메뉴 건너뛰기




Volumn 40, Issue 6, 1998, Pages 659-667

Cysteine proteinase plays a key role for the initiation of yolk digestion during development of Xenopus laevis

Author keywords

Cathepsin D; Cysteine proteinase; Development; Xenopus; Yolk digestion

Indexed keywords

CYSTEINE PROTEINASE;

EID: 0031761930     PISSN: 00121592     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1440-169X.1998.t01-4-00010.x     Document Type: Article
Times cited : (27)

References (32)
  • 1
    • 7844237010 scopus 로고
    • Properties of lysosomal enzymes
    • (Eds J. T. Dingle & H. B. Fell), North-Holland Publishing, Amsterdam
    • Barrett, A. J. 1969. Properties of lysosomal enzymes. In Lysosomes in Biology and Pathology, Vol. 2 (Eds J. T. Dingle & H. B. Fell), pp. 245-312. North-Holland Publishing, Amsterdam.
    • (1969) Lysosomes in Biology and Pathology , vol.2 , pp. 245-312
    • Barrett, A.J.1
  • 2
    • 0001310293 scopus 로고
    • Cathepsin D and other carboxyl proteinases
    • (Ed. A. J. Barrett), North-Holland Publishing, Amsterdam
    • Barrett, A. J. 1977. Cathepsin D and other carboxyl proteinases. In Proteinases in Mammalian Cells and Tissues (Ed. A. J. Barrett), pp. 209-248. North-Holland Publishing, Amsterdam.
    • (1977) Proteinases in Mammalian Cells and Tissues , pp. 209-248
    • Barrett, A.J.1
  • 3
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • Barrett, A. J. & Kirschke, H. 1981. Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol. 80, 535-561.
    • (1981) Methods Enzymol. , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 4
    • 0015890981 scopus 로고
    • Staining of phospho-proteins on acrylamide gel electropherograms
    • Cutting, J. A. & Roth, T. F. 1973. Staining of phospho-proteins on acrylamide gel electropherograms. Anal. Biochem. 54, 386-394.
    • (1973) Anal. Biochem. , vol.54 , pp. 386-394
    • Cutting, J.A.1    Roth, T.F.2
  • 5
    • 0345815365 scopus 로고
    • The breakdown of isolated yolk granules by cations
    • Essner, E. S. 1954. The breakdown of isolated yolk granules by cations. Protoplasma 43, 79-89.
    • (1954) Protoplasma , vol.43 , pp. 79-89
    • Essner, E.S.1
  • 6
    • 0028587431 scopus 로고
    • Changes in yolk platelet pH during Xenopus laevis development correlate with yolk utilization
    • Fagotto, F. & Maxfield, F. R. 1994a. Changes in yolk platelet pH during Xenopus laevis development correlate with yolk utilization. J. Cell Sci. 107, 3325-3337.
    • (1994) J. Cell Sci. , vol.107 , pp. 3325-3337
    • Fagotto, F.1    Maxfield, F.R.2
  • 7
    • 0028284661 scopus 로고
    • Yolk platelets in Xenopus oocytes maintain an acidic internal pH which may be essential for sodium accumulation
    • Fagotto, F. & Maxfield, F. R. 1994b. Yolk platelets in Xenopus oocytes maintain an acidic internal pH which may be essential for sodium accumulation. J. Cell Biol. 125, 1047-1056.
    • (1994) J. Cell Biol. , vol.125 , pp. 1047-1056
    • Fagotto, F.1    Maxfield, F.R.2
  • 9
    • 0025059406 scopus 로고
    • Purification and characterization of a cysteine proteinase from silkworm eggs
    • Kageyama, T. & Takahashi, S. Y. 1990. Purification and characterization of a cysteine proteinase from silkworm eggs. Eur. J. Biochem. 193, 203-210.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 203-210
    • Kageyama, T.1    Takahashi, S.Y.2
  • 10
    • 0000749481 scopus 로고
    • Studies on amphibian yolk: 5 Electron microscopic observations on the utilization of yolk platelets during embryogenesis
    • Karasaki, S. 1963. Studies on amphibian yolk: 5 Electron microscopic observations on the utilization of yolk platelets during embryogenesis. J. Ultrastruct. Res. 9, 225-247.
    • (1963) J. Ultrastruct. Res. , vol.9 , pp. 225-247
    • Karasaki, S.1
  • 11
  • 13
    • 0345815364 scopus 로고
    • Required salt concentration for successful fertilization of Xenopus laevis
    • Moriya, M. 1976. Required salt concentration for successful fertilization of Xenopus laevis. J. Fac. Sci. Hokkaido University Ser. VI 20, 272-276.
    • (1976) J. Fac. Sci. Hokkaido University Ser. VI , vol.20 , pp. 272-276
    • Moriya, M.1
  • 14
    • 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 113, 835-840.
    • (1996) Comp. Biochem. Physiol. B , vol.113 , pp. 835-840
    • Nakamura, K.1    Yonezawa, S.2    Yoshizaki, N.3
  • 16
    • 0018182060 scopus 로고
    • Labilization of the superficial layer and reduction in size of yolk platelets during early development of Xenopus laevis
    • Robertson, N. 1978. Labilization of the superficial layer and reduction in size of yolk platelets during early development of Xenopus laevis. Cell Differ. 7, 185-192.
    • (1978) Cell Differ. , vol.7 , pp. 185-192
    • Robertson, N.1
  • 17
    • 0013809740 scopus 로고
    • The utilization of yolk platelets by tissues of Xenopus embryos studied by a safranin staining method
    • Selman, G. G. & Pawsey, G. I. 1965. The utilization of yolk platelets by tissues of Xenopus embryos studied by a safranin staining method. J. Embryol. Exp. Morphol. 14, 191-212.
    • (1965) J. Embryol. Exp. Morphol. , vol.14 , pp. 191-212
    • Selman, G.G.1    Pawsey, G.I.2
  • 18
    • 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, P. J. & 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
  • 19
    • 0015838709 scopus 로고
    • The distribution of sodium and potassium in amphibian embryos during early development
    • Slack, C., Warner, A. E. & Warren, R. L. 1973. The distribution of sodium and potassium in amphibian embryos during early development. J. Physiol. 232, 297-312.
    • (1973) J. Physiol. , vol.232 , pp. 297-312
    • Slack, C.1    Warner, A.E.2    Warren, R.L.3
  • 20
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • Smith, P. K., Krohn, R. I. & Hermanson, G. Y. 1975. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150, 76-85.
    • (1975) Anal. Biochem. , vol.150 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.Y.3
  • 21
    • 0027177631 scopus 로고
    • Cysteine proteinase from the eggs of the silkmoth. Bombyx mon: Identification of a latent enzyme and characterization of activation and proteolytic processing in vivo and in vitro
    • Takahashi, S. Y., Yamamoto, Y., Shinoya, Y. & Kageyama, Y. 1993. Cysteine proteinase from the eggs of the silkmoth. Bombyx mon: Identification of a latent enzyme and characterization of activation and proteolytic processing in vivo and in vitro. J. Biochem. 114, 267-272.
    • (1993) J. Biochem. , vol.114 , pp. 267-272
    • Takahashi, S.Y.1    Yamamoto, Y.2    Shinoya, Y.3    Kageyama, Y.4
  • 22
    • 0001573128 scopus 로고
    • Acid cysteine proteinase from the eggs of silkmoth, Bombyx mori: Tissue distribution, developmental changes and the sites of synthesis for the enzyme
    • Takahashi, S. Y., Zhao, X., Kageyama, T. & Yamamoto, Y. 1992. Acid cysteine proteinase from the eggs of silkmoth, Bombyx mori: Tissue distribution, developmental changes and the sites of synthesis for the enzyme. Insect Biochem. Mol. Biol. 22, 369-377.
    • (1992) Insect Biochem. Mol. Biol. , vol.22 , pp. 369-377
    • Takahashi, S.Y.1    Zhao, X.2    Kageyama, T.3    Yamamoto, Y.4
  • 23
    • 0022163146 scopus 로고
    • Vitellogenesis and oocyte growth in nonmammalian vertebrates
    • (Ed. W. L. Browder), pp. Plenum Press, New York
    • Wallace, R. A. 1985. Vitellogenesis and oocyte growth in nonmammalian vertebrates. In Developmental Biology: A Comprehensive Synthesis, Vol. 1 (Ed. W. L. Browder), pp. 127-166. Plenum Press, New York.
    • (1985) Developmental Biology: A Comprehensive Synthesis , vol.1 , pp. 127-166
    • Wallace, R.A.1
  • 24
    • 0019888345 scopus 로고
    • The structure of vitellogenin
    • Wiley, H. S. & Wallace, R. A. 1981. The structure of vitellogenin. J. Biol. Chem. 256, 8626-8634.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8626-8634
    • Wiley, H.S.1    Wallace, R.A.2
  • 25
    • 0023387984 scopus 로고
    • Cathepsin e from rat neutrophils: Its properties and possible relations to cathepsin D-like and cathepsin E-like acid proteinases
    • Yonezawa, S., Tanaka, T. & Miyauchi, T. 1987. Cathepsin E from rat neutrophils: Its properties and possible relations to cathepsin D-like and cathepsin E-like acid proteinases. Arch. Biochem. Biophys. 256, 499-508.
    • (1987) Arch. Biochem. Biophys. , vol.256 , pp. 499-508
    • Yonezawa, S.1    Tanaka, T.2    Miyauchi, T.3
  • 26
    • 0000465587 scopus 로고
    • Ultrastructure of the hatching gland cells in the South African clawed toad, Xenopus laevis
    • Yoshizaki, N. 1973. Ultrastructure of the hatching gland cells in the South African clawed toad, Xenopus laevis. J. Fac. Sci. Hokkaido University Ser. VI 18, 469-480.
    • (1973) J. Fac. Sci. Hokkaido University Ser. VI , vol.18 , pp. 469-480
    • Yoshizaki, N.1
  • 27
    • 1842420090 scopus 로고
    • Ultrastructural cytochemistry of hatching gland cells in Xenopus embryos in relation to the hatching process
    • Yoshizaki, N. 1974. Ultrastructural cytochemistry of hatching gland cells in Xenopus embryos in relation to the hatching process. J. Fac. Sci. Hokkaido University Ser. VI 19, 309-314.
    • (1974) J. Fac. Sci. Hokkaido University Ser. VI , vol.19 , pp. 309-314
    • Yoshizaki, N.1
  • 28
    • 0028134180 scopus 로고
    • Identification and localization of a ligand molecule of Xenopus cortical granule lectins
    • Yoshizaki, N. 1994. Identification and localization of a ligand molecule of Xenopus cortical granule lectins. Zool. Sci. 11, 275-284.
    • (1994) Zool. Sci. , vol.11 , pp. 275-284
    • Yoshizaki, N.1
  • 29
    • 0000828056 scopus 로고
    • Necessity of oviducal pars recta secretions for the formation of the fertilization layer in Xenopus laevis
    • Yoshizaki, N. & Katagiri, C. 1984. Necessity of oviducal pars recta secretions for the formation of the fertilization layer in Xenopus laevis. Zool. Sci. 1, 255-264.
    • (1984) Zool. Sci. , vol.1 , pp. 255-264
    • Yoshizaki, N.1    Katagiri, C.2
  • 30
    • 0031903727 scopus 로고    scopus 로고
    • Purification and properties of embryonic cysteine proteinase which participates in yolk-lysis of Xenopus laevis
    • Yoshizaki, N., Moriyama, A. & Yonezawa, S. 1998. Purification and properties of embryonic cysteine proteinase which participates in yolk-lysis of Xenopus laevis. Comp. Biochem. Physiol. B119, 571-576.
    • (1998) Comp. Biochem. Physiol. , vol.B119 , pp. 571-576
    • Yoshizaki, N.1    Moriyama, A.2    Yonezawa, S.3
  • 31
    • 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. Develop Growth Differ. 36, 299-306.
    • (1994) Develop Growth Differ. , vol.36 , pp. 299-306
    • Yoshizaki, N.1    Yonezawa, S.2
  • 32
    • 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. Develop. Growth Differ. 38, 549-556.
    • (1996) Develop. Growth Differ. , vol.38 , pp. 549-556
    • Yoshizaki, N.1    Yonezawa, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.