메뉴 건너뛰기




Volumn 111, Issue 5, 2010, Pages 1231-1243

Role of lysyl oxidase propeptide in secretion and enzyme activity

Author keywords

endoplasmic reticulum; ER associated protein degradation; glycosylation; lysyl oxidase; propeptide; subcellular localization

Indexed keywords

COMPLEMENTARY DNA; LYSYL OXIDASE PROPEPTIDE; PROTEIN LYSINE 6 OXIDASE; UNCLASSIFIED DRUG;

EID: 78649809075     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.22845     Document Type: Article
Times cited : (43)

References (45)
  • 1
    • 57749098804 scopus 로고    scopus 로고
    • Lysyl oxidase binds transforming growth factor-beta and regulates its signaling via amine oxidase activity
    • Atsawasuwan P, Mochida Y, Katafuchi M, Kaku M, Fong KSK, Csiszar K, Yamauchi M,. 2008. Lysyl oxidase binds transforming growth factor-beta and regulates its signaling via amine oxidase activity. J Biol Chem 283: 34229-34240.
    • (2008) J Biol Chem , vol.283 , pp. 34229-34240
    • Atsawasuwan, P.1    Mochida, Y.2    Katafuchi, M.3    Kaku, M.4    Fong, K.S.K.5    Csiszar, K.6    Yamauchi, M.7
  • 2
    • 0033208984 scopus 로고    scopus 로고
    • ER protein quality control and proteasome-mediated protein degradation
    • Brodsky JL, McCracken AA,. 1999. ER protein quality control and proteasome-mediated protein degradation. Semin Cell Dev Biol 10: 507-513.
    • (1999) Semin Cell Dev Biol , vol.10 , pp. 507-513
    • Brodsky, J.L.1    McCracken, A.A.2
  • 3
    • 0022309853 scopus 로고
    • Binding of lysyl oxidase to fibrils of type i collagen
    • Cronlund AL, Smith BD, Kagan HM,. 1985. Binding of lysyl oxidase to fibrils of type I collagen. Connect Tissue Res 14: 109-119.
    • (1985) Connect Tissue Res , vol.14 , pp. 109-119
    • Cronlund, A.L.1    Smith, B.D.2    Kagan, H.M.3
  • 4
    • 0028837996 scopus 로고
    • The proteolytic processing site of the precursor of lysyl oxidase
    • Cronshaw AD, Fothergill-Gilmore LA, Hulmes DJ,. 1995. The proteolytic processing site of the precursor of lysyl oxidase. Biochem J 306: 279-284.
    • (1995) Biochem J , vol.306 , pp. 279-284
    • Cronshaw, A.D.1    Fothergill-Gilmore, L.A.2    Hulmes, D.J.3
  • 5
    • 0035232015 scopus 로고    scopus 로고
    • Lysyl oxidases: A novel multifunctional amine oxidase family
    • Csiszar K,. 2001. Lysyl oxidases: A novel multifunctional amine oxidase family. Prog Nucleic Acid Res Mol Biol 70: 1-32.
    • (2001) Prog Nucleic Acid Res Mol Biol , vol.70 , pp. 1-32
    • Csiszar, K.1
  • 6
    • 33746208871 scopus 로고    scopus 로고
    • A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation
    • Denic V, Quan EM, Weissman JS,. 2006. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 126: 349-359.
    • (2006) Cell , vol.126 , pp. 349-359
    • Denic, V.1    Quan, E.M.2    Weissman, J.S.3
  • 7
    • 0035424237 scopus 로고    scopus 로고
    • ER quality control: Towards an understanding at the molecular level
    • Ellgaard L, Helenius A,. 2001. ER quality control: Towards an understanding at the molecular level. Curr Opin Cell Biol 13: 431-437.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 431-437
    • Ellgaard, L.1    Helenius, A.2
  • 8
    • 21644448430 scopus 로고    scopus 로고
    • Cellular fibronectin binds to lysyl oxidase with high affinity and is critical for its proteolytic activation
    • Fogelgren B, Polgar N, Szauter KM, Ujfaludi Z, Laczko R, Fong KS, Csiszar K,. 2005. Cellular fibronectin binds to lysyl oxidase with high affinity and is critical for its proteolytic activation. J Biol Chem 280: 24690-24697.
    • (2005) J Biol Chem , vol.280 , pp. 24690-24697
    • Fogelgren, B.1    Polgar, N.2    Szauter, K.M.3    Ujfaludi, Z.4    Laczko, R.5    Fong, K.S.6    Csiszar, K.7
  • 10
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a mis folded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond C, Helenius A,. 1994. Quality control in the secretory pathway: Retention of a mis folded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J Cell Biol 126: 41-52.
    • (1994) J Cell Biol , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 11
    • 0002347802 scopus 로고
    • Characterization and regulation of lysyl oxidase
    • Mecham R.P., editor. Orlando, FL: Academic Press. pp.
    • Kagan HM,. 1986. Characterization and regulation of lysyl oxidase. In:, Mecham RP, editor. Biology of extracellular matrix. Orlando, FL: Academic Press. pp 321-398.
    • (1986) Biology of Extracellular Matrix , pp. 321-398
    • Kagan, H.M.1
  • 12
    • 0029086204 scopus 로고
    • Isolation of active site peptides of lysyl oxidase
    • Kagan HM, Cai P,. 1995. Isolation of active site peptides of lysyl oxidase. Methods Enzymol 258: 122-132.
    • (1995) Methods Enzymol , vol.258 , pp. 122-132
    • Kagan, H.M.1    Cai, P.2
  • 13
    • 0037371153 scopus 로고    scopus 로고
    • Lysyl oxidase: Properties, specificity, and biological roles inside and outside of the cell
    • Kagan HM, Li W,. 2003. Lysyl oxidase: Properties, specificity, and biological roles inside and outside of the cell. J Cell Biochem 88: 660-672.
    • (2003) J Cell Biochem , vol.88 , pp. 660-672
    • Kagan, H.M.1    Li, W.2
  • 14
    • 0028787719 scopus 로고
    • Expression of lysyl oxidase from cDNA constructs in mammalian cells: The propeptide region is not essential to the folding and secretion of the functional enzyme
    • Kagan HM, Reddy VB, Panchenko MV, Nagan N, Boak AM, Gacheru SN, Thomas KM,. 1995. Expression of lysyl oxidase from cDNA constructs in mammalian cells: The propeptide region is not essential to the folding and secretion of the functional enzyme. J Cell Biochem 59: 329-338.
    • (1995) J Cell Biochem , vol.59 , pp. 329-338
    • Kagan, H.M.1    Reddy, V.B.2    Panchenko, M.V.3    Nagan, N.4    Boak, A.M.5    Gacheru, S.N.6    Thomas, K.M.7
  • 15
    • 33745496962 scopus 로고    scopus 로고
    • Ubiquitin-proteasome-dependent degradation of mammalian ER stearoyl-CoA desaturase
    • Kato H, Sakaki K, Mihara K,. 2006. Ubiquitin-proteasome-dependent degradation of mammalian ER stearoyl-CoA desaturase. J Cell Sci 119: 2342-2353.
    • (2006) J Cell Sci , vol.119 , pp. 2342-2353
    • Kato, H.1    Sakaki, K.2    Mihara, K.3
  • 17
    • 0033813351 scopus 로고    scopus 로고
    • Human bleomycin hydrolase regulates the secretion of amyloid precursor protein
    • Lefterov IM, Koldamova RP, Lazo JS,. 2000. Human bleomycin hydrolase regulates the secretion of amyloid precursor protein. FASEB J 14: 1837-1847.
    • (2000) FASEB J , vol.14 , pp. 1837-1847
    • Lefterov, I.M.1    Koldamova, R.P.2    Lazo, J.S.3
  • 19
    • 33750437433 scopus 로고    scopus 로고
    • Lysyl oxidase: An oxidative enzyme and effector of cell function
    • Lucero HA, Kagan HM,. 2006. Lysyl oxidase: An oxidative enzyme and effector of cell function. Cell Mol Life Sci 63: 2304-2316.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2304-2316
    • Lucero, H.A.1    Kagan, H.M.2
  • 21
    • 0037027504 scopus 로고    scopus 로고
    • Inactivation of the lysyl oxidase gene Lox leads to aortic aneurysms, cardiovascular dysfunction, and perinatal death in mice
    • Mäki JM, Räsänen J, Tikkanen H, Sormunen R, Mäkikallio K, Kivirikko KI, Soininen R,. 2002. Inactivation of the lysyl oxidase gene Lox leads to aortic aneurysms, cardiovascular dysfunction, and perinatal death in mice. Circulation 106: 2503-2509.
    • (2002) Circulation , vol.106 , pp. 2503-2509
    • Mäki, J.M.1    Räsänen, J.2    Tikkanen, H.3    Sormunen, R.4    Mäkikallio, K.5    Kivirikko, K.I.6    Soininen, R.7
  • 22
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng L, Mohan R, Kwok BH, Elofsson M, Sin N, Crews CM,. 1999. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc Natl Acad Sci USA 96: 10403-10408.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10403-10408
    • Meng, L.1    Mohan, R.2    Kwok, B.H.3    Elofsson, M.4    Sin, N.5    Crews, C.M.6
  • 23
    • 0041731993 scopus 로고    scopus 로고
    • Autocrine growth factor regulation of lysyl oxidase expression in transformed fibroblasts
    • Palamakumbura AH, Sommer P, Trackman PC,. 2003. Autocrine growth factor regulation of lysyl oxidase expression in transformed fibroblasts. J Biol Chem 278: 30781-30787.
    • (2003) J Biol Chem , vol.278 , pp. 30781-30787
    • Palamakumbura, A.H.1    Sommer, P.2    Trackman, P.C.3
  • 25
    • 0029863235 scopus 로고    scopus 로고
    • Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase
    • Panchenko MV, Stetler-Stevenson WG, Trubetskoy OV, Gacheru SN, Kagan HM,. 1996. Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase. J Biol Chem 271: 7113-7119.
    • (1996) J Biol Chem , vol.271 , pp. 7113-7119
    • Panchenko, M.V.1    Stetler-Stevenson, W.G.2    Trubetskoy, O.V.3    Gacheru, S.N.4    Kagan, H.M.5
  • 26
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi AJ,. 2000. Protein glucosylation and its role in protein folding. Annu Rev Biochem 69: 69-93.
    • (2000) Annu Rev Biochem , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 27
    • 34547769774 scopus 로고    scopus 로고
    • Paradoxical roles for lysyl oxidases in cancer-A prospect
    • Payne SL, Hendrix MJC, Kirschmann DA,. 2007. Paradoxical roles for lysyl oxidases in cancer-A prospect. J Cell Biochem 101: 1338-1354.
    • (2007) J Cell Biochem , vol.101 , pp. 1338-1354
    • Payne, S.L.1    Hendrix, M.J.C.2    Kirschmann, D.A.3
  • 29
    • 0025765996 scopus 로고
    • Removal of N-glycosylation sites of the yeast acid phosphatase severely affects protein folding
    • Riederer MA, Hinnen A,. 1991. Removal of N-glycosylation sites of the yeast acid phosphatase severely affects protein folding. J Bacteriol 173: 3539-3546.
    • (1991) J Bacteriol , vol.173 , pp. 3539-3546
    • Riederer, M.A.1    Hinnen, A.2
  • 31
    • 0034932144 scopus 로고    scopus 로고
    • Substrate-specific regulation of the ribosome-Translocation junction by N-terminal signal sequences
    • Rutkowski DT, Lingappa VR, Hegde RS,. 2001. Substrate-specific regulation of the ribosome-Translocation junction by N-terminal signal sequences. Proc Natl Acad Sci USA 98: 7823-7828.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7823-7828
    • Rutkowski, D.T.1    Lingappa, V.R.2    Hegde, R.S.3
  • 32
    • 0023880441 scopus 로고
    • Effect of glycosylation on the mechanism of renaturation of invertase from yeast
    • Schulke N, Schmid FX,. 1988. Effect of glycosylation on the mechanism of renaturation of invertase from yeast. J Biol Chem 263: 8832-8837.
    • (1988) J Biol Chem , vol.263 , pp. 8832-8837
    • Schulke, N.1    Schmid, F.X.2
  • 34
    • 33746778834 scopus 로고    scopus 로고
    • Rough sheets and smooth tubules
    • Shibata Y, Voeltz GK, Rapoport TA,. 2006. Rough sheets and smooth tubules. Cell 126: 435-439.
    • (2006) Cell , vol.126 , pp. 435-439
    • Shibata, Y.1    Voeltz, G.K.2    Rapoport, T.A.3
  • 36
    • 0026666773 scopus 로고
    • Post-translational glycosylation and proteolytic processing of a lysyl oxidase precursor
    • Trackman PC, Bedell-Hogan D, Tang J, Kagan HM,. 1992. Post-translational glycosylation and proteolytic processing of a lysyl oxidase precursor. J Biol Chem 267: 8666-8671.
    • (1992) J Biol Chem , vol.267 , pp. 8666-8671
    • Trackman, P.C.1    Bedell-Hogan, D.2    Tang, J.3    Kagan, H.M.4
  • 37
    • 0344393021 scopus 로고    scopus 로고
    • Quality control and protein folding in the secretory pathway
    • Trombetta ES, Parodi AJ,. 2003. Quality control and protein folding in the secretory pathway. Annu Rev Cell Dev Biol 19: 649-676.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 649-676
    • Trombetta, E.S.1    Parodi, A.J.2
  • 38
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai B, Ye Y, Rapoport TA,. 2002. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat Rev Mol Cell Biol 3: 246-255.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 39
    • 0035933765 scopus 로고    scopus 로고
    • Multiple bone morphogenetic protein 1-related mammalian metalloproteinases process pro-lysyl oxidase at the correct physiological site and control lysyl oxidase activation in mouse embryo fibroblast cultures
    • Uzel MI, Scott IC, Babakhanlou-Chase H, Palamakumbura AH, Pappano WN, Hong HH, Greenspan DS, Trackman PC,. 2001. Multiple bone morphogenetic protein 1-related mammalian metalloproteinases process pro-lysyl oxidase at the correct physiological site and control lysyl oxidase activation in mouse embryo fibroblast cultures. J Biol Chem 276: 22537-22543.
    • (2001) J Biol Chem , vol.276 , pp. 22537-22543
    • Uzel, M.I.1    Scott, I.C.2    Babakhanlou-Chase, H.3    Palamakumbura, A.H.4    Pappano, W.N.5    Hong, H.H.6    Greenspan, D.S.7    Trackman, P.C.8
  • 40
    • 0018676475 scopus 로고
    • Native cross-links in collagen fibrils induce resistance to human synovial collagenase
    • Vater CA, Harris ED, Siegel RC,. 1979. Native cross-links in collagen fibrils induce resistance to human synovial collagenase. Biochem J 181: 639-645.
    • (1979) Biochem J , vol.181 , pp. 639-645
    • Vater, C.A.1    Harris, E.D.2    Siegel, R.C.3
  • 42
    • 0022371312 scopus 로고
    • Assessment of lysyl oxidase variants by urea gel electrophoresis: Evidence against disulfide isomers as bases of the enzyme heterogeneity
    • Williams MA, Kagan HM,. 1985. Assessment of lysyl oxidase variants by urea gel electrophoresis: Evidence against disulfide isomers as bases of the enzyme heterogeneity. Anal Biochem 149: 430-437.
    • (1985) Anal Biochem , vol.149 , pp. 430-437
    • Williams, M.A.1    Kagan, H.M.2
  • 43
    • 34447120193 scopus 로고    scopus 로고
    • Repression of BCL2 by the tumor suppressor activity of the lysyl oxidase propeptide inhibits transformed phenotype of lung and pancreatic cancer cells
    • Wu M, Min C, Wang X, Yu Z, Kirsch KH, Trackman PC, Sonenshein GE,. 2007. Repression of BCL2 by the tumor suppressor activity of the lysyl oxidase propeptide inhibits transformed phenotype of lung and pancreatic cancer cells. Cancer Res 67: 6278-6285.
    • (2007) Cancer Res , vol.67 , pp. 6278-6285
    • Wu, M.1    Min, C.2    Wang, X.3    Yu, Z.4    Kirsch, K.H.5    Trackman, P.C.6    Sonenshein, G.E.7
  • 44
    • 30344462664 scopus 로고    scopus 로고
    • The role of the cathepsin e propeptide in correct folding, maturation and sorting to the endosome
    • Yasuda Y, Tsukuba T, Okamoto K, Kadowaki T, Yamamoto K,. 2005. The role of the cathepsin E propeptide in correct folding, maturation and sorting to the endosome. J Biochem 138: 621-630.
    • (2005) J Biochem , vol.138 , pp. 621-630
    • Yasuda, Y.1    Tsukuba, T.2    Okamoto, K.3    Kadowaki, T.4    Yamamoto, K.5
  • 45


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.