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Volumn 366, Issue 4, 2008, Pages 1048-1053

Dysfunction of the ER chaperone BiP accelerates the renal tubular injury

Author keywords

Caspase 12; Chaperone; Endoplasmic reticulum stress; Protein overload nephropathy; Tubular interstitial injury

Indexed keywords

CASPASE 12; GLUCOSE REGULATED PROTEIN 78;

EID: 37549033821     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.12.098     Document Type: Article
Times cited : (83)

References (27)
  • 1
    • 0036176161 scopus 로고    scopus 로고
    • K/DOQI clinical practice guidelines for chronic kidney disease: evaluation, classification, and stratification. Am. J. Kidney Dis. 39 (2002) S1-266.
  • 4
    • 0029782625 scopus 로고    scopus 로고
    • Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia
    • Kuznetsov G., Bush K.T., Zhang P.L., and Nigam S.K. Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia. Proc. Natl. Acad. Sci. USA 93 (1996) 8584-8589
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8584-8589
    • Kuznetsov, G.1    Bush, K.T.2    Zhang, P.L.3    Nigam, S.K.4
  • 6
    • 27744500069 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-associated caspase 12 mediates cisplatin-induced LLC-PK1 cell apoptosis
    • Liu H., and Baliga R. Endoplasmic reticulum stress-associated caspase 12 mediates cisplatin-induced LLC-PK1 cell apoptosis. J. Am. Soc. Nephrol. 16 (2005) 1985-1992
    • (2005) J. Am. Soc. Nephrol. , vol.16 , pp. 1985-1992
    • Liu, H.1    Baliga, R.2
  • 7
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., and Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8 (2007) 519-529
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 8
    • 0032190546 scopus 로고    scopus 로고
    • Cloning of mammalian Ire1 reveals diversity in the ER stress responses
    • Wang X.Z., Harding H.P., Zhang Y., Jolicoeur E.M., Kuroda M., and Ron D. Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J. 17 (1998) 5708-5717
    • (1998) EMBO J. , vol.17 , pp. 5708-5717
    • Wang, X.Z.1    Harding, H.P.2    Zhang, Y.3    Jolicoeur, E.M.4    Kuroda, M.5    Ron, D.6
  • 9
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state
    • McCullough K.D., Martindale J.L., Klotz L.O., Aw T.Y., and Holbrook N.J. Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol. Cell. Biol. 21 (2001) 1249-1259
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.O.3    Aw, T.Y.4    Holbrook, N.J.5
  • 10
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano F., Wang X., Bertolotti A., Zhang Y., Chung P., Harding H.P., and Ron D. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287 (2000) 664-666
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 11
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T., and Tohyama M. Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J. Biol. Chem. 276 (2001) 13935-13940
    • (2001) J. Biol. Chem. , vol.276 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3    Yui, D.4    Gomi, F.5    Katayama, T.6    Tohyama, M.7
  • 14
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • Marciniak S.J., and Ron D. Endoplasmic reticulum stress signaling in disease. Physiol. Rev. 86 (2006) 1133-1149
    • (2006) Physiol. Rev. , vol.86 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 15
    • 0028862992 scopus 로고
    • Two redundant systems maintain levels of resident proteins within the yeast endoplasmic reticulum
    • Beh C.T., and Rose M.D. Two redundant systems maintain levels of resident proteins within the yeast endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 92 (1995) 9820-9823
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9820-9823
    • Beh, C.T.1    Rose, M.D.2
  • 17
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S., and Pelham H.R. A C-terminal signal prevents secretion of luminal ER proteins. Cell 48 (1987) 899-907
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 18
    • 0025187298 scopus 로고
    • A human homologue of the yeast HDEL receptor
    • Lewis M.J., and Pelham H.R. A human homologue of the yeast HDEL receptor. Nature 348 (1990) 162-163
    • (1990) Nature , vol.348 , pp. 162-163
    • Lewis, M.J.1    Pelham, H.R.2
  • 19
    • 10644278579 scopus 로고    scopus 로고
    • Targeted deletion of angiotensin II type 1A receptor does not protect mice from progressive nephropathy of overload proteinuria
    • Benigni A., Corna D., Zoja C., Longaretti L., Gagliardini E., Perico N., Coffman T.M., and Remuzzi G. Targeted deletion of angiotensin II type 1A receptor does not protect mice from progressive nephropathy of overload proteinuria. J. Am. Soc. Nephrol. 15 (2004) 2666-2674
    • (2004) J. Am. Soc. Nephrol. , vol.15 , pp. 2666-2674
    • Benigni, A.1    Corna, D.2    Zoja, C.3    Longaretti, L.4    Gagliardini, E.5    Perico, N.6    Coffman, T.M.7    Remuzzi, G.8
  • 20
    • 0032159827 scopus 로고    scopus 로고
    • Macrophages, myofibroblasts, and extracellular matrix accumulation in interstitial fibrosis of chronic progressive nephropathy in aged rats
    • Nakatsuji S., Yamate J., and Sakuma S. Macrophages, myofibroblasts, and extracellular matrix accumulation in interstitial fibrosis of chronic progressive nephropathy in aged rats. Vet. Pathol. 35 (1998) 352-360
    • (1998) Vet. Pathol. , vol.35 , pp. 352-360
    • Nakatsuji, S.1    Yamate, J.2    Sakuma, S.3
  • 21
    • 0032512094 scopus 로고    scopus 로고
    • Pathophysiology of progressive nephropathies
    • Remuzzi G., and Bertani T. Pathophysiology of progressive nephropathies. N. Engl. J. Med. 339 (1998) 1448-1456
    • (1998) N. Engl. J. Med. , vol.339 , pp. 1448-1456
    • Remuzzi, G.1    Bertani, T.2
  • 22
    • 0031952093 scopus 로고    scopus 로고
    • Tubulointerstitial disease in aging: evidence for underlying peritubular capillary damage, a potential role for renal ischemia
    • Thomas S.E., Anderson S., Gordon K.L., Oyama T.T., Shankland S.J., and Johnson R.J. Tubulointerstitial disease in aging: evidence for underlying peritubular capillary damage, a potential role for renal ischemia. J. Am. Soc. Nephrol. 9 (1998) 231-242
    • (1998) J. Am. Soc. Nephrol. , vol.9 , pp. 231-242
    • Thomas, S.E.1    Anderson, S.2    Gordon, K.L.3    Oyama, T.T.4    Shankland, S.J.5    Johnson, R.J.6
  • 23
    • 0024519366 scopus 로고
    • Age-related nephropathy and proteinuria in rats with intact kidneys exposed to diets with different protein content
    • Bertani T., Zoja C., Abbate M., Rossini M., and Remuzzi G. Age-related nephropathy and proteinuria in rats with intact kidneys exposed to diets with different protein content. Lab. Invest. 60 (1989) 196-204
    • (1989) Lab. Invest. , vol.60 , pp. 196-204
    • Bertani, T.1    Zoja, C.2    Abbate, M.3    Rossini, M.4    Remuzzi, G.5
  • 25
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen B., and Braakman I. Protein folding and quality control in the endoplasmic reticulum. Curr. Opin. Cell Biol. 16 (2004) 343-349
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.