메뉴 건너뛰기




Volumn 49, Issue 9, 2008, Pages 3961-3969

Cultured porcine trabecular meshwork cells display altered lysosomal function when subjected to chronic oxidative stress

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; CATHEPSIN; LEUPEPTIN; LIPOFUSCIN; MESSENGER RNA; REACTIVE OXYGEN METABOLITE; OXYGEN;

EID: 53149093231     PISSN: 01460404     EISSN: 15525783     Source Type: Journal    
DOI: 10.1167/iovs.08-1915     Document Type: Article
Times cited : (45)

References (61)
  • 1
    • 37349078627 scopus 로고    scopus 로고
    • Risk Factors for Incident Open-angle Glaucoma. the Barbados Eye Studies
    • DOI 10.1016/j.ophtha.2007.03.017, PII S0161642007002424
    • Leske MC, Wu SY, Hennis A, Honkanen R, Nemesure B. Risk factors for incident open-angle glaucoma: the Barbados Eye Studies. Ophthalmology. 2008;115:85-93. (Pubitemid 350309410)
    • (2008) Ophthalmology , vol.115 , Issue.1 , pp. 85-93
    • Leske, M.C.1    Wu, S.-Y.2    Hennis, A.3    Honkanen, R.4    Nemesure, B.5
  • 2
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman KB, Ames BN. The free radical theory of aging matures. Physiol Rev. 1998;78:547-581. (Pubitemid 28182903)
    • (1998) Physiological Reviews , vol.78 , Issue.2 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 3
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • Harman D. Aging: a theory based on free radical and radiation chemistry. J Gerontol. 1956;11:298-300.
    • (1956) J Gerontol , vol.11 , pp. 298-300
    • Harman, D.1
  • 4
    • 26044482960 scopus 로고    scopus 로고
    • Protein oxidation and degradation during postmitotic senescence
    • DOI 10.1016/j.freeradbiomed.2005.06.009, PII S0891584905003539
    • Grune T, Merker K, Jung T, Sitte N, Davies KJ. Protein oxidation and degradation during postmitotic senescence. Free Radic Biol Med. 2005;39:1208-1215. (Pubitemid 41407714)
    • (2005) Free Radical Biology and Medicine , vol.39 , Issue.9 , pp. 1208-1215
    • Grune, T.1    Merker, K.2    Jung, T.3    Sitte, N.4    Davies, K.J.A.5
  • 5
    • 33644641768 scopus 로고    scopus 로고
    • Oxidative stress, accumulation of biological 'garbage', and aging
    • DOI 10.1089/ars.2006.8.197
    • Terman A, Brunk UT. Oxidative stress, accumulation of biological 'garbage', and aging. Antioxid Redox Signal. 2006;8:197-204. (Pubitemid 43324546)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.1-2 , pp. 197-204
    • Terman, A.1    Brunk, U.T.2
  • 6
    • 4544322045 scopus 로고    scopus 로고
    • Free radicals and aging
    • Barja G. Free radicals and aging. Trends Neurosci. 2004;27:595-600.
    • (2004) Trends Neurosci , vol.27 , pp. 595-600
    • Barja, G.1
  • 7
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • DOI 10.1016/S0891-5849(00)00317-8, PII S0891584900003178
    • Cadenas E, Davies KJ. Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med. 2000;29:222-230. (Pubitemid 30734905)
    • (2000) Free Radical Biology and Medicine , vol.29 , Issue.3-4 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.A.2
  • 8
    • 0036709816 scopus 로고    scopus 로고
    • Oxidative stress hypothesis of aging
    • Sohal RS. Oxidative stress hypothesis of aging. Free Radic Biol Med. 2002;33:573-574.
    • (2002) Free Radic Biol Med , vol.33 , pp. 573-574
    • Sohal, R.S.1
  • 9
    • 0028883513 scopus 로고
    • Free radicals and aging of anterior segment tissues of the eye: A hypothesis
    • Green K. Free radicals and aging of anterior segment tissues of the eye: a hypothesis. Ophthalmic Res. 1995;27(suppl 1):143-149.
    • (1995) Ophthalmic Res , vol.27 , Issue.SUPPL. 1 , pp. 143-149
    • Green, K.1
  • 10
    • 34247266702 scopus 로고    scopus 로고
    • Oxidative stress in glaucoma: A burden of evidence
    • DOI 10.1097/01.ijg.0000243480.67532.1b, PII 0006119820070500000012
    • Kumar DM, Agarwal N. Oxidative stress in glaucoma: a burden of evidence. J Glaucoma. 2007;16:334-343. (Pubitemid 46626062)
    • (2007) Journal of Glaucoma , vol.16 , Issue.3 , pp. 334-343
    • Maneesh Kumar, D.1    Agarwal, N.2
  • 11
    • 33846810059 scopus 로고    scopus 로고
    • Glaucomatous outflow pathway and oxidative stress
    • DOI 10.1016/j.exer.2006.10.008, PII S0014483506004155
    • Sacca SC, Izzotti A, Rossi P, Traverso C. Glaucomatous outflow pathway and oxidative stress. Exp Eye Res. 2007;84:389-399. (Pubitemid 46210055)
    • (2007) Experimental Eye Research , vol.84 , Issue.3 , pp. 389-399
    • Sacca, S.C.1    Izzotti, A.2    Rossi, P.3    Traverso, C.4
  • 13
    • 0042206639 scopus 로고    scopus 로고
    • Association of increased autophagic inclusions labeled for beta-galactosidase with fibroblastic aging
    • DOI 10.1016/S0531-5565(03)00132-3
    • Gerland LM, Peyrol S, Lallemand C, Branche R, Magaud JP, Ffrench M. Association of increased autophagic inclusions labeled for beta-galactosidase with fibroblastic aging. Exp Gerontol. 2003;38:887-895. (Pubitemid 36952670)
    • (2003) Experimental Gerontology , vol.38 , Issue.8 , pp. 887-895
    • Gerland, L.-M.1    Peyrol, S.2    Lallemand, C.3    Branche, R.4    Magaud, J.-P.5    Ffrench, M.6
  • 14
    • 0033730616 scopus 로고    scopus 로고
    • Senescence-associated beta-galactosidase reflects an increase in lysosomal mass during replicative ageing of human endothelial cells
    • Kurz DJ, Decary S, Hong Y, Erusalimsky JD. Senescence-associated (beta)-galactosidase reflects an increase in lysosomal mass during replicative ageing of human endothelial cells. J Cell Sci. 2000;113:3613-3622. (Pubitemid 30838285)
    • (2000) Journal of Cell Science , vol.113 , Issue.20 , pp. 3613-3622
    • Kurz, D.J.1    Decary, S.2    Hong, Y.3    Erusalimsky, J.D.4
  • 15
    • 26244445013 scopus 로고    scopus 로고
    • The limitations and validities of senescence associated-beta- galactosidase activity as an aging marker for human foreskin fibroblast Hs68 cells
    • Yang NC, Hu ML. The limitations and validities of senescence associated-beta-galactosidase activity as an aging marker for human foreskin fibroblast Hs68 cells. Exp Gerontol. 2005;40:813-819.
    • (2005) Exp Gerontol , vol.40 , pp. 813-819
    • Yang, N.C.1    Hu, M.L.2
  • 16
    • 0001944263 scopus 로고    scopus 로고
    • How do intracellular proteolytic systems change with age?
    • Cuervo AM, Dice JF. How do intracellular proteolytic systems change with age? Front Biosci. 1998;3:D25-D43.
    • (1998) Front Biosci , vol.3
    • Cuervo, A.M.1    Dice, J.F.2
  • 17
    • 0034113064 scopus 로고    scopus 로고
    • When lysosomes get old
    • Cuervo AM, Dice JF. When lysosomes get old. Exp Gerontol. 2000;35:119-131.
    • (2000) Exp Gerontol , vol.35 , pp. 119-131
    • Cuervo, A.M.1    Dice, J.F.2
  • 19
    • 0141650806 scopus 로고    scopus 로고
    • Aging, lipofuscin formation, and free radical-mediated inhibition of cellular proteolytic systems
    • DOI 10.1016/S1568-1637(03)00028-X
    • Szweda PA, Camouse M, Lundberg KC, Oberley TD, Szweda LI. Aging, lipofuscin formation, and free radical-mediated inhibition of cellular proteolytic systems. Ageing Res Rev. 2003;2:383-405. (Pubitemid 37159400)
    • (2003) Ageing Research Reviews , vol.2 , Issue.4 , pp. 383-405
    • Szweda, P.A.1    Camouse, M.2    Lundberg, K.C.3    Oberley, T.D.4    Szweda, L.I.5
  • 20
    • 0036830228 scopus 로고    scopus 로고
    • The neuropathogenic contributions of lysosomal dysfunction
    • Bahr BA, Bendiske J. The neuropathogenic contributions of lysosomal dysfunction. J Neurochem. 2002;83:481-489.
    • (2002) J Neurochem , vol.83 , pp. 481-489
    • Bahr, B.A.1    Bendiske, J.2
  • 22
    • 33644658460 scopus 로고    scopus 로고
    • Oxidative stress and lysosomes: CNS-related consequences and implications for lysosomal enhancement strategies and induction of autophagy
    • DOI 10.1089/ars.2006.8.185
    • Butler D, Bahr BA. Oxidative stress and lysosomes: CNS-related consequences and implications for lysosomal enhancement strategies and induction of autophagy. Antioxid Redox Signal. 2006;8:185-196. (Pubitemid 43324545)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.1-2 , pp. 185-196
    • Butler, D.1    Bahr, B.A.2
  • 23
    • 34047265829 scopus 로고    scopus 로고
    • Effects of lipid peroxidation-related protein modifications on RPE lysosomal functions and POS phagocytosis
    • DOI 10.1167/iovs.06-0549
    • Kaemmerer E, Schutt F, Krohne TU, Holz FG, Kopitz J. Effects of lipid peroxidation-related protein modifications on RPE lysosomal functions and POS phagocytosis. Invest Ophthalmol Vis Sci. 2007;48:1342-1347. (Pubitemid 351261433)
    • (2007) Investigative Ophthalmology and Visual Science , vol.48 , Issue.3 , pp. 1342-1347
    • Kaemmerer, E.1    Schutt, F.2    Krohne, T.U.3    Holz, F.G.4    Kopitz, J.5
  • 26
    • 38449091923 scopus 로고    scopus 로고
    • The autophagy-lysosomal degradation pathway: Role in neurodegenerative disease and therapy
    • DOI 10.2741/2714
    • Shacka JJ, Roth KA, Zhang J. The autophagy-lysosomal degradation pathway: role in neurodegenerative disease and therapy. Front Biosci. 2008;13:718-736. (Pubitemid 351599777)
    • (2008) Frontiers in Bioscience , vol.13 , Issue.2 , pp. 718-736
    • Shacka, J.J.1    Roth, K.A.2    Zhang, J.3
  • 28
    • 0028836002 scopus 로고
    • Monodansylcadaverine (MDC) is a specific in vivo marker for autophagic vacuoles
    • Biederbick A, Kern HF, Elsasser HP. Monodansylcadaverine (MDC) is a specific in vivo marker for autophagic vacuoles. Eur J Cell Biol. 1995;66:3-14.
    • (1995) Eur J Cell Biol , vol.66 , pp. 3-14
    • Biederbick, A.1    Kern, H.F.2    Elsasser, H.P.3
  • 30
    • 33847747817 scopus 로고    scopus 로고
    • Expression of cathepsin K is regulated by shear stress in cultured endothelial cells and is increased in endothelium in human atherosclerosis
    • Platt MO, Ankeny RF, Shi GP, et al. Expression of cathepsin K is regulated by shear stress in cultured endothelial cells and is increased in endothelium in human atherosclerosis. Am J Physiol Heart Circ Physiol. 2007;292:H1479-H1486.
    • (2007) Am J Physiol Heart Circ Physiol , vol.292
    • Platt, M.O.1    Ankeny, R.F.2    Shi, G.P.3
  • 31
    • 0021676154 scopus 로고
    • Effects of the protease inhibitor leupeptin on proteolytic activities and regeneration of mouse skeletal muscles after exercise injuries
    • Salminen A. Effects of the protease inhibitor leupeptin on proteolytic activities and regeneration of mouse skeletal muscles after exercise injuries. Am J Pathol. 1984;117:64-70. (Pubitemid 15200367)
    • (1984) American Journal of Pathology , vol.117 , Issue.1 , pp. 64-70
    • Salminen, A.1
  • 32
    • 0029439509 scopus 로고
    • Oxidative stress: The paradox of aerobic life
    • Davies KJ. Oxidative stress: the paradox of aerobic life. Biochem Soc Symp. 1995;61:1-31.
    • (1995) Biochem Soc Symp , vol.61 , pp. 1-31
    • Davies, K.J.1
  • 33
    • 0036628724 scopus 로고    scopus 로고
    • Role of oxidative stress and protein oxidation in the aging process
    • Sohal RS. Role of oxidative stress and protein oxidation in the aging process. Free Radic Biol Med. 2002;33:37-44.
    • (2002) Free Radic Biol Med , vol.33 , pp. 37-44
    • Sohal, R.S.1
  • 37
    • 0032169551 scopus 로고    scopus 로고
    • Ceroid/lipofuscin formation in cultured human fibroblasts: The role of oxidative stress and lysosomal proteolysis
    • DOI 10.1016/S0047-6374(98)00073-6, PII S0047637498000736
    • Terman A, Brunk UT. Ceroid/lipofuscin formation in cultured human fibroblasts: the role of oxidative stress and lysosomal proteolysis. Mech Ageing Dev. 1998;104:277-291. (Pubitemid 28472901)
    • (1998) Mechanisms of Ageing and Development , vol.104 , Issue.3 , pp. 277-291
    • Terman, A.1    Brunk, U.T.2
  • 38
    • 33744462609 scopus 로고    scopus 로고
    • Oxidative stress induces intralysosomal accumulation of alzheimer amyloid beta-protein in cultured neuroblastoma cells
    • DOI 10.1196/annals.1354.032
    • Zheng L, Roberg K, Jerhammar F, Marcusson J, Terman A. Oxidative stress induces intralysosomal accumulation of Alzheimer amyloid beta-protein in cultured neuroblastoma cells. Ann N Y Acad Sci. 2006;1067:248-251. (Pubitemid 43806332)
    • (2006) Annals of the New York Academy of Sciences , vol.1067 , Issue.1 , pp. 248-251
    • Zheng, L.1    Roberg, K.2    Jerhammar, F.3    Marcusson, J.4    Terman, A.5
  • 40
    • 0002255786 scopus 로고
    • Functional anatomy of the anterior chamber angle
    • Jakobiec FJ, ed. Philadelphia: Harper and Row
    • Tripathi R, Tripathi B. Functional anatomy of the anterior chamber angle. In: Jakobiec FJ, ed. Ocular Anatomy, Embryology, and Teratology. Philadelphia: Harper and Row; 1982;197-248.
    • (1982) Ocular Anatomy, Embryology, and Teratology , pp. 197-248
    • Tripathi, R.1    Tripathi, B.2
  • 42
    • 0028886612 scopus 로고
    • Age-related changes in cellular localization and enzymatic activities of cathepsins B, L and D in the rat trigeminal ganglion neuron
    • Amano T, Nakanishi H, Kondo T, Tanaka T, Oka M, Yamamoto K. Age-related changes in cellular localization and enzymatic activities of cathepsins B, L and D in the rat trigeminal ganglion neuron. Mech Ageing Dev. 1995;83:133-141.
    • (1995) Mech Ageing Dev , vol.83 , pp. 133-141
    • Amano, T.1    Nakanishi, H.2    Kondo, T.3    Tanaka, T.4    Oka, M.5    Yamamoto, K.6
  • 43
    • 0033745870 scopus 로고    scopus 로고
    • Increased expression of mature cathepsin B in aging rat liver
    • Keppler D, Walter R, Perez C, Sierra F. Increased expression of mature cathepsin B in aging rat liver. Cell Tissue Res. 2000;302:181-188. (Pubitemid 30839457)
    • (2000) Cell and Tissue Research , vol.302 , Issue.2 , pp. 181-188
    • Keppler, D.1    Walter, R.2    Perez, C.3    Sierra, F.4
  • 44
    • 0031022255 scopus 로고    scopus 로고
    • Increased expression of cathepsins e and D in neurons of the aged rat brain and their colocalization with lipofuscin and carboxy-terminal fragments of Alzheimer amyloid precursor protein
    • Nakanishi H, Amano T, Sastradipura DF, et al. Increased expression of cathepsins E and D in neurons of the aged rat brain and their colocalization with lipofuscin and carboxy-terminal fragments of Alzheimer amyloid precursor protein. J Neurochem. 1997;68:739-749. (Pubitemid 27044739)
    • (1997) Journal of Neurochemistry , vol.68 , Issue.2 , pp. 739-749
    • Nakanishi, H.1    Amano, T.2    Sastradipura, D.F.3    Yoshimine, Y.4    Tsukuba, T.5    Tanabe, K.6    Hirotsu, I.7    Ohono, T.8    Yamamoto, K.9
  • 45
    • 0034766880 scopus 로고    scopus 로고
    • Inhibition of RPE lysosomal and antioxidant activity by the age pigment lipofuscin
    • Shamsi FA, Boulton M. Inhibition of RPE lysosomal and antioxidant activity by the age pigment lipofuscin. Invest Ophthalmol Vis Sci. 2001;42:3041-3046. (Pubitemid 33035307)
    • (2001) Investigative Ophthalmology and Visual Science , vol.42 , Issue.12 , pp. 3041-3046
    • Shamsi, F.A.1    Boulton, M.2
  • 46
    • 0035127395 scopus 로고    scopus 로고
    • Biosynthesis and processing of cathepsin K in cultured human osteoclasts
    • Rieman DJ, McClung HA, Dodds RA, et al. Biosynthesis and processing of cathepsin K in cultured human osteoclasts. Bone. 2001;28:282-289.
    • (2001) Bone , vol.28 , pp. 282-289
    • Rieman, D.J.1    McClung, H.A.2    Dodds, R.A.3
  • 47
    • 0036929283 scopus 로고    scopus 로고
    • Processing and activation of lysosomal proteinases
    • Ishidoh K, Kominami E. Processing and activation of lysosomal proteinases. Biol Chem. 2002;383:1827-1831.
    • (2002) Biol Chem , vol.383 , pp. 1827-1831
    • Ishidoh, K.1    Kominami, E.2
  • 48
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: Multifunctional enzymes in cancer
    • Mohamed MM, Sloane BF. Cysteine cathepsins: multifunctional enzymes in cancer. Nat Rev Cancer. 2006;6:764-775.
    • (2006) Nat Rev Cancer , vol.6 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 50
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • DOI 10.1093/emboj/20.17.4629
    • Turk V, Turk B, Turk D. Lysosomal cysteine proteases: facts and opportunities. EMBO J. 2001;20:4629-4633. (Pubitemid 32848615)
    • (2001) EMBO Journal , vol.20 , Issue.17 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 51
    • 0018149312 scopus 로고
    • The waste-product theory of aging: Waste dilution by cell division
    • Hirsch HR. The waste-product theory of aging: waste dilution by cell division. Mech Ageing Dev. 1978;8:51-62.
    • (1978) Mech Ageing Dev , vol.8 , pp. 51-62
    • Hirsch, H.R.1
  • 54
    • 38849127441 scopus 로고    scopus 로고
    • Isolevuglandin-modified proteins, including elevated levels of inactive calpain-1, accumulate in glaucomatous trabecular meshwork
    • DOI 10.1021/bi701517m
    • Govindarajan B, Laird J, Salomon RG, Bhattacharya SK. Isolevuglandin-modified proteins, including elevated levels of inactive calpain-1, accumulate in glaucomatous trabecular meshwork. Biochemistry. 2008;47:817-825. (Pubitemid 351195453)
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 817-825
    • Govindarajan, B.1    Laird, J.2    Salomon, R.G.3    Bhattacharya, S.K.4
  • 55
    • 33744957641 scopus 로고    scopus 로고
    • Advanced atherosclerotic foam cell formation has features of an acquired lysosomal storage disorder
    • Jerome WG. Advanced atherosclerotic foam cell formation has features of an acquired lysosomal storage disorder. Rejuvenation Res. 2006;9:245-255.
    • (2006) Rejuvenation Res , vol.9 , pp. 245-255
    • Jerome, W.G.1
  • 56
    • 2442648066 scopus 로고    scopus 로고
    • Inhibition of the ATP-driven proton pump in RPE lysosomes by the major lipofuscin fluorophore A2-E may contribute to the pathogenesis of age-related macular degeneration
    • Bergmann M, Schutt F, Holz FG, Kopitz J. Inhibition of the ATP-driven proton pump in RPE lysosomes by the major lipofuscin fluorophore A2-E may contribute to the pathogenesis of age-related macular degeneration. FASEB J. 2004;18:562-564.
    • (2004) FASEB J , vol.18 , pp. 562-564
    • Bergmann, M.1    Schutt, F.2    Holz, F.G.3    Kopitz, J.4
  • 61
    • 0025765168 scopus 로고
    • Lysosomal enzyme activity in human aqueous humor
    • Weinreb RN, Jeng S, Miller AL. Lysosomal enzyme activity in human aqueous humor. Clin Chim Acta. 1991;199:1-5.
    • (1991) Clin Chim Acta , vol.199 , pp. 1-5
    • Weinreb, R.N.1    Jeng, S.2    Miller, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.