메뉴 건너뛰기




Volumn 110, Issue 51, 2013, Pages 20467-20472

Human resistin, a proinflammatory cytokine, shows chaperone-like activity

Author keywords

Chaperokine; Protein folding

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; CHAPERONE; CITRATE SYNTHASE; RECOMBINANT HORMONE; RESISTIN; THAPSIGARGIN; TUNICAMYCIN;

EID: 84890841657     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1306145110     Document Type: Article
Times cited : (39)

References (33)
  • 1
    • 0035905758 scopus 로고    scopus 로고
    • The hormone resistin links obesity to diabetes
    • Steppan CM, et al. (2001) The hormone resistin links obesity to diabetes. Nature 409(6818):307-312.
    • (2001) Nature , vol.409 , Issue.6818 , pp. 307-312
    • Steppan, C.M.1
  • 2
    • 0037427540 scopus 로고    scopus 로고
    • Resistin is expressed in human macrophages and directly regulated by PPAR gamma activators
    • Patel L, et al. (2003) Resistin is expressed in human macrophages and directly regulated by PPAR gamma activators. Biochem Biophys Res Commun 300(2):472-476.
    • (2003) Biochem Biophys Res Commun , vol.300 , Issue.2 , pp. 472-476
    • Patel, L.1
  • 3
    • 0242320395 scopus 로고    scopus 로고
    • Circulating resistin levels are not associated with obesity or insulin resistance in humans and are not regulated by fasting or leptin administration: Crosssectional and interventional studies in normal, insulin-Resistant, and diabetic subjects
    • Lee JH, et al. (2003) Circulating resistin levels are not associated with obesity or insulin resistance in humans and are not regulated by fasting or leptin administration: Crosssectional and interventional studies in normal, insulin-Resistant, and diabetic subjects. J Clin Endocrinol Metab 88(10):4848-4856.
    • (2003) J Clin Endocrinol Metab , vol.88 , Issue.10 , pp. 4848-4856
    • Lee, J.H.1
  • 4
    • 23044439100 scopus 로고    scopus 로고
    • Human resistin stimulates the pro-Inflammatory cytokines TNFalpha and IL-12 in macrophages by NF-KappaB-Dependent pathway
    • Silswal N, et al. (2005) Human resistin stimulates the pro-Inflammatory cytokines TNFalpha and IL-12 in macrophages by NF-KappaB-Dependent pathway. Biochem Biophys Res Commun 334(4):1092-1101.
    • (2005) Biochem Biophys Res Commun , vol.334 , Issue.4 , pp. 1092-1101
    • Silswal, N.1
  • 5
    • 33745171469 scopus 로고    scopus 로고
    • Role of resistin in inflammation and inflammation-Related diseases
    • Pang SS, Le YY (2006) Role of resistin in inflammation and inflammation-Related diseases. Cell Mol Immunol 3(1):29-34.
    • (2006) Cell Mol Immunol , vol.3 , Issue.1 , pp. 29-34
    • Pang, S.S.1    Le, Y.Y.2
  • 6
    • 0042925580 scopus 로고    scopus 로고
    • Resistin messenger-RNA expression is increased by proinflammatory cytokines in vitro
    • Kaser S, et al. (2003) Resistin messenger-RNA expression is increased by proinflammatory cytokines in vitro. Biochem Biophys Res Commun 309(2):286-290.
    • (2003) Biochem Biophys Res Commun , vol.309 , Issue.2 , pp. 286-290
    • Kaser, S.1
  • 7
    • 15744399190 scopus 로고    scopus 로고
    • An inflammatory cascade leading to hyperresistinemia in humans
    • Lehrke M, et al. (2004) An inflammatory cascade leading to hyperresistinemia in humans. PLoS Med 1(2):e45.
    • (2004) PLoS Med , vol.1 , Issue.2
    • Lehrke, M.1
  • 8
    • 0037434632 scopus 로고    scopus 로고
    • The genomic organization of mouse resistin reveals major differences from the human resistin: Functional implications
    • Ghosh S, Singh AK, Aruna B, Mukhopadhyay S, Ehtesham NZ (2003) The genomic organization of mouse resistin reveals major differences from the human resistin: Functional implications. Gene 305(1):27-34.
    • (2003) Gene , vol.305 , Issue.1 , pp. 27-34
    • Ghosh, S.1    Singh, A.K.2    Aruna, B.3    Mukhopadhyay, S.4    Ehtesham, N.Z.5
  • 9
    • 0042820167 scopus 로고    scopus 로고
    • Human recombinant resistin protein displays a tendency to aggregate by forming intermolecular disulfide linkages
    • Aruna B, et al. (2003) Human recombinant resistin protein displays a tendency to aggregate by forming intermolecular disulfide linkages. Biochemistry 42(36):10554-10559.
    • (2003) Biochemistry , vol.42 , Issue.36 , pp. 10554-10559
    • Aruna, B.1
  • 10
    • 56749128040 scopus 로고    scopus 로고
    • Biophysical analyses of human resistin: Oligomer formation suggests novel biological function
    • Aruna B, et al. (2008) Biophysical analyses of human resistin: Oligomer formation suggests novel biological function. Biochemistry 47(47):12457-12466.
    • (2008) Biochemistry , vol.47 , Issue.47 , pp. 12457-12466
    • Aruna, B.1
  • 11
    • 79952390552 scopus 로고    scopus 로고
    • Correlation of membrane binding and hydrophobicity to the chaperone-Like activity of PDC-109, the major protein of bovine seminal plasma
    • Sankhala RS, Damai RS, Swamy MJ (2011) Correlation of membrane binding and hydrophobicity to the chaperone-Like activity of PDC-109, the major protein of bovine seminal plasma. PLoS ONE 6(3):e17330.
    • (2011) PLoS ONE , vol.6 , Issue.3
    • Sankhala, R.S.1    Damai, R.S.2    Swamy, M.J.3
  • 12
    • 0028981330 scopus 로고
    • Alpha-Crystallin can act as a chaperone under conditions of oxidative stress
    • Wang K, Spector A (1995) Alpha-Crystallin can act as a chaperone under conditions of oxidative stress. Invest Ophthalmol Vis Sci 36(2):311-321.
    • (1995) Invest Ophthalmol Vis Sci , vol.36 , Issue.2 , pp. 311-321
    • Wang, K.1    Spector, A.2
  • 13
    • 68049125092 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress regulates adipocyte resistin expression
    • Lefterova MI, et al. (2009) Endoplasmic reticulum stress regulates adipocyte resistin expression. Diabetes 58(8):1879-1886.
    • (2009) Diabetes , vol.58 , Issue.8 , pp. 1879-1886
    • Lefterova, M.I.1
  • 14
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234(3):779-815.
    • (1993) J Mol Biol , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 15
    • 84890816445 scopus 로고
    • Assaying proteins for molecular chaperone activity
    • eds Galbraith DW, Bourque DP, Bohnert HJ Academic Press London; New York; Orlando, FL; San Diego 3 555
    • Garrett JL (1995) Assaying proteins for molecular chaperone activity. Methods in Plant Cell Biology, eds Galbraith DW, Bourque DP, Bohnert HJ (Academic Press, London; New York; Orlando, FL; San Diego), pp ii-Xxii, 3-555.
    • (1995) Methods in Plant Cell Biology , pp. 2-22
    • Garrett, J.L.1
  • 16
    • 0025382818 scopus 로고
    • The molecular chaperone concept
    • Ellis RJ (1990) The molecular chaperone concept. Semin Cell Biol 1(1):1-9.
    • (1990) Semin Cell Biol , vol.1 , Issue.1 , pp. 1-9
    • Ellis, R.J.1
  • 17
    • 70350457983 scopus 로고    scopus 로고
    • Facilitated oligomerization of mycobacterial GroEL: Evidence for phosphorylation-Mediated oligomerization
    • Kumar CM, et al. (2009) Facilitated oligomerization of mycobacterial GroEL: Evidence for phosphorylation-Mediated oligomerization. J Bacteriol 191(21):6525-6538.
    • (2009) J Bacteriol , vol.191 , Issue.21 , pp. 6525-6538
    • Kumar, C.M.1
  • 18
    • 0141868801 scopus 로고    scopus 로고
    • Comparative studies of resistin expression and phylogenomics in human and mouse
    • Yang RZ, et al. (2003) Comparative studies of resistin expression and phylogenomics in human and mouse. Biochem Biophys Res Commun 310(3):927-935.
    • (2003) Biochem Biophys Res Commun , vol.310 , Issue.3 , pp. 927-935
    • Yang, R.Z.1
  • 19
    • 0029124685 scopus 로고
    • Temperature-Induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-Crystallin
    • Das KP, Surewicz WK (1995) Temperature-Induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-Crystallin. FEBS Lett 369(2-3): 321-325.
    • (1995) FEBS Lett , vol.369 , Issue.2-3 , pp. 321-325
    • Das, K.P.1    Surewicz, W.K.2
  • 20
    • 84855826057 scopus 로고    scopus 로고
    • Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: Studies on the structure and chaperone function using mutant mimics
    • Nagaraj RH, et al. (2012) Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: Studies on the structure and chaperone function using mutant mimics. PLoS ONE 7(1):e30257.
    • (2012) PLoS ONE , vol.7 , Issue.1
    • Nagaraj, R.H.1
  • 21
    • 39149143645 scopus 로고    scopus 로고
    • Chaperone machines in action
    • Saibil HR (2008) Chaperone machines in action. Curr Opin Struct Biol 18(1):35-42.
    • (2008) Curr Opin Struct Biol , vol.18 , Issue.1 , pp. 35-42
    • Saibil, H.R.1
  • 22
    • 0034719136 scopus 로고    scopus 로고
    • Clusterin is an ATP-Independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-Competent state
    • Poon S, Easterbrook-Smith SB, Rybchyn MS, Carver JA, Wilson MR (2000) Clusterin is an ATP-Independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-Competent state. Biochemistry 39(51):15953-15960.
    • (2000) Biochemistry , vol.39 , Issue.51 , pp. 15953-15960
    • Poon, S.1    Easterbrook-Smith, S.B.2    Rybchyn, M.S.3    Carver, J.A.4    Wilson, M.R.5
  • 23
    • 79952363991 scopus 로고    scopus 로고
    • Genetic selection designed to stabilize proteins uncovers a chaperone called Spy
    • Quan S, et al. (2011) Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nat Struct Mol Biol 18(3):262-269.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.3 , pp. 262-269
    • Quan, S.1
  • 24
    • 0036085697 scopus 로고    scopus 로고
    • Cross-Talk between cellular stress, cell cycle and anticancer agents: Mechanistic aspects
    • Tiligada E, Miligkos V, Delitheos A (2002) Cross-Talk between cellular stress, cell cycle and anticancer agents: Mechanistic aspects. Curr Med Chem Anticancer Agents 2(4): 553-566.
    • (2002) Curr Med Chem Anticancer Agents , vol.2 , Issue.4 , pp. 553-566
    • Tiligada, E.1    Miligkos, V.2    Delitheos, A.3
  • 25
    • 23944470067 scopus 로고    scopus 로고
    • DNA damage signals facilitate osmotic stress adaptation
    • Kültz D (2005) DNA damage signals facilitate osmotic stress adaptation. Am J Physiol Renal Physiol 289(3):F504-F505.
    • (2005) Am J Physiol Renal Physiol , vol.289 , Issue.3 , pp. 504-505
    • Kültz, D.1
  • 26
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • Marciniak SJ, Ron D (2006) Endoplasmic reticulum stress signaling in disease. Physiol Rev 86(4):1133-1149.
    • (2006) Physiol Rev , vol.86 , Issue.4 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 27
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier L, Usherwood YK, Chung KT, Hendershot LM (2002) A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13(12):4456-4469.
    • (2002) Mol Biol Cell , vol.13 , Issue.12 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 28
    • 34249287709 scopus 로고    scopus 로고
    • Pronounced elevation of resistin correlates with severity of disease in severe sepsis and septic shock
    • Sundén-Cullberg J, et al. (2007) Pronounced elevation of resistin correlates with severity of disease in severe sepsis and septic shock. Crit Care Med 35(6):1536-1542.
    • (2007) Crit Care Med , vol.35 , Issue.6 , pp. 1536-1542
    • Sundén-Cullberg, J.1
  • 29
    • 79960260454 scopus 로고    scopus 로고
    • Treatment end point determinants for pulmonary tuberculosis: Human resistin as a surrogate biomarker
    • Ehtesham NZ, et al. (2011) Treatment end point determinants for pulmonary tuberculosis: Human resistin as a surrogate biomarker. Tuberculosis (Edinb) 91(4):293-299.
    • (2011) Tuberculosis (Edinb) , vol.91 , Issue.4 , pp. 293-299
    • Ehtesham, N.Z.1
  • 30
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-Induced cell death through its E3 ubiquitin-Protein ligase activity
    • Imai Y, Soda M, Takahashi R (2000) Parkin suppresses unfolded protein stress-Induced cell death through its E3 ubiquitin-Protein ligase activity. J Biol Chem 275(46): 35661-35664.
    • (2000) J Biol Chem , vol.275 , Issue.46 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 31
    • 47949099916 scopus 로고    scopus 로고
    • From endoplasmic-Reticulum stress to the inflammatory response
    • Zhang K, Kaufman RJ (2008) From endoplasmic-Reticulum stress to the inflammatory response. Nature 454(7203):455-462.
    • (2008) Nature , vol.454 , Issue.7203 , pp. 455-462
    • Zhang, K.1    Kaufman, R.J.2
  • 32
    • 70349972139 scopus 로고    scopus 로고
    • The role of resistin as a regulator of inflammation: Implications for various human pathologies
    • Filková M, Haluzík M, Gay S, Senolt L (2009) The role of resistin as a regulator of inflammation: Implications for various human pathologies. Clin Immunol 133(2): 157-170.
    • (2009) Clin Immunol , vol.133 , Issue.2 , pp. 157-170
    • Filková, M.1    Haluzík, M.2    Gay, S.3    Senolt, L.4
  • 33
    • 68349129102 scopus 로고    scopus 로고
    • Biophysical characterization and unfolding of LEF4 factor of RNA polymerase from AcNPV
    • Rasheedi S, et al. (2009) Biophysical characterization and unfolding of LEF4 factor of RNA polymerase from AcNPV. Biopolymers 91(7):574-582.
    • (2009) Biopolymers , vol.91 , Issue.7 , pp. 574-582
    • Rasheedi, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.