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Volumn 276, Issue 7, 2009, Pages 1891-1899

Proteolytic processing of porcine deoxyribonuclease II occurs in lysosomes but is not required for enzyme activation

Author keywords

Chloroquine; Cycloheximide; DNase II; Lysosome; Post translational processing

Indexed keywords

COMPLEMENTARY DNA; CYCLOHEXIMIDE; DEOXYRIBONUCLEASE II; RECOMBINANT ENZYME;

EID: 62149143606     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.06915.x     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 0014321776 scopus 로고
    • A comparative study of acid deoxyribonucleases extracted from different tissues and species
    • Cordonnier C Bernardi G (1968) A comparative study of acid deoxyribonucleases extracted from different tissues and species. Can J Biochem 46, 989 995.
    • (1968) Can J Biochem , vol.46 , pp. 989-995
    • Cordonnier, C.1    Bernardi, G.2
  • 2
    • 0026509553 scopus 로고
    • Human urine deoxyribonuclease II (DNase II) isoenzymes: A novel immunoaffinity purification, biochemical multiplicity, genetic heterogeneity and broad distribution among tissues and body fluids
    • Yasuda T, Nadano D, Awazu S Kishi K (1992) Human urine deoxyribonuclease II (DNase II) isoenzymes: a novel immunoaffinity purification, biochemical multiplicity, genetic heterogeneity and broad distribution among tissues and body fluids. Biochim Biophys Acta 1119, 185 193.
    • (1992) Biochim Biophys Acta , vol.1119 , pp. 185-193
    • Yasuda, T.1    Nadano, D.2    Awazu, S.3    Kishi, K.4
  • 4
    • 0015500455 scopus 로고
    • Isolation of deoxyribonuclease II of rat liver lysosomes
    • Dulaney JT Touster O (1972) Isolation of deoxyribonuclease II of rat liver lysosomes. J Biol Chem 247, 1424 1432.
    • (1972) J Biol Chem , vol.247 , pp. 1424-1432
    • Dulaney, J.T.1    Touster, O.2
  • 5
    • 0024576873 scopus 로고
    • Deoxyribonuclease II purified from the isolated lysosomes of porcine spleen and from porcine liver homogenates. Comparison with deoxyribonuclease II purified from porcine spleen homogenates
    • Liao TH, Liao WC, Chang HC Lu KS (1989) Deoxyribonuclease II purified from the isolated lysosomes of porcine spleen and from porcine liver homogenates. Comparison with deoxyribonuclease II purified from porcine spleen homogenates. Biochim Biophys Acta 1007, 15 22.
    • (1989) Biochim Biophys Acta , vol.1007 , pp. 15-22
    • Liao, T.H.1    Liao, W.C.2    Chang, H.C.3    Lu, K.S.4
  • 7
    • 0033571449 scopus 로고    scopus 로고
    • Role of macrophage lysosomal enzymes in the degradation of nucleosomes of apoptotic cells
    • Odaka C Mizuochi T (1999) Role of macrophage lysosomal enzymes in the degradation of nucleosomes of apoptotic cells. J Immunol 163, 5346 5352.
    • (1999) J Immunol , vol.163 , pp. 5346-5352
    • Odaka, C.1    Mizuochi, T.2
  • 9
    • 0036040938 scopus 로고    scopus 로고
    • Up-regulation of human deoxyribonuclease II gene expression during myelomonocytic differentiation of HL-60 and THP-1 cells
    • Chou SF, Chen HL Lu SC (2002) Up-regulation of human deoxyribonuclease II gene expression during myelomonocytic differentiation of HL-60 and THP-1 cells. Biochem Biophys Res Commun 296, 48 53.
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 48-53
    • Chou, S.F.1    Chen, H.L.2    Lu, S.C.3
  • 11
    • 0022238107 scopus 로고
    • The subunit structure and active site sequence of porcine spleen deoxyribonuclease
    • Liao TH (1985) The subunit structure and active site sequence of porcine spleen deoxyribonuclease. J Biol Chem 260, 10708 10713.
    • (1985) J Biol Chem , vol.260 , pp. 10708-10713
    • Liao, T.H.1
  • 12
    • 14444274100 scopus 로고    scopus 로고
    • Porcine spleen deoxyribonuclease II. Covalent structure, cDNA sequence, molecular cloning, and gene expression
    • Wang CC, Lu SC, Chen HL Liao TH (1998) Porcine spleen deoxyribonuclease II. Covalent structure, cDNA sequence, molecular cloning, and gene expression. J Biol Chem 273, 17192 17198.
    • (1998) J Biol Chem , vol.273 , pp. 17192-17198
    • Wang, C.C.1    Lu, S.C.2    Chen, H.L.3    Liao, T.H.4
  • 15
    • 33748350938 scopus 로고    scopus 로고
    • Identification of three crucial histidine residues (His115, His132 and His297) in porcine deoxyribonuclease II
    • Cheng YC, Hsueh CC, Lu SC Liao TH (2006) Identification of three crucial histidine residues (His115, His132 and His297) in porcine deoxyribonuclease II. Biochem J 398, 177 185.
    • (2006) Biochem J , vol.398 , pp. 177-185
    • Cheng, Y.C.1    Hsueh, C.C.2    Lu, S.C.3    Liao, T.H.4
  • 16
    • 0019796999 scopus 로고
    • The effect of chloroquine on lysosomal function and cell-coat glycoprotein transport in the absorptive cells of cultured human small-intestinal tissue
    • Blok J, Mulder-Stapel AA, Ginsel LA Daems WT (1981) The effect of chloroquine on lysosomal function and cell-coat glycoprotein transport in the absorptive cells of cultured human small-intestinal tissue. Cell Tissue Res 218, 227 251.
    • (1981) Cell Tissue Res , vol.218 , pp. 227-251
    • Blok, J.1    Mulder-Stapel, A.A.2    Ginsel, L.A.3    Daems, W.T.4
  • 17
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma S Poole B (1978) Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc Natl Acad Sci USA 75, 3327 3331.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 18
    • 0020973226 scopus 로고
    • Inhibitors of lysosomal function
    • Seglen PO (1983) Inhibitors of lysosomal function. Meth Enzymol 96, 737 764.
    • (1983) Meth Enzymol , vol.96 , pp. 737-764
    • Seglen, P.O.1
  • 19
    • 50649106648 scopus 로고    scopus 로고
    • Cathepsin D - Many functions of one aspartic protease
    • Benes P, Vetvicka V Fusek M (2008) Cathepsin D - many functions of one aspartic protease. Crit Rev Oncol Hematol 68, 12 28.
    • (2008) Crit Rev Oncol Hematol , vol.68 , pp. 12-28
    • Benes, P.1    Vetvicka, V.2    Fusek, M.3
  • 20
    • 34548059220 scopus 로고    scopus 로고
    • Cathepsin D deficiency and NCL/Batten disease: There's more to death than apoptosis
    • Shacka JJ Roth KA (2007) Cathepsin D deficiency and NCL/Batten disease: there's more to death than apoptosis. Autophagy 3, 474 476.
    • (2007) Autophagy , vol.3 , pp. 474-476
    • Shacka, J.J.1    Roth, K.A.2
  • 21
    • 0018903866 scopus 로고
    • Biosynthesis of lysosomal enzymes in fibroblasts. Synthesis as precursors of higher molecular weight
    • Hasilik A Neufeld EF (1980) Biosynthesis of lysosomal enzymes in fibroblasts. Synthesis as precursors of higher molecular weight. J Biol Chem 255, 4937 4945.
    • (1980) J Biol Chem , vol.255 , pp. 4937-4945
    • Hasilik, A.1    Neufeld, E.F.2
  • 22
    • 0019412485 scopus 로고
    • Transport and processing of lysosomal enzymes by smooth muscle cells and endothelial cells
    • Hasilik A, Voss B Von Figura K (1981) Transport and processing of lysosomal enzymes by smooth muscle cells and endothelial cells. Exp Cell Res 133, 23 30.
    • (1981) Exp Cell Res , vol.133 , pp. 23-30
    • Hasilik, A.1    Voss, B.2    Von Figura, K.3
  • 23
    • 0020559445 scopus 로고
    • Biosynthesis and transport of lysosomal enzymes in human monocytes and macrophages. Effects of ammonium chloride, zymosan and tunicamycin
    • Imort M, Zuhlsdorf M, Feige U, Hasilik A von Figura K (1983) Biosynthesis and transport of lysosomal enzymes in human monocytes and macrophages. Effects of ammonium chloride, zymosan and tunicamycin. Biochem J 214, 671 678.
    • (1983) Biochem J , vol.214 , pp. 671-678
    • Imort, M.1    Zuhlsdorf, M.2    Feige, U.3    Hasilik, A.4    Von Figura, K.5
  • 24
    • 0020538837 scopus 로고
    • Biosynthesis and transport of cathepsin D in cultured human fibroblasts
    • Gieselmann V, Pohlmann R, Hasilik A Von Figura K (1983) Biosynthesis and transport of cathepsin D in cultured human fibroblasts. J Cell Biol 97, 1 5.
    • (1983) J Cell Biol , vol.97 , pp. 1-5
    • Gieselmann, V.1    Pohlmann, R.2    Hasilik, A.3    Von Figura, K.4
  • 25
    • 0024451999 scopus 로고
    • Isolation of procathepsin D from mature cathepsin D by pepstatin affinity chromatography. Autocatalytic proteolysis of the zymogen form of the enzyme
    • Conner GE (1989) Isolation of procathepsin D from mature cathepsin D by pepstatin affinity chromatography. Autocatalytic proteolysis of the zymogen form of the enzyme. Biochem J 263, 601 604.
    • (1989) Biochem J , vol.263 , pp. 601-604
    • Conner, G.E.1
  • 26
    • 0019887728 scopus 로고
    • Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases
    • Green GD Shaw E (1981) Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases. J Biol Chem 256, 1923 1928.
    • (1981) J Biol Chem , vol.256 , pp. 1923-1928
    • Green, G.D.1    Shaw, E.2
  • 27
    • 0021269154 scopus 로고
    • Enhanced degradation of cathepsin D synthesized in the presence of the threonine analog beta-hydroxynorvaline
    • Hentze M, Hasilik A von Figura K (1984) Enhanced degradation of cathepsin D synthesized in the presence of the threonine analog beta-hydroxynorvaline. Arch Biochem Biophys 230, 375 382.
    • (1984) Arch Biochem Biophys , vol.230 , pp. 375-382
    • Hentze, M.1    Hasilik, A.2    Von Figura, K.3
  • 28
    • 0021978631 scopus 로고
    • Processing of human cathepsin D in lysosomes in vitro
    • Gieselmann V, Hasilik A von Figura K (1985) Processing of human cathepsin D in lysosomes in vitro. J Biol Chem 260, 3215 3220.
    • (1985) J Biol Chem , vol.260 , pp. 3215-3220
    • Gieselmann, V.1    Hasilik, A.2    Von Figura, K.3
  • 29
    • 0023653476 scopus 로고
    • Identification of a precursor form of cathepsin D in microsomal lumen: Characterization of enzymatic activation and proteolytic
    • Nishimura Y, Higaki M Kato K (1987) Identification of a precursor form of cathepsin D in microsomal lumen: characterization of enzymatic activation and proteolytic. Biochem Biophys Res Commun 148, 335 343.
    • (1987) Biochem Biophys Res Commun , vol.148 , pp. 335-343
    • Nishimura, Y.1    Higaki, M.2    Kato, K.3
  • 31
    • 0036296304 scopus 로고    scopus 로고
    • Revised structure of the active form of human deoxyribonuclease IIalpha
    • MacLea KS, Krieser RJ Eastman A (2002) Revised structure of the active form of human deoxyribonuclease IIalpha. Biochem Biophy Res Commun 292, 415 421.
    • (2002) Biochem Biophy Res Commun , vol.292 , pp. 415-421
    • MacLea, K.S.1    Krieser, R.J.2    Eastman, A.3
  • 32
    • 0027932822 scopus 로고
    • Differential sorting of lysosomal enzymes in mannose 6-phosphate receptor-deficient fibroblasts
    • Ludwig T, Munier-Lehmann H, Bauer U, Hollinshead M, Ovitt C, Lobel P Hoflack B (1994) Differential sorting of lysosomal enzymes in mannose 6-phosphate receptor-deficient fibroblasts. EMBO J 13, 3430 3437.
    • (1994) EMBO J , vol.13 , pp. 3430-3437
    • Ludwig, T.1    Munier-Lehmann, H.2    Bauer, U.3    Hollinshead, M.4    Ovitt, C.5    Lobel, P.6    Hoflack, B.7
  • 33
    • 0030016181 scopus 로고    scopus 로고
    • Autophosphorylation of the Fes tyrosine kinase. Evidence for an intermolecular mechanism involving two kinase domain tyrosine residues
    • Rogers JA, Read RD, Li J, Peters KL Smithgall TE (1996) Autophosphorylation of the Fes tyrosine kinase. Evidence for an intermolecular mechanism involving two kinase domain tyrosine residues. J Biol Chem 271, 17519 17525.
    • (1996) J Biol Chem , vol.271 , pp. 17519-17525
    • Rogers, J.A.1    Read, R.D.2    Li, J.3    Peters, K.L.4    Smithgall, T.E.5
  • 34
    • 8544271925 scopus 로고
    • Measurements of deoxyribonuclease activities in human serum and urine with metachromatic agar-diffusion method
    • Shen PM, Su YK, Lin SM, Kao JT Liao TH (1993) Measurements of deoxyribonuclease activities in human serum and urine with metachromatic agar-diffusion method. J Chin Biochem Soc 22, 99 107.
    • (1993) J Chin Biochem Soc , vol.22 , pp. 99-107
    • Shen, P.M.1    Su, Y.K.2    Lin, S.M.3    Kao, J.T.4    Liao, T.H.5
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0014064044 scopus 로고
    • A protein sequenator
    • Edman P Begg G (1967) A protein sequenator. Eur J Biochem 1, 80 91.
    • (1967) Eur J Biochem , vol.1 , pp. 80-91
    • Edman, P.1    Begg, G.2


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