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Volumn 169, Issue 1, 2014, Pages 25-30

Biochemical characterization of cathepsin D from the mussel Lamellidens corrianus

Author keywords

Cathepsin D; Invertebrate; Lamellidens corrianus; Mannose 6 phosphate receptor; Zymogram

Indexed keywords

ANTISERUM; CATHEPSIN D; FRESH WATER; GLYCOPEPTIDASE; GLYCOPROTEIN; HEMOGLOBIN; LYSOSOME ENZYME; MANNOSE 6 PHOSPHATE RECEPTOR 300; MANNOSE 6 PHOSPHATE RECEPTOR 46; PEPSTATIN; SOMATOMEDIN B RECEPTOR; UNCLASSIFIED DRUG;

EID: 84891349808     PISSN: 10964959     EISSN: 18791107     Source Type: Journal    
DOI: 10.1016/j.cbpb.2013.12.003     Document Type: Article
Times cited : (11)

References (45)
  • 1
    • 78049242138 scopus 로고    scopus 로고
    • Cathepsin D from the hepatopancreas of the cuttlefish (Sepia officinalis): purification and characterization
    • Balti R., Hmidet N., Jellouli K., Nedjar-Arroume N., Guillochon D., Nasri M. Cathepsin D from the hepatopancreas of the cuttlefish (Sepia officinalis): purification and characterization. J. Agric. Food Chem. 2010, 58:10623-10630.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 10623-10630
    • Balti, R.1    Hmidet, N.2    Jellouli, K.3    Nedjar-Arroume, N.4    Guillochon, D.5    Nasri, M.6
  • 2
    • 0014774690 scopus 로고
    • Cathepsin D. Purification of isoenzymes from human and chicken liver
    • Barrett A.J. Cathepsin D. Purification of isoenzymes from human and chicken liver. Biochem. J. 1970, 117:601-607.
    • (1970) Biochem. J. , vol.117 , pp. 601-607
    • Barrett, A.J.1
  • 3
    • 0021346370 scopus 로고
    • Cathepsin D from pig myometrium. Characterization of the proteinase
    • Barth R., Afting E.G. Cathepsin D from pig myometrium. Characterization of the proteinase. Biochem. J. 1984, 219:899-904.
    • (1984) Biochem. J. , vol.219 , pp. 899-904
    • Barth, R.1    Afting, E.G.2
  • 5
    • 0030044878 scopus 로고    scopus 로고
    • Purification and characterization of a digestive cathepsin D proteinase isolated from Tribolium castaneum larvae (Herbst)
    • Blanco-Labra A., Martinez-Gallardo N.A., Sandoval-Cardoso L., Delano-Frier J. Purification and characterization of a digestive cathepsin D proteinase isolated from Tribolium castaneum larvae (Herbst). Insect Biochem. Mol. Biol. 1996, 26:95-100.
    • (1996) Insect Biochem. Mol. Biol. , vol.26 , pp. 95-100
    • Blanco-Labra, A.1    Martinez-Gallardo, N.A.2    Sandoval-Cardoso, L.3    Delano-Frier, J.4
  • 6
    • 0031872245 scopus 로고    scopus 로고
    • Purification and partial characterization of cathepsin D from porcine (Sus scrofa) liver using affinity chromatography
    • Canduri F., Ward R.J., de Azevedo Junior W.F., Gomes R.A., Arni R.K. Purification and partial characterization of cathepsin D from porcine (Sus scrofa) liver using affinity chromatography. Biochem. Mol. Biol. Int. 1998, 45:797-803.
    • (1998) Biochem. Mol. Biol. Int. , vol.45 , pp. 797-803
    • Canduri, F.1    Ward, R.J.2    de Azevedo Junior, W.F.3    Gomes, R.A.4    Arni, R.K.5
  • 7
    • 0032963373 scopus 로고    scopus 로고
    • Cathepsin D from the liver of the Antarctic icefish Chionodraco hamatus exhibits unusual activity and stability at high temperatures1
    • Capasso C., Lees W.E., Capasso A., Scudiero R., Carginale V., Kille P., Kay J., Parisi E. Cathepsin D from the liver of the Antarctic icefish Chionodraco hamatus exhibits unusual activity and stability at high temperatures1. Biochim. Biophys. Acta 1999, 1431:64-73.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 64-73
    • Capasso, C.1    Lees, W.E.2    Capasso, A.3    Scudiero, R.4    Carginale, V.5    Kille, P.6    Kay, J.7    Parisi, E.8
  • 8
    • 0000547403 scopus 로고
    • Purification and characterization of a lysosomal aspartic protease with cathepsin D activity from the mosquito
    • Cho W.L., Dhadialla T.S., Raikhel A.S. Purification and characterization of a lysosomal aspartic protease with cathepsin D activity from the mosquito. Insect Biochem. 1991, 21:165-176.
    • (1991) Insect Biochem. , vol.21 , pp. 165-176
    • Cho, W.L.1    Dhadialla, T.S.2    Raikhel, A.S.3
  • 9
    • 0025290527 scopus 로고
    • The structure and function of the aspartic proteinases
    • Davies D.R. The structure and function of the aspartic proteinases. Annu. Rev. Biophys. Biophys. Chem. 1990, 19:189-215.
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 10
    • 0027124132 scopus 로고
    • Purification and crystallization of human cathepsin D
    • Fusek M., Baudys M., Metcalf P. Purification and crystallization of human cathepsin D. J. Mol. Biol. 1992, 226:555-557.
    • (1992) J. Mol. Biol. , vol.226 , pp. 555-557
    • Fusek, M.1    Baudys, M.2    Metcalf, P.3
  • 11
    • 84985399999 scopus 로고
    • Purification and characterization of cathepsin D from the digestive gland of the pelagic squid Todarodes sagittatus
    • Gildberg A. Purification and characterization of cathepsin D from the digestive gland of the pelagic squid Todarodes sagittatus. J. Sci. Food Agric. 1987, 39:85-94.
    • (1987) J. Sci. Food Agric. , vol.39 , pp. 85-94
    • Gildberg, A.1
  • 12
  • 15
    • 0018903866 scopus 로고
    • Biosynthesis of lysosomal enzymes in fibroblasts. Synthesis as precursors of higher molecular weight
    • Hasilik A., Neufeld E.F. Biosynthesis of lysosomal enzymes in fibroblasts. Synthesis as precursors of higher molecular weight. J. Biol. Chem. 1980, 255:4937-4945.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4937-4945
    • Hasilik, A.1    Neufeld, E.F.2
  • 17
    • 64549088906 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression analysis of cathepsin D gene from turbot Scophthalmus maximus
    • Jia A., Zhang X.H. Molecular cloning, characterization and expression analysis of cathepsin D gene from turbot Scophthalmus maximus. Fish Shellfish Immunol. 2009, 26:606-613.
    • (2009) Fish Shellfish Immunol. , vol.26 , pp. 606-613
    • Jia, A.1    Zhang, X.H.2
  • 18
    • 0038517747 scopus 로고
    • Comparative study on the cathepsin D from banded shrimp (Penaeus japonicus) and grass shrimp (Penaeus monodon)
    • Jiang S.T., Nei F.P., Chen H.C. Comparative study on the cathepsin D from banded shrimp (Penaeus japonicus) and grass shrimp (Penaeus monodon). J. Agric. Food Chem. 1992, 40:961-966.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 961-966
    • Jiang, S.T.1    Nei, F.P.2    Chen, H.C.3
  • 20
    • 0025365591 scopus 로고
    • Lysosomal enzyme targeting
    • Kornfeld S. Lysosomal enzyme targeting. Biochem. Soc. Trans. 1990, 18:367-374.
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 367-374
    • Kornfeld, S.1
  • 21
    • 78649949400 scopus 로고    scopus 로고
    • Purification and partial characterization of ostrich skeletal muscle cathepsin D and its activity during meat maturation
    • Krause J., Tshidino S.C., Ogawa T., Watanabe Y., Oosthuizen V., Somai B., Muramoto K., Naude R.J. Purification and partial characterization of ostrich skeletal muscle cathepsin D and its activity during meat maturation. Meat Sci. 2011, 87:196-201.
    • (2011) Meat Sci. , vol.87 , pp. 196-201
    • Krause, J.1    Tshidino, S.C.2    Ogawa, T.3    Watanabe, Y.4    Oosthuizen, V.5    Somai, B.6    Muramoto, K.7    Naude, R.J.8
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 84856209649 scopus 로고    scopus 로고
    • Isolation, affinity purification and biochemical characterization of a lysosomal cathepsin D from the deuterostome Asterias rubens
    • Merino V., Siva Kumar N. Isolation, affinity purification and biochemical characterization of a lysosomal cathepsin D from the deuterostome Asterias rubens. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2012, 161:240-246.
    • (2012) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.161 , pp. 240-246
    • Merino, V.1    Siva Kumar, N.2
  • 26
    • 8444249345 scopus 로고    scopus 로고
    • Salmon spawning migration and muscle protein metabolism: the August Krogh principle at work
    • Mommsen T.P. Salmon spawning migration and muscle protein metabolism: the August Krogh principle at work. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2004, 139:383-400.
    • (2004) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.139 , pp. 383-400
    • Mommsen, T.P.1
  • 27
    • 77950138173 scopus 로고    scopus 로고
    • Evolution of mannose 6-phosphate receptors (MPR300 and 46): lysosomal enzyme sorting proteins
    • Nadimpalli S.K., Amancha P.K. Evolution of mannose 6-phosphate receptors (MPR300 and 46): lysosomal enzyme sorting proteins. Curr. Protein Pept. Sci. 2010, 11:68-90.
    • (2010) Curr. Protein Pept. Sci. , vol.11 , pp. 68-90
    • Nadimpalli, S.K.1    Amancha, P.K.2
  • 28
    • 4444241847 scopus 로고    scopus 로고
    • Biochemical and immunological characterization of a glycosylated alpha-fucosidase from the invertebrate Unio: interaction of the enzyme with its in vivo binding partners
    • Nadimpalli S.K., Padmanabhan N., Koduru S. Biochemical and immunological characterization of a glycosylated alpha-fucosidase from the invertebrate Unio: interaction of the enzyme with its in vivo binding partners. Protein Expr. Purif. 2004, 37:279-287.
    • (2004) Protein Expr. Purif. , vol.37 , pp. 279-287
    • Nadimpalli, S.K.1    Padmanabhan, N.2    Koduru, S.3
  • 29
    • 0029936001 scopus 로고    scopus 로고
    • Vitellogenesis-related ovary cathepsin D from Xenopus laevis: purification and properties in comparison with liver cathepsin D
    • Nakamura K., Yonezawa S., Yoshizaki N. Vitellogenesis-related ovary cathepsin D from Xenopus laevis: purification and properties in comparison with liver cathepsin D. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 1996, 113:835-840.
    • (1996) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.113 , pp. 835-840
    • Nakamura, K.1    Yonezawa, S.2    Yoshizaki, N.3
  • 30
    • 0035132092 scopus 로고    scopus 로고
    • Purification and characterization of cathepsin D from herring muscle (Clupea harengus)
    • Nielsen L.B., Nielsen H.H. Purification and characterization of cathepsin D from herring muscle (Clupea harengus). Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2001, 128:351-363.
    • (2001) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.128 , pp. 351-363
    • Nielsen, L.B.1    Nielsen, H.H.2
  • 31
    • 0023905240 scopus 로고
    • Identification of latent procathepsin B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro
    • Nishimura Y., Kawabata T., Kato K. Identification of latent procathepsin B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro. Arch. Biochem. Biophys. 1988, 261:64-71.
    • (1988) Arch. Biochem. Biophys. , vol.261 , pp. 64-71
    • Nishimura, Y.1    Kawabata, T.2    Kato, K.3
  • 32
    • 70449642350 scopus 로고    scopus 로고
    • Sequence and function of lysosomal and digestive cathepsin D-like proteinases of Musca domestica midgut
    • Padilha M.H., Pimentel A.C., Ribeiro A.F., Terra W.R. Sequence and function of lysosomal and digestive cathepsin D-like proteinases of Musca domestica midgut. Insect Biochem. Mol. Biol. 2009, 39:782-791.
    • (2009) Insect Biochem. Mol. Biol. , vol.39 , pp. 782-791
    • Padilha, M.H.1    Pimentel, A.C.2    Ribeiro, A.F.3    Terra, W.R.4
  • 33
  • 34
    • 0028115873 scopus 로고
    • Western blotting and enzymatic activity analysis of cathepsin D in breast tissue and sera of patients with breast cancer and benign breast disease and of normal controls
    • Schultz D.C., Bazel S., Wright L.M., Tucker S., Lange M.K., Tachovsky T., Longo S., Niedbala S., Alhadeff J.A. Western blotting and enzymatic activity analysis of cathepsin D in breast tissue and sera of patients with breast cancer and benign breast disease and of normal controls. Cancer Res. 1994, 54:48-54.
    • (1994) Cancer Res. , vol.54 , pp. 48-54
    • Schultz, D.C.1    Bazel, S.2    Wright, L.M.3    Tucker, S.4    Lange, M.K.5    Tachovsky, T.6    Longo, S.7    Niedbala, S.8    Alhadeff, J.A.9
  • 37
    • 84876354518 scopus 로고    scopus 로고
    • Isolation, purification, and biochemical characterization of two forms of lysosomal beta-N-acetylhexosaminidase from the invertebrate Unio
    • Venugopal A., Sivakumar N. Isolation, purification, and biochemical characterization of two forms of lysosomal beta-N-acetylhexosaminidase from the invertebrate Unio. Biosci. Biotechnol. Biochem. 2013, 77:497-504.
    • (2013) Biosci. Biotechnol. Biochem. , vol.77 , pp. 497-504
    • Venugopal, A.1    Sivakumar, N.2
  • 38
    • 84859433487 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a lysosomal alpha-fucosidase from the deuterostomia Asterias rubens
    • Visa M., Hammer E., Volker U., Koliwer-Brandl H., Kelm S., Nadimpalli S.K. Purification and biochemical characterization of a lysosomal alpha-fucosidase from the deuterostomia Asterias rubens. Biochimie 2012, 94:1199-1205.
    • (2012) Biochimie , vol.94 , pp. 1199-1205
    • Visa, M.1    Hammer, E.2    Volker, U.3    Koliwer-Brandl, H.4    Kelm, S.5    Nadimpalli, S.K.6
  • 39
    • 34249054477 scopus 로고    scopus 로고
    • Cathepsin D from Atlantic cod (Gadus morhua L) liver. Isolation and comparative studies
    • Wang P.A., Stenvik J., Larsen R., Maehre H., Olsen R.L. Cathepsin D from Atlantic cod (Gadus morhua L) liver. Isolation and comparative studies. Comp. Biochem. Physiol. B 2007, 147:504-511.
    • (2007) Comp. Biochem. Physiol. B , vol.147 , pp. 504-511
    • Wang, P.A.1    Stenvik, J.2    Larsen, R.3    Maehre, H.4    Olsen, R.L.5
  • 41
    • 53249132917 scopus 로고    scopus 로고
    • Purification and characterization of cathepsin D from normal human breast tissue
    • Wright L.M., Levy E.S., Patel N.P., Alhadeff J.A. Purification and characterization of cathepsin D from normal human breast tissue. J. Protein Chem. 1997, 16:171-181.
    • (1997) J. Protein Chem. , vol.16 , pp. 171-181
    • Wright, L.M.1    Levy, E.S.2    Patel, N.P.3    Alhadeff, J.A.4
  • 42
    • 56949094433 scopus 로고    scopus 로고
    • Mannose-6-phosphate receptors (MPR 300 and 46) from the highly evolved invertebrate Asterias rubens (Echinodermate): biochemical and functional characterization of MPR 46 protein
    • Yadavalli S., Nadimpalli S.K. Mannose-6-phosphate receptors (MPR 300 and 46) from the highly evolved invertebrate Asterias rubens (Echinodermate): biochemical and functional characterization of MPR 46 protein. Glycoconj. J. 2008, 25:889-901.
    • (2008) Glycoconj. J. , vol.25 , pp. 889-901
    • Yadavalli, S.1    Nadimpalli, S.K.2
  • 43
    • 77949264934 scopus 로고    scopus 로고
    • Role of cation independent mannose 6-phosphate receptor protein in sorting and intracellular trafficking of lysosomal enzymes in chicken embryonic fibroblast (CEF) cells
    • Yadavalli S., Nadimpalli S.K. Role of cation independent mannose 6-phosphate receptor protein in sorting and intracellular trafficking of lysosomal enzymes in chicken embryonic fibroblast (CEF) cells. Glycoconj. J. 2010, 27:39-48.
    • (2010) Glycoconj. J. , vol.27 , pp. 39-48
    • Yadavalli, S.1    Nadimpalli, S.K.2


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