메뉴 건너뛰기




Volumn 75, Issue 1, 2008, Pages 97-104

Changes in cathepsin gene expression and relative enzymatic activity during gilthead sea bream oogenesis

Author keywords

Egg; Lysosomal enzymes; Yolk

Indexed keywords

CATHEPSIN; CATHEPSIN B; CATHEPSIN D; CATHEPSIN L; ENZYME INHIBITOR; LIPOVITELLIN; LYSOSOME ENZYME; MESSENGER RNA; YOLK PROTEIN;

EID: 36849077753     PISSN: 1040452X     EISSN: 10982795     Source Type: Journal    
DOI: 10.1002/mrd.20768     Document Type: Article
Times cited : (32)

References (28)
  • 1
    • 15744398038 scopus 로고    scopus 로고
    • Baldwin WST, Roling JA, Peterson S, Chapman LM. 2005. Effects of nonylphenol on hepatic testosterone metabolism and the expression of acute phase proteins in winter f lounder (Pleuronectes americanus): Comparison to the effects of Saint John's Wort Com. Biochem Physiol 140:87-96.
    • Baldwin WST, Roling JA, Peterson S, Chapman LM. 2005. Effects of nonylphenol on hepatic testosterone metabolism and the expression of acute phase proteins in winter f lounder (Pleuronectes americanus): Comparison to the effects of Saint John's Wort Com. Biochem Physiol 140:87-96.
  • 3
    • 0030814882 scopus 로고    scopus 로고
    • Molecular characterisation of ovarian cathepsin D in the rainbow trout, Oncorhynchus mykiss
    • Brooks S, Tyler CR, Carnevali O, Coward K, Sumpter JP. 1997. Molecular characterisation of ovarian cathepsin D in the rainbow trout, Oncorhynchus mykiss. Gene 201:45-54.
    • (1997) Gene , vol.201 , pp. 45-54
    • Brooks, S.1    Tyler, C.R.2    Carnevali, O.3    Coward, K.4    Sumpter, J.P.5
  • 4
    • 0037403521 scopus 로고    scopus 로고
    • Exposure to xenobiotic compounds: Looking for new biomarkers
    • Carnevali O, Maradonna F. 2003. Exposure to xenobiotic compounds: Looking for new biomarkers. Gen Comp Endocrinol 131:203-209.
    • (2003) Gen Comp Endocrinol , vol.131 , pp. 203-209
    • Carnevali, O.1    Maradonna, F.2
  • 5
    • 0032918875 scopus 로고    scopus 로고
    • Yolk formation and degradation during oocyte maturation in seabream Sparus aurata: Involvement of two lysosomal proteinases
    • Carnevali O, Carletta R, Cambi A, Vita A, Bromage N. 1999a. Yolk formation and degradation during oocyte maturation in seabream Sparus aurata: Involvement of two lysosomal proteinases. Biol Reprod 60:140-146.
    • (1999) Biol Reprod , vol.60 , pp. 140-146
    • Carnevali, O.1    Carletta, R.2    Cambi, A.3    Vita, A.4    Bromage, N.5
  • 6
    • 0032794641 scopus 로고    scopus 로고
    • Molecular cloning and expression of ovarian cathepsin D in seabream, Sparus aurata
    • Carnevali O, Centonze F, Brooks S, Marota I, Sumpter JP. 1999b. Molecular cloning and expression of ovarian cathepsin D in seabream, Sparus aurata. Biol Reprod 61:785-791.
    • (1999) Biol Reprod , vol.61 , pp. 785-791
    • Carnevali, O.1    Centonze, F.2    Brooks, S.3    Marota, I.4    Sumpter, J.P.5
  • 8
    • 0036514179 scopus 로고    scopus 로고
    • Cathepsin D produces antimicrobial peptide parasin I fromhistone H2A in the skin mucosa of fish
    • Cho JH, Park IY, Kim HS, Lee WT, Kim MS, Kim SC. 2002. Cathepsin D produces antimicrobial peptide parasin I fromhistone H2A in the skin mucosa of fish. FASEB J 16:429-431.
    • (2002) FASEB J , vol.16 , pp. 429-431
    • Cho, J.H.1    Park, I.Y.2    Kim, H.S.3    Lee, W.T.4    Kim, M.S.5    Kim, S.C.6
  • 9
    • 0032924303 scopus 로고    scopus 로고
    • Isolation, characterization and molecular cloning of cathepsin D from lizard ovary: Changes in enzyme activity and mRNA expression throughout ovarian cycle
    • De Stasio R, Borrelli L, Kille P, Parisi E, Filosa S. 1999. Isolation, characterization and molecular cloning of cathepsin D from lizard ovary: Changes in enzyme activity and mRNA expression throughout ovarian cycle. Mol Reprod Dev 52:126-134.
    • (1999) Mol Reprod Dev , vol.52 , pp. 126-134
    • De Stasio, R.1    Borrelli, L.2    Kille, P.3    Parisi, E.4    Filosa, S.5
  • 10
    • 0036321923 scopus 로고    scopus 로고
    • In vivo oocyte hydration in Atlantic halibut (Hippoglossus hippoglossus); proteolytic liberation of free amino acids, and ion transport, are driving forces for osmotic water influx
    • Finn RN, Ostby GC, Norberg B, Fyhn HJ. 2002. In vivo oocyte hydration in Atlantic halibut (Hippoglossus hippoglossus); proteolytic liberation of free amino acids, and ion transport, are driving forces for osmotic water influx. J Exp Biol 205:211-224.
    • (2002) J Exp Biol , vol.205 , pp. 211-224
    • Finn, R.N.1    Ostby, G.C.2    Norberg, B.3    Fyhn, H.J.4
  • 11
    • 0036545614 scopus 로고    scopus 로고
    • Complementary profiling of gene expression at the Transcriptome and proteome levels in Saccaromyces cerevisiae
    • Griffin TJ, Gygi SP, Ideker T, Rist B, Eng JHood, Aebersold LR. 2002. Complementary profiling of gene expression at the Transcriptome and proteome levels in Saccaromyces cerevisiae. Mol Cell Proteomics 1:323-333.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 323-333
    • Griffin, T.J.1    Gygi, S.P.2    Ideker, T.3    Rist, B.4    JHood, E.5    Aebersold, L.R.6
  • 12
    • 0036006819 scopus 로고    scopus 로고
    • Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids
    • Hiramatsu N, Ichikawa N, Fukada H, Fujita T, Sullivan CV, Hara A. 2002b. Identification and characterization of proteases involved in specific proteolysis of vitellogenin and yolk proteins in salmonids. J Exp Zool 292:11-25.
    • (2002) J Exp Zool , vol.292 , pp. 11-25
    • Hiramatsu, N.1    Ichikawa, N.2    Fukada, H.3    Fujita, T.4    Sullivan, C.V.5    Hara, A.6
  • 13
    • 0032079894 scopus 로고    scopus 로고
    • Molecular cloning, expression and characterization of an Ascaris inhibitor for pepsin and cathepsin E
    • Kageyama T. 1998. Molecular cloning, expression and characterization of an Ascaris inhibitor for pepsin and cathepsin E. Eur J Biochem 253:804-809.
    • (1998) Eur J Biochem , vol.253 , pp. 804-809
    • Kageyama, T.1
  • 14
    • 0027769327 scopus 로고
    • A selective colorimetric assay for cathepsin L using Z-Phe-Arg-4-methoxy-beta-naphthylamide
    • Kamboj RC, Pal S, Raghav N, Singh H. 1993. A selective colorimetric assay for cathepsin L using Z-Phe-Arg-4-methoxy-beta-naphthylamide. Biochimie 75:873-878.
    • (1993) Biochimie , vol.75 , pp. 873-878
    • Kamboj, R.C.1    Pal, S.2    Raghav, N.3    Singh, H.4
  • 15
    • 0035184222 scopus 로고    scopus 로고
    • Molecular characterization of putative yolk processing enzymes and their expression during oogenesis and embryogenesis in rainbow trout (Oncorhynchus mykiss)
    • Kwon JY, Prat F, Randall C, Tyler CR. 2001. Molecular characterization of putative yolk processing enzymes and their expression during oogenesis and embryogenesis in rainbow trout (Oncorhynchus mykiss). Biol Reprod 65:1701-1709.
    • (2001) Biol Reprod , vol.65 , pp. 1701-1709
    • Kwon, J.Y.1    Prat, F.2    Randall, C.3    Tyler, C.R.4
  • 16
    • 25144498370 scopus 로고    scopus 로고
    • Derivation of major yolk proteins from parental vitellogenins and alternative processing during oocyte maturation in Fundulus heteroclitus
    • LaFleur GJ, Jr., Raldua D, Fabra M, Carnevali O, Denslow N, Wallace RA, Cerda J. 2005. Derivation of major yolk proteins from parental vitellogenins and alternative processing during oocyte maturation in Fundulus heteroclitus. Biol Reprod 73:815-824.
    • (2005) Biol Reprod , vol.73 , pp. 815-824
    • LaFleur Jr., G.J.1    Raldua, D.2    Fabra, M.3    Carnevali, O.4    Denslow, N.5    Wallace, R.A.6    Cerda, J.7
  • 18
    • 0023661275 scopus 로고
    • Specific proteolysis regulates fusion between endocytic compartments in Xenopus oocytes
    • Opresko LK, Karpf RA. 1987. Specific proteolysis regulates fusion between endocytic compartments in Xenopus oocytes. Cell 51:557-568.
    • (1987) Cell , vol.51 , pp. 557-568
    • Opresko, L.K.1    Karpf, R.A.2
  • 19
    • 0038324087 scopus 로고    scopus 로고
    • Ovarian follicle growth, maturation, and ovulation in teleost fish
    • Patino R, Sullivan CV. 2002. Ovarian follicle growth, maturation, and ovulation in teleost fish. Fish Physiol Biochem 26:57-70.
    • (2002) Fish Physiol Biochem , vol.26 , pp. 57-70
    • Patino, R.1    Sullivan, C.V.2
  • 21
    • 0028095918 scopus 로고
    • Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout
    • Sire MF, Babin PJ, Vernier JM. 1994. Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout. J Exp Zool 269:69-83.
    • (1994) J Exp Zool , vol.269 , pp. 69-83
    • Sire, M.F.1    Babin, P.J.2    Vernier, J.M.3
  • 22
    • 0019757154 scopus 로고
    • Cathepsin D from porcine and bovine spleen
    • Takahashi T, Tang J. 1981. Cathepsin D from porcine and bovine spleen. Methods in Enzymology. Vol. 80, pp 565-581.
    • (1981) Methods in Enzymology , vol.80 , pp. 565-581
    • Takahashi, T.1    Tang, J.2
  • 23
    • 0346787805 scopus 로고    scopus 로고
    • Molecular characerization of cathepsin L from hepatopancreas of carp Cyprinus carpio
    • Tsunemoto K, Osatomi K, Nozaki Y, Hara K, Ishihara T. 2004. Molecular characerization of cathepsin L from hepatopancreas of carp Cyprinus carpio. Comp Biochem Physiol 137:107-114.
    • (2004) Comp Biochem Physiol , vol.137 , pp. 107-114
    • Tsunemoto, K.1    Osatomi, K.2    Nozaki, Y.3    Hara, K.4    Ishihara, T.5
  • 24
    • 0022244976 scopus 로고
    • Phosvitins in Fundulus oocytes and eggs. Preliminary chromatographic and electrophoretic analyses together with biological consideration
    • Wallace R, Begovac PC. 1985. Phosvitins in Fundulus oocytes and eggs. Preliminary chromatographic and electrophoretic analyses together with biological consideration. J Biol Chem 15:11268-11274.
    • (1985) J Biol Chem , vol.15 , pp. 11268-11274
    • Wallace, R.1    Begovac, P.C.2
  • 25
    • 0022416087 scopus 로고
    • Major protein changes during vitellogenesis and maturation of Fundulus oocytes
    • Wallace R, Selman K. 1985. Major protein changes during vitellogenesis and maturation of Fundulus oocytes. Dev Biol 110:492-498.
    • (1985) Dev Biol , vol.110 , pp. 492-498
    • Wallace, R.1    Selman, K.2
  • 27
    • 0029061297 scopus 로고
    • Precursor-product relationship between chicken vitellogenin and the yolk proteins: The 40 kDa yolk plasma glycoprotein is derived from the C-terminal cysteine rich domain of vitellogenin II
    • Yamamura J, Adachi T, Aoki N, Nakajima H, Nakamura R, Matsuda T. 1995. Precursor-product relationship between chicken vitellogenin and the yolk proteins: The 40 kDa yolk plasma glycoprotein is derived from the C-terminal cysteine rich domain of vitellogenin II. Bioch Biophys Acta 1244:384-394.
    • (1995) Bioch Biophys Acta , vol.1244 , pp. 384-394
    • Yamamura, J.1    Adachi, T.2    Aoki, N.3    Nakajima, H.4    Nakamura, R.5    Matsuda, T.6
  • 28
    • 0028023542 scopus 로고
    • Cathepsin D activity in the vitellogenesis of Xenopus laevis
    • Yoshizaki N, Yonezawa S. 1994. Cathepsin D activity in the vitellogenesis of Xenopus laevis. Dev Growth Differ 36:299-306.
    • (1994) Dev Growth Differ , vol.36 , pp. 299-306
    • Yoshizaki, N.1    Yonezawa, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.