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Volumn 142, Issue 2, 2005, Pages 153-163

Expression and tissue distribution of astacin-like squid metalloprotease (ALSM)

Author keywords

ALSM; Astacin; Embryo; Expression; Liver; Metalloprotease; Squid; Tissue distribution

Indexed keywords

ASTACIN LIKE SQUID METALLOPROTEASE; ASTACIN LIKE SQUID METALLOPROTEASE I; ASTACIN LIKE SQUID METALLOPROTEASE III; ISOENZYME; MESSENGER RNA; METALLOPROTEINASE; UNCLASSIFIED DRUG;

EID: 24344462574     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2005.05.018     Document Type: Article
Times cited : (6)

References (36)
  • 1
    • 0001544446 scopus 로고
    • Embryonic stages of Loligo bleekeri Keferstein (Mollusca: Cephalopoda)
    • G. Baeg, Y. Sakurai, and K. Shimazaki Embryonic stages of Loligo bleekeri Keferstein (Mollusca: Cephalopoda) Veliger 35 1992 234 241
    • (1992) Veliger , vol.35 , pp. 234-241
    • Baeg, G.1    Sakurai, Y.2    Shimazaki, K.3
  • 2
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'
    • W. Bode, F.X. Gomis-Ruth, and W. Stocker Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins' FEBS Lett. 331 1993 134 140
    • (1993) FEBS Lett. , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Ruth, F.X.2    Stocker, W.3
  • 3
    • 0029016839 scopus 로고
    • The astacin family of metalloendopeptidases
    • J.S. Bond, and R.J. Beynon The astacin family of metalloendopeptidases Protein Sci. 4 1995 1247 1261
    • (1995) Protein Sci. , vol.4 , pp. 1247-1261
    • Bond, J.S.1    Beynon, R.J.2
  • 4
    • 0023470609 scopus 로고
    • Distribution of meprin in kidneys from mice with high- and low-meprin activity
    • S.S. Craig, J.F. Reckelhoff, and J.S. Bond Distribution of meprin in kidneys from mice with high- and low-meprin activity Am. J. Physiol. 253 1987 C535 C540
    • (1987) Am. J. Physiol. , vol.253
    • Craig, S.S.1    Reckelhoff, J.F.2    Bond, J.S.3
  • 6
    • 0034795758 scopus 로고    scopus 로고
    • Properties of the hatching enzyme from Xenopus laevis
    • T.J. Fan, and C. Katagiri Properties of the hatching enzyme from Xenopus laevis Eur. J. Biochem. 268 2001 4892 4898
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4892-4898
    • Fan, T.J.1    Katagiri, C.2
  • 7
  • 8
    • 2542472436 scopus 로고    scopus 로고
    • Structure and developmental expression of hatching enzyme genes of the Japanese eel Anguilla japonica: An aspect of the evolution of fish hatching enzyme gene
    • J. Hiroi, K. Maruyama, K. Kawazu, T. Kaneko, R. Ohtani-Kaneko, and S. Yasumasu Structure and developmental expression of hatching enzyme genes of the Japanese eel Anguilla japonica: an aspect of the evolution of fish hatching enzyme gene Dev. Genes Evol. 214 2004 176 184
    • (2004) Dev. Genes Evol. , vol.214 , pp. 176-184
    • Hiroi, J.1    Maruyama, K.2    Kawazu, K.3    Kaneko, T.4    Ohtani-Kaneko, R.5    Yasumasu, S.6
  • 9
    • 0028862762 scopus 로고
    • Temporal and spatial patterns of gene expression for the hatching enzyme in the teleost embryo, Oryzias latipes
    • K. Inohaya, S. Yasumasu, M. Ishimaru, A. Ohyama, I. Iuchi, and K. Yamagami Temporal and spatial patterns of gene expression for the hatching enzyme in the teleost embryo, Oryzias latipes Dev. Biol. 171 1995 374 385
    • (1995) Dev. Biol. , vol.171 , pp. 374-385
    • Inohaya, K.1    Yasumasu, S.2    Ishimaru, M.3    Ohyama, A.4    Iuchi, I.5    Yamagami, K.6
  • 10
    • 0036333809 scopus 로고    scopus 로고
    • Competency of embryonic cardiomyocytes to undergo Purkinje fiber differentiation is regulated by endothelin receptor expression
    • N. Kanzawa, C.P. Poma, K. Takebayashi-Suzuki, K.G. Diaz, J. Layliev, and T. Mikawa Competency of embryonic cardiomyocytes to undergo Purkinje fiber differentiation is regulated by endothelin receptor expression Development 129 2002 3185 3194
    • (2002) Development , vol.129 , pp. 3185-3194
    • Kanzawa, N.1    Poma, C.P.2    Takebayashi-Suzuki, K.3    Diaz, K.G.4    Layliev, J.5    Mikawa, T.6
  • 11
    • 0031029642 scopus 로고    scopus 로고
    • Molecular cloning of Xenopus hatching enzyme and its specific expression in hatching gland cells
    • C. Katagiri, R. Maeda, C. Yamashika, K. Mita, T.D. Sargent, and S. Yasumasu Molecular cloning of Xenopus hatching enzyme and its specific expression in hatching gland cells Int. J. Dev. Biol. 41 1997 19 25
    • (1997) Int. J. Dev. Biol. , vol.41 , pp. 19-25
    • Katagiri, C.1    Maeda, R.2    Yamashika, C.3    Mita, K.4    Sargent, T.D.5    Yasumasu, S.6
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0028069474 scopus 로고
    • HCE, a constituent of the hatching enzymes of Oryzias latipes embryos, releases unique proline-rich polypeptides from its natural substrate, the hardened chorion
    • K.S. Lee, S. Yasumasu, K. Nomura, and I. Iuchi HCE, a constituent of the hatching enzymes of Oryzias latipes embryos, releases unique proline-rich polypeptides from its natural substrate, the hardened chorion FEBS Lett. 339 1994 281 284
    • (1994) FEBS Lett. , vol.339 , pp. 281-284
    • Lee, K.S.1    Yasumasu, S.2    Nomura, K.3    Iuchi, I.4
  • 14
    • 0030671306 scopus 로고    scopus 로고
    • Production of a DPP activity gradient in the early Drosophila embryo through the opposing actions of the SOG and TLD proteins
    • G. Marques, M. Musacchio, M.J. Shimell, K. Wunnenberg-Stapleton, K.W. Cho, and M.B. O'Connor Production of a DPP activity gradient in the early Drosophila embryo through the opposing actions of the SOG and TLD proteins Cell 91 1997 417 426
    • (1997) Cell , vol.91 , pp. 417-426
    • Marques, G.1    Musacchio, M.2    Shimell, M.J.3    Wunnenberg-Stapleton, K.4    Cho, K.W.5    O'Connor, M.B.6
  • 15
    • 17444450739 scopus 로고    scopus 로고
    • The astacin protein family in Caenorhabditis elegans
    • F. Mohrlen, H. Hutter, and R. Zwilling The astacin protein family in Caenorhabditis elegans Eur. J. Biochem. 270 2003 4909 4920
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4909-4920
    • Mohrlen, F.1    Hutter, H.2    Zwilling, R.3
  • 16
    • 0027463895 scopus 로고
    • Purification and characterization of two metalloproteinases from squid mantle muscle, myosinase I and myosinase II
    • Y. Okamoto, H. Otsuka-Fuchino, S. Horiuchi, T. Tamiya, J.J. Matsumoto, and T. Tsuchiya Purification and characterization of two metalloproteinases from squid mantle muscle, myosinase I and myosinase II Biochim. Biophys. Acta 1161 1993 97 104
    • (1993) Biochim. Biophys. Acta , vol.1161 , pp. 97-104
    • Okamoto, Y.1    Otsuka-Fuchino, H.2    Horiuchi, S.3    Tamiya, T.4    Matsumoto, J.J.5    Tsuchiya, T.6
  • 17
    • 0030598867 scopus 로고    scopus 로고
    • Dorsoventral patterning in Xenopus: Inhibition of ventral signals by direct binding of chordin to BMP-4
    • S. Piccolo, Y. Sasai, B. Lu, and E.M. De Robertis Dorsoventral patterning in Xenopus: inhibition of ventral signals by direct binding of chordin to BMP-4 Cell 86 1996 589 598
    • (1996) Cell , vol.86 , pp. 589-598
    • Piccolo, S.1    Sasai, Y.2    Lu, B.3    De Robertis, E.M.4
  • 19
    • 0030159796 scopus 로고    scopus 로고
    • BMP-1 and the astacin family of metalloproteinases: A potential link between the extracellular matrix, growth factors and pattern formation
    • M.P. Sarras Jr. BMP-1 and the astacin family of metalloproteinases: a potential link between the extracellular matrix, growth factors and pattern formation BioEssays 18 1996 439 442
    • (1996) BioEssays , vol.18 , pp. 439-442
    • Sarras Jr., M.P.1
  • 20
    • 0028221677 scopus 로고
    • A T7 expression vector for producing N- and C-terminal fusion proteins with glutathione S-transferase
    • A.D. Sharrocks A T7 expression vector for producing N- and C-terminal fusion proteins with glutathione S-transferase Gene 138 1994 105 108
    • (1994) Gene , vol.138 , pp. 105-108
    • Sharrocks, A.D.1
  • 21
    • 0025986820 scopus 로고
    • The Drosophila dorsal-ventral patterning gene tolloid is related to human bone morphogenetic protein 1
    • M.J. Shimell, E.L. Ferguson, S.R. Childs, and M.B. O'Connor The Drosophila dorsal-ventral patterning gene tolloid is related to human bone morphogenetic protein 1 Cell 67 1991 469 481
    • (1991) Cell , vol.67 , pp. 469-481
    • Shimell, M.J.1    Ferguson, E.L.2    Childs, S.R.3    O'Connor, M.B.4
  • 22
    • 1842582323 scopus 로고
    • A new ribboning embedding medium for histology
    • H.F. Steedman A new ribboning embedding medium for histology Nature 179 1957 1345
    • (1957) Nature , vol.179 , pp. 1345
    • Steedman, H.F.1
  • 23
    • 0000854427 scopus 로고    scopus 로고
    • Distribution of myosinase I and myosinase II in tissues of Coleoidea
    • T. Tajima, J. Tamori, N. Kanzawa, T. Tamiya, and T. Tsuchiya Distribution of myosinase I and myosinase II in tissues of Coleoidea Fish. Sci. 64 1998 808 811
    • (1998) Fish. Sci. , vol.64 , pp. 808-811
    • Tajima, T.1    Tamori, J.2    Kanzawa, N.3    Tamiya, T.4    Tsuchiya, T.5
  • 24
    • 0028608106 scopus 로고
    • Bone morphogenetic protein-1 and a mammalian tolloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues
    • K. Takahara, G.E. Lyons, and D.S. Greenspan Bone morphogenetic protein-1 and a mammalian tolloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues J. Biol. Chem. 269 1994 32572 32578
    • (1994) J. Biol. Chem. , vol.269 , pp. 32572-32578
    • Takahara, K.1    Lyons, G.E.2    Greenspan, D.S.3
  • 25
    • 0033825398 scopus 로고    scopus 로고
    • In vivo induction of cardiac Purkinje fiber differentiation by coexpression of preproendothelin-1 and endothelin converting enzyme-1
    • K. Takebayashi-Suzuki, M. Yanagisawa, R.G. Gourdie, N. Kanzawa, and T. Mikawa In vivo induction of cardiac Purkinje fiber differentiation by coexpression of preproendothelin-1 and endothelin converting enzyme-1 Development 127 2000 3523 3532
    • (2000) Development , vol.127 , pp. 3523-3532
    • Takebayashi-Suzuki, K.1    Yanagisawa, M.2    Gourdie, R.G.3    Kanzawa, N.4    Mikawa, T.5
  • 26
    • 0032731204 scopus 로고    scopus 로고
    • Purification and characterization of a novel isoform of myosinase from spear squid liver
    • J. Tamori, N. Kanzawa, T. Tajima, T. Tamiya, and T. Tsuchiya Purification and characterization of a novel isoform of myosinase from spear squid liver J. Biochem. (Tokyo) 126 1999 969 974
    • (1999) J. Biochem. (Tokyo) , vol.126 , pp. 969-974
    • Tamori, J.1    Kanzawa, N.2    Tajima, T.3    Tamiya, T.4    Tsuchiya, T.5
  • 28
    • 0024526399 scopus 로고
    • Biosynthesis of Astacus protease, a digestive enzyme from crayfish
    • G. Vogt, W. Stocker, V. Storch, and R. Zwilling Biosynthesis of Astacus protease, a digestive enzyme from crayfish Histochemistry 91 1989 373 381
    • (1989) Histochemistry , vol.91 , pp. 373-381
    • Vogt, G.1    Stocker, W.2    Storch, V.3    Zwilling, R.4
  • 30
    • 0025775951 scopus 로고
    • A membrane-bound metallo-endopeptidase from rat kidney hydrolyzing parathyroid hormone. Purification and characterization
    • T. Yamaguchi, H. Kido, M. Fukase, T. Fujita, and N. Katunuma A membrane-bound metallo-endopeptidase from rat kidney hydrolyzing parathyroid hormone. Purification and characterization Eur. J. Biochem. 200 1991 563 571
    • (1991) Eur. J. Biochem. , vol.200 , pp. 563-571
    • Yamaguchi, T.1    Kido, H.2    Fukase, M.3    Fujita, T.4    Katunuma, N.5
  • 31
    • 0028990388 scopus 로고
    • r hydra metalloproteinase (HMP1), a member of the astacin family, localizes to the extracellular matrix of Hydra vulgaris in a head-specific manner and has a developmental function
    • r hydra metalloproteinase (HMP1), a member of the astacin family, localizes to the extracellular matrix of Hydra vulgaris in a head-specific manner and has a developmental function Development 121 1995 1591 1602
    • (1995) Development , vol.121 , pp. 1591-1602
    • Yan, L.1    Pollock, G.H.2    Nagase, H.3    Sarras Jr., M.P.4
  • 32
    • 0033959339 scopus 로고    scopus 로고
    • Identification and characterization of hydra metalloproteinase 2 (HMP2): A meprin-like astacin metalloproteinase that functions in foot morphogenesis
    • L. Yan, K. Fei, J. Zhang, S. Dexter, and M.P. Sarras Jr. Identification and characterization of hydra metalloproteinase 2 (HMP2): a meprin-like astacin metalloproteinase that functions in foot morphogenesis Development 127 2000 129 141
    • (2000) Development , vol.127 , pp. 129-141
    • Yan, L.1    Fei, K.2    Zhang, J.3    Dexter, S.4    Sarras Jr., M.P.5
  • 33
    • 0034163284 scopus 로고    scopus 로고
    • Hydra metalloproteinase 1: A secreted astacin metalloproteinase whose apical axis expression is differentially regulated during head regeneration
    • L. Yan, A. Leontovich, K. Fei, and M.P. Sarras Jr. Hydra metalloproteinase 1: a secreted astacin metalloproteinase whose apical axis expression is differentially regulated during head regeneration Dev. Biol. 219 2000 115 128
    • (2000) Dev. Biol. , vol.219 , pp. 115-128
    • Yan, L.1    Leontovich, A.2    Fei, K.3    Sarras Jr., M.P.4
  • 34
    • 0026512758 scopus 로고
    • Two constituent proteases of a teleostean hatching enzyme: Concurrent syntheses and packaging in the same secretory granules in discrete arrangement
    • S. Yasumasu, S. Katow, T.S. Hamazaki, I. Iuchi, and K. Yamagami Two constituent proteases of a teleostean hatching enzyme: concurrent syntheses and packaging in the same secretory granules in discrete arrangement Dev. Biol. 149 1992 349 356
    • (1992) Dev. Biol. , vol.149 , pp. 349-356
    • Yasumasu, S.1    Katow, S.2    Hamazaki, T.S.3    Iuchi, I.4    Yamagami, K.5
  • 35
    • 0026697681 scopus 로고
    • Isolation of cDNAs for LCE and HCE, two constituent proteases of the hatching enzyme of Oryzias latipes, and concurrent expression of their mRNAs during development
    • S. Yasumasu, K. Yamada, K. Akasaka, K. Mitsunaga, I. Iuchi, H. Shimada, and K. Yamagami Isolation of cDNAs for LCE and HCE, two constituent proteases of the hatching enzyme of Oryzias latipes, and concurrent expression of their mRNAs during development Dev. Biol. 153 1992 250 258
    • (1992) Dev. Biol. , vol.153 , pp. 250-258
    • Yasumasu, S.1    Yamada, K.2    Akasaka, K.3    Mitsunaga, K.4    Iuchi, I.5    Shimada, H.6    Yamagami, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.