 0025190717 scopus 로고
    • Decreased expression of heat shock protein 70 mRNA and protein after heat treatment in cells of aged rats
    • Fargnoli J, Kunisada T, Fornace AJ, Schneider EL, Holbrook NJ: Decreased expression of heat shock protein 70 mRNA and protein after heat treatment in cells of aged rats. Proc Natl Acad Sci USA 1990;87:846-850.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 846-850
    • Fargnoli, J.1    Kunisada, T.2    Fornace, A.J.3    Schneider, E.L.4    Holbrook, N.J.5
  • 12
    • 0027511556 scopus 로고
    • The effect of age on the synthesis of two heat shock proteins in the HSP70 family
    • Wu B, Gu MJ, Heydari AR, Richardson A: The effect of age on the synthesis of two heat shock proteins in the HSP70 family. J Gerontol 1993; 48:B50-B56.
    • (1993) J Gerontol , vol.48
    • Wu, B.1    Gu, M.J.2    Heydari, A.R.3    Richardson, A.4
  • 13
    • 0020324688 scopus 로고
    • Dietary protein intake and the progressive nature of kidney disease
    • Brenner BM, Meyer TW, Hostetter TH: Dietary protein intake and the progressive nature of kidney disease. N Engl J Med 1982;307: 652-659.
    • (1982) N Engl J Med , vol.307 , pp. 652-659
    • Brenner, B.M.1    Meyer, T.W.2    Hostetter, T.H.3
  • 14
    • 0007897203 scopus 로고
    • The aging kidney
    • Brockehurst JC, Tallis RC, Fillit HM (eds): Edinburgh, Churchill Livingstone
    • Fillit H, Rowe J: The aging kidney; in Brockehurst JC, Tallis RC, Fillit HM (eds): Textbook of Geriatric Medicine and Gerontology. Edinburgh, Churchill Livingstone, 1992, pp 612- 628.
    • (1992) Textbook of Geriatric Medicine and Gerontology , pp. 612-628
    • Fillit, H.1    Rowe, J.2
  • 16
    • 0000769573 scopus 로고
    • Isolation and functional analysis of a human 70,000-dalton heat shock protein gene segment
    • Vollemy R, Ahmed A, Schiller P, Bromley P, Rungger D: Isolation and functional analysis of a human 70,000-dalton heat shock protein gene segment. Proc Natl Acad Sci USA 1985;82: 4949-4953.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4949-4953
    • Vollemy, R.1    Ahmed, A.2    Schiller, P.3    Bromley, P.4    Rungger, D.5
  • 17
    • 0020577769 scopus 로고
    • Isolation and characterization of full-length cDNA clones for human alpha-, beta- and gamma-actin mRNAs: Skeletal but not cytoplasmic actins have amino terminal cysteine that is subsequently removed
    • Gunning P, Ponte P, Okayama H, Engel J, Blau H, Kedes L: Isolation and characterization of full-length cDNA clones for human alpha-, beta- and gamma-actin mRNAs: Skeletal but not cytoplasmic actins have amino terminal cysteine that is subsequently removed. Mol Cell Biol 1983;3:787-795.
    • (1983) Mol Cell Biol , vol.3 , pp. 787-795
    • Gunning, P.1    Ponte, P.2    Okayama, H.3    Engel, J.4    Blau, H.5    Kedes, L.6
  • 19
    • 0023690359 scopus 로고
    • Increased expression of basement membrane components in human endothelial cells cultured in high glucose
    • Cagliero E, Maiello M, Boeri D, Roy S, Lorenzi M: Increased expression of basement membrane components in human endothelial cells cultured in high glucose. J Clin Invest 1988;82: 735-738.
    • (1988) J Clin Invest , vol.82 , pp. 735-738
    • Cagliero, E.1    Maiello, M.2    Boeri, D.3    Roy, S.4    Lorenzi, M.5
  • 20
    • 0026501919 scopus 로고
    • Chromatographic quantitation of plasma and erythrocyte pentosidine in diabetic and uremic subjects
    • Odetti P, Fogarty J, Sell DR, Monnier VM: Chromatographic quantitation of plasma and erythrocyte pentosidine in diabetic and uremic subjects. Diabetes 1992;41:153-159.
    • (1992) Diabetes , vol.41 , pp. 153-159
    • Odetti, P.1    Fogarty, J.2    Sell, D.R.3    Monnier, V.M.4
  • 21
    • 0000573558 scopus 로고
    • Expression and function of vertebrate HSP70 genes
    • Morimoto RI, Tissières R, Georgopulos C (eds): Cold Spring Harbor, Cold Spring Harbor Press
    • Morimoto RI, Milarski KM: Expression and function of vertebrate HSP70 genes; in Morimoto RI, Tissières R, Georgopulos C (eds): Stress Proteins in Biology and Medicine. Cold Spring Harbor, Cold Spring Harbor Press, 1990, pp 323-359.
    • (1990) Stress Proteins in Biology and Medicine , pp. 323-359
    • Morimoto, R.I.1    Milarski, K.M.2
  • 22
    • 0027325351 scopus 로고
    • HSP23 and HSP26 exhibit distinct spatial and temporal patterns of constitutive expression in Drosophila adults
    • Marin R, Valet JP, Tanguay RM: HSP23 and HSP26 exhibit distinct spatial and temporal patterns of constitutive expression in Drosophila adults. Dev Genet 1993;14:69-77.
    • (1993) Dev Genet , vol.14 , pp. 69-77
    • Marin, R.1    Valet, J.P.2    Tanguay, R.M.3
  • 23
    • 0025185228 scopus 로고
    • Age-dependent decrease in the heat-inducible DNA sequence-specific binding activity in human diploid fibroblasts
    • Choi H-S, Lin Z, Li B, Liu AY-C: Age-dependent decrease in the heat-inducible DNA sequence-specific binding activity in human diploid fibroblasts. J Biol Chem 1990;265:18005- 18011.
    • (1990) J Biol Chem , vol.265 , pp. 18005-18011
    • Choi, H.-S.1    Lin, Z.2    Li, B.3    Liu, A.Y.-C.4
  • 25
    • 0021720972 scopus 로고
    • HMGCo A reductase: A negatively regulated gene activation with unusual promoter and 5′ prime untranslated regions
    • Reynolds GA, Basu SK, OsborneTF, Chin DJ, Gil G, Brown MS, Goldstein JL, Luskey KL: HMGCo A reductase: A negatively regulated gene activation with unusual promoter and 5′ prime untranslated regions. Cell 1984;38:275- 285.
    • (1984) Cell , vol.38 , pp. 275-285
    • Reynolds, G.A.1    Basu, S.K.2    Osborne, T.F.3    Chin, D.J.4    Gil, G.5    Brown, M.S.6    Goldstein, J.L.7    Luskey, K.L.8
  • 26
    • 0025301808 scopus 로고
    • r 70,000 heat shock genes in control or heat shock leukemic cells as correlated to their heat response
    • r 70,000 heat shock genes in control or heat shock leukemic cells as correlated to their heat response. Cancer Res 1990;50:2877-2884.
    • (1990) Cancer Res , vol.50 , pp. 2877-2884
    • Mivechi, N.F.1    Rossi, J.J.2
  • 27
    • 0028207948 scopus 로고
    • Stress response of senescent T lymphocytes: Reduced HSP 70 is independent of the proliferative block
    • Effros RB, Zu X, Walford RL: Stress response of senescent T lymphocytes: Reduced HSP 70 is independent of the proliferative block. J Gerontol 1994;49:B65-B70.
    • (1994) J Gerontol , vol.49
    • Effros, R.B.1    Zu, X.2    Walford, R.L.3
  • 28
    • 0006849332 scopus 로고
    • Expression of human HSP70 during the synthetic phase of the cell cycle
    • Milarski KM, Morimoto RI: Expression of human HSP70 during the synthetic phase of the cell cycle. Proc Natl Acad Sci USA 1986;83: 9517-9521.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 9517-9521
    • Milarski, K.M.1    Morimoto, R.I.2
  • 29
    • 0026060017 scopus 로고
    • Heat shock proteins and cell proliferation
    • Pechan PM: Heat shock proteins and cell proliferation. FEBS Lett 1991;280:1-4.
    • (1991) FEBS Lett , vol.280 , pp. 1-4
    • Pechan, P.M.1
  • 30
    • 0020807840 scopus 로고
    • Protein synthesis and degradation during aging and senescence
    • Macrides SC: Protein synthesis and degradation during aging and senescence. Biol Rev 1983;58:343-422.
    • (1983) Biol Rev , vol.58 , pp. 343-422
    • Macrides, S.C.1
  • 31
    • 0024852380 scopus 로고
    • Structure elucidation of a fluorescent crosslink from human senescent extracellular matrix: Implication of pentoses in the aging process
    • Sell DR, Monnier VM: Structure elucidation of a fluorescent crosslink from human senescent extracellular matrix: Implication of pentoses in the aging process. J Biol Chem 1989;264: 21597-21602.
    • (1989) J Biol Chem , vol.264 , pp. 21597-21602
    • Sell, D.R.1    Monnier, V.M.2
  • 32
    • 0010672991 scopus 로고
    • RNA and protein metabolism
    • Finch CE, Schneider EL (eds): New York, Van Nostrand Reinhold
    • Reff ME: RNA and protein metabolism; in Finch CE, Schneider EL (eds): Handbook of the Biology of Aging. New York, Van Nostrand Reinhold, 1985, pp 225-254.
    • (1985) Handbook of the Biology of Aging , pp. 225-254
    • Reff, M.E.1
  • 33
    • 0022211777 scopus 로고
    • Stress-induced proteins in chondrocytes from patients with osteoarthritis
    • Kubo T, Towle CA, Mankin HJ, Treadwell BV: Stress-induced proteins in chondrocytes from patients with osteoarthritis. Arthritis Rheum 1985;28:1140-1145.
    • (1985) Arthritis Rheum , vol.28 , pp. 1140-1145
    • Kubo, T.1    Towle, C.A.2    Mankin, H.J.3    Treadwell, B.V.4
  • 34
    • 0022546075 scopus 로고
    • Ischemia of the dog heart induces the appearance of a cardiac mRNA coding for a protein with migration characteristics similar to heat shock/stress protein 71
    • Dillman WH, Metha HB, Barrieux A, Guth BD, Neeley WE, Ross J Jr: Ischemia of the dog heart induces the appearance of a cardiac mRNA coding for a protein with migration characteristics similar to heat shock/stress protein 71. Circ Res 1986;59:110-114.
    • (1986) Circ Res , vol.59 , pp. 110-114
    • Dillman, W.H.1    Metha, H.B.2    Barrieux, A.3    Guth, B.D.4    Neeley, W.E.5    Ross Jr., J.6
  • 36
    • 0027218225 scopus 로고
    • Induced expression of heat shock protein on biliary epithelium in patients with primary sclerosing cholangitis and primary biliary cirrhosis
    • Broomé U, Scheynius A, Hultcrantz R: Induced expression of heat shock protein on biliary epithelium in patients with primary sclerosing cholangitis and primary biliary cirrhosis. Hepatology 1993;18:298-303.
    • (1993) Hepatology , vol.18 , pp. 298-303
    • Broomé, U.1    Scheynius, A.2    Hultcrantz, R.3
  • 37
    • 0022636655 scopus 로고
    • Activation of hemin-regulated initiation factor kinase in heat- shocked HELA cells
    • De Benedetti A, Baglioni C: Activation of hemin-regulated initiation factor kinase in heat- shocked HELA cells. J Biol Chem 1986;261: 338-342.
    • (1986) J Biol Chem , vol.261 , pp. 338-342
    • De Benedetti, A.1    Baglioni, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.