메뉴 건너뛰기




Volumn 69, Issue 2, 2004, Pages 205-214

Thyroglobulin type-1 domain protease inhibitors exhibit specific expression in the cortical ooplasm of vitellogenic rainbow trout oocytes

Author keywords

Fish; Follicle; Oocyte; Protease inhibitors; Vitellogenesis

Indexed keywords

AMINO ACID; MESSENGER RNA; OOCYTE PROTEASE INHIBITOR 1; OOCYTE PROTEASE INHIBITOR 2; PROTEINASE INHIBITOR; THYROGLOBULIN; UNCLASSIFIED DRUG; VITELLOGENIN;

EID: 4444294560     PISSN: 1040452X     EISSN: None     Source Type: Journal    
DOI: 10.1002/mrd.20118     Document Type: Article
Times cited : (7)

References (38)
  • 1
    • 0034792230 scopus 로고    scopus 로고
    • Cysteine protease inhibitor is specifically expressed in pre- and early-vitellogenic oocytes from the brook trout periovulatory ovary
    • Bobe J, Goetz FW. 2001. Cysteine protease inhibitor is specifically expressed in pre- and early-vitellogenic oocytes from the brook trout periovulatory ovary. Mol Reprod Dev 60:312-318.
    • (2001) Mol Reprod Dev , vol.60 , pp. 312-318
    • Bobe, J.1    Goetz, F.W.2
  • 2
    • 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
  • 3
    • 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
  • 4
    • 0031854445 scopus 로고    scopus 로고
    • Trout ovulatory proteins are partially responsible for the anti-proteolytic activity found in trout coelomic fluid
    • Coffman MA, Goetz FW. 1998. Trout ovulatory proteins are partially responsible for the anti-proteolytic activity found in trout coelomic fluid. Biol Reprod 59:497-502.
    • (1998) Biol Reprod , vol.59 , pp. 497-502
    • Coffman, M.A.1    Goetz, F.W.2
  • 5
    • 0036893454 scopus 로고    scopus 로고
    • Cellular localization of tissue inhibitors of metalloproteinases in the rat ovary throughout pseudopregnancy
    • Curry TEJ, Wheeler SE. 2002. Cellular localization of tissue inhibitors of metalloproteinases in the rat ovary throughout pseudopregnancy. Biol Reprod 67:1943-1951.
    • (2002) Biol Reprod , vol.67 , pp. 1943-1951
    • Curry, T.E.J.1    Wheeler, S.E.2
  • 6
    • 0035941480 scopus 로고    scopus 로고
    • A survey of genes in the Atlantic salmon (Salmo salar) as identified by expressed sequence tags
    • Davey GC, Caplice NC, Martin SA, Powell R. 2001. A survey of genes in the Atlantic salmon (Salmo salar) as identified by expressed sequence tags. Gene 263:121-130.
    • (2001) Gene , vol.263 , pp. 121-130
    • Davey, G.C.1    Caplice, N.C.2    Martin, S.A.3    Powell, R.4
  • 7
    • 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
  • 8
    • 0025527484 scopus 로고
    • Yolk degradation in tick eggs: I. Occurrence of a cathepsin L-like acid proteinase in yolk spheres
    • Fagotto F. 1990. Yolk degradation in tick eggs: I. Occurrence of a cathepsin L-like acid proteinase in yolk spheres. Arch Insect Biochem Physiol 14:217-235.
    • (1990) Arch Insect Biochem Physiol , vol.14 , pp. 217-235
    • Fagotto, F.1
  • 9
    • 0030998472 scopus 로고    scopus 로고
    • Heparin-binding, highly basic regions within the thyroglobulin type-1 repeat of insulin-like growth factor (IGF)-binding proteins (IGFBPs)-3, -5, and -6 inhibit IGFBP-4 degradation
    • Fowlkes JL, Thrailkill KM, George-Nascimento C, Rosenberg CK, Serra DM. 1997. Heparin-binding, highly basic regions within the thyroglobulin type-1 repeat of insulin-like growth factor (IGF)-binding proteins (IGFBPs)-3, -5, and -6 inhibit IGFBP-4 degradation. Endocrinology 138:2280-2285.
    • (1997) Endocrinology , vol.138 , pp. 2280-2285
    • Fowlkes, J.L.1    Thrailkill, K.M.2    George-Nascimento, C.3    Rosenberg, C.K.4    Serra, D.M.5
  • 11
    • 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, Kara A. 2002. 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    Kara, A.6
  • 12
    • 0041350302 scopus 로고    scopus 로고
    • Vitellogenin transport and yolk formation in the quail ovary
    • Ito Y, Kihara M, Nakamura E, Yonezawa S, Yoshizaki N. 2003. Vitellogenin transport and yolk formation in the quail ovary. Zool Sci 20:717-726.
    • (2003) Zool Sci , vol.20 , pp. 717-726
    • Ito, Y.1    Kihara, M.2    Nakamura, E.3    Yonezawa, S.4    Yoshizaki, N.5
  • 13
    • 0001808598 scopus 로고    scopus 로고
    • Cathepsin L in eggs and larvae of perch, Perca fluviatilis: Variations with developmental stage and spawning period
    • Kestemont P, Cooremans J, Abi-Ayad A, Mélard C. 1999. Cathepsin L in eggs and larvae of perch, Perca fluviatilis: Variations with developmental stage and spawning period. Fish Physiol Biochem 21:59-64.
    • (1999) Fish Physiol Biochem , vol.21 , pp. 59-64
    • Kestemont, P.1    Cooremans, J.2    Abi-Ayad, A.3    Mélard, C.4
  • 14
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • Kozak M. 1986. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44:283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 15
    • 0037786036 scopus 로고    scopus 로고
    • Yolk mobilization in perch, Perca fluviatilis L., embryos
    • Krieger J, Fleig R. 1999. Yolk mobilization in perch, Perca fluviatilis L., embryos. Fish Physiol Biochem 21:157-165.
    • (1999) Fish Physiol Biochem , vol.21 , pp. 157-165
    • Krieger, J.1    Fleig, R.2
  • 16
    • 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
  • 17
    • 0040736139 scopus 로고    scopus 로고
    • Thyroglobulin type-1 domains in equistatin inhibit both papain-like cysteine proteinases and cathepsin D
    • Lenarcic B, Turk V. 1999. Thyroglobulin type-1 domains in equistatin inhibit both papain-like cysteine proteinases and cathepsin D. J Biol Chem 274:563-566.
    • (1999) J Biol Chem , vol.274 , pp. 563-566
    • Lenarcic, B.1    Turk, V.2
  • 18
    • 0040020321 scopus 로고    scopus 로고
    • Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain
    • Lenarcic B, Ritonja A, Strukelj B, Turk B, Turk V. 1997. Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain. J Biol Chem 272:13899-13903.
    • (1997) J Biol Chem , vol.272 , pp. 13899-13903
    • Lenarcic, B.1    Ritonja, A.2    Strukelj, B.3    Turk, B.4    Turk, V.5
  • 22
    • 0029797002 scopus 로고    scopus 로고
    • Characterization of the type-1 repeat from thyroglobulin, a cysteine-rich module found in proteins from different families
    • Molina F, Bouanani M, Pau B, Granier C. 1996. Characterization of the type-1 repeat from thyroglobulin, a cysteine-rich module found in proteins from different families. Eur J Biochem 240:125-133.
    • (1996) Eur J Biochem , vol.240 , pp. 125-133
    • Molina, F.1    Bouanani, M.2    Pau, B.3    Granier, C.4
  • 23
    • 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. 1996. Vitellogenesis-related ovary cathepsin D from Xenopus laevis: Purification and properties in comparison with liver cathepsin D. Comp Biochem Physiol B Biochem Mol Biol 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
  • 24
    • 0035132399 scopus 로고    scopus 로고
    • Procathepsin and acid phosphatase are stored in Musca domestica yolk spheres
    • Ribolla PEM, Bijovsky AT, de Bianchi AG. 2001. Procathepsin and acid phosphatase are stored in Musca domestica yolk spheres. J Insect Physiol 47:225-232.
    • (2001) J Insect Physiol , vol.47 , pp. 225-232
    • Ribolla, P.E.M.1    Bijovsky, A.T.2    De Bianchi, A.G.3
  • 25
    • 0018195291 scopus 로고
    • Follicular atresia in the ovaries of nonmammalian vertebrates
    • Saidapur SK. 1978. Follicular atresia in the ovaries of nonmammalian vertebrates. Int Rev Cytol 54:225-244.
    • (1978) Int Rev Cytol , vol.54 , pp. 225-244
    • Saidapur, S.K.1
  • 26
    • 0028095918 scopus 로고
    • Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout
    • Sire M-F, Babin PJ, Vernier J-M. 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
  • 27
    • 0018652618 scopus 로고
    • Vitellogenesis: A versatile model for hormonal regulation of gene expression
    • Tata JR, Smith DF. 1979. Vitellogenesis: A versatile model for hormonal regulation of gene expression. Rec Prog Horm Res 35:47-95.
    • (1979) Rec Prog Horm Res , vol.35 , pp. 47-95
    • Tata, J.R.1    Smith, D.F.2
  • 28
    • 0344484133 scopus 로고    scopus 로고
    • Oocyte growth and development in teleosts
    • Tyler CR, Sumpter JP. 1996. Oocyte growth and development in teleosts. Rev Fish Biol Fish 6:287-318.
    • (1996) Rev Fish Biol Fish , vol.6 , pp. 287-318
    • Tyler, C.R.1    Sumpter, J.P.2
  • 29
    • 0025002923 scopus 로고
    • An in vitro culture system for studying vitellogenin uptake into ovarian follicles of the rainbow trout, Salmo gairdneri
    • Tyler CR, Sumpter JP, Bromage NR. 1990. An in vitro culture system for studying vitellogenin uptake into ovarian follicles of the rainbow trout, Salmo gairdneri. J Exp Zool 255:216-231.
    • (1990) J Exp Zool , vol.255 , pp. 216-231
    • Tyler, C.R.1    Sumpter, J.P.2    Bromage, N.R.3
  • 30
    • 0026014169 scopus 로고
    • Involvement of gonadotropin in the uptake of vitellogenin into vitellogenic oocytes of the rainbow trout, Oncorhynchus mykiss
    • Tyler CR, Sumpter JP, Kawauchi H, Swanson P. 1991. Involvement of gonadotropin in the uptake of vitellogenin into vitellogenic oocytes of the rainbow trout, Oncorhynchus mykiss. Gen Comp Endocrinol 84:291-299.
    • (1991) Gen Comp Endocrinol , vol.84 , pp. 291-299
    • Tyler, C.R.1    Sumpter, J.P.2    Kawauchi, H.3    Swanson, P.4
  • 31
    • 0027367699 scopus 로고
    • Vitellogenesis in insects and other groups - A review
    • Valle D. 1993. Vitellogenesis in insects and other groups-A review. Mem Inst Oswaldo Cruz 88:1-26.
    • (1993) Mem Inst Oswaldo Cruz , vol.88 , pp. 1-26
    • Valle, D.1
  • 32
    • 0023109345 scopus 로고
    • Multivesicular bodies play a key role in vitellogenin endocytosis by Xenopus oocytes
    • Wall DA, Patel S. 1987. Multivesicular bodies play a key role in vitellogenin endocytosis by Xenopus oocytes. Dev Biol 119:275-289.
    • (1987) Dev Biol , vol.119 , pp. 275-289
    • Wall, D.A.1    Patel, S.2
  • 33
    • 0022416087 scopus 로고
    • Major protein changes during vitellogenesis and maturation of Fundulus oocytes
    • Wallace RA, 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.A.1    Selman, K.2
  • 34
    • 0037965468 scopus 로고    scopus 로고
    • Yolk proteolysis in rainbow trout oocytes after serum-free culture: Evidence for a novel biochemical mechanism of atresia in oviparous vertebrates
    • Wood AW, Van Der Kraak G. 2003. Yolk proteolysis in rainbow trout oocytes after serum-free culture: Evidence for a novel biochemical mechanism of atresia in oviparous vertebrates. Mol Reprod Dev 65:219-227.
    • (2003) Mol Reprod Dev , vol.65 , pp. 219-227
    • Wood, A.W.1    Van Der Kraak, G.2
  • 35
    • 0028069204 scopus 로고
    • Cysteine proteinase from the eggs of the silkmoth, Bombyx mori: Site of synthesis and a suggested role in yolk protein degradation
    • Yamamoto Y, Zhao X, Suzuki AC, Takahashi SY. 1994. Cysteine proteinase from the eggs of the silkmoth, Bombyx mori: Site of synthesis and a suggested role in yolk protein degradation. J Insect Physiol 40:447-454.
    • (1994) J Insect Physiol , vol.40 , pp. 447-454
    • Yamamoto, Y.1    Zhao, X.2    Suzuki, A.C.3    Takahashi, S.Y.4
  • 36
    • 0025787834 scopus 로고
    • Cysteine protease inhibitor in egg of chum salmon
    • Yamashita M, Konagaya S. 1991. Cysteine protease inhibitor in egg of chum salmon. J Biochem (Tokyo) 110:762-766.
    • (1991) J Biochem (Tokyo) , vol.110 , pp. 762-766
    • Yamashita, M.1    Konagaya, S.2
  • 37
    • 0030067774 scopus 로고    scopus 로고
    • A novel cysteine protease inhibitor of the egg of chum salmon, containing a cysteine-rich thyroglobulin-like motif
    • Yamashita M, Konagaya S. 1996. A novel cysteine protease inhibitor of the egg of chum salmon, containing a cysteine-rich thyroglobulin-like motif. J Biol Chem 271:1282-1284.
    • (1996) J Biol Chem , vol.271 , pp. 1282-1284
    • Yamashita, M.1    Konagaya, S.2
  • 38
    • 0029992556 scopus 로고    scopus 로고
    • Salt concentration-dependency of vitellogenin processing by cathepsin D in Xenopus laevis
    • Yoshizaki N, Yonezawa S. 1996. Salt concentration-dependency of vitellogenin processing by cathepsin D in Xenopus laevis. Dev Growth Diff 38:549-556.
    • (1996) Dev Growth Diff , vol.38 , pp. 549-556
    • Yoshizaki, N.1    Yonezawa, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.