메뉴 건너뛰기




Volumn 206, Issue 2, 1998, Pages 273-282

ADAM 20 and 21; Two novel human testis-specific membrane metalloproteases with similarity to fertilin-α

Author keywords

Degenerate PCR; Disintegrins; Spermatocytes; Zinc metalloproteases

Indexed keywords

ADAM 20; ADAM 21; FERTILIN ALPHA; MELTRIN GAMMA; MEMBRANE ENZYME; MESSENGER RNA; METALLOPROTEINASE; UNCLASSIFIED DRUG; ZINC ION;

EID: 0032509768     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(97)00597-0     Document Type: Article
Times cited : (63)

References (50)
  • 1
    • 0031568847 scopus 로고    scopus 로고
    • ADAM 13: A novel ADAM expressed in somitic mesoderm and neural crest cells during Xenopus laevis development
    • Alfandari D., Wolfsberg T.G., White J.M., DeSimone D.W. ADAM 13: a novel ADAM expressed in somitic mesoderm and neural crest cells during Xenopus laevis development. Dev. Biol. 182:1997;314-330.
    • (1997) Dev. Biol. , vol.182 , pp. 314-330
    • Alfandari, D.1    Wolfsberg, T.G.2    White, J.M.3    Desimone, D.W.4
  • 5
    • 0030834283 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNF-α And Notch
    • Blobel C.P. Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNF-α and Notch. Cell. 90:1997;589-592.
    • (1997) Cell , vol.90 , pp. 589-592
    • Blobel, C.P.1
  • 6
    • 0025371355 scopus 로고
    • Proteolytic processing of a protein involved in egg-sperm fusion correlates with acquisition of fertilization competence
    • Blobel C.P., Myles D.G., Primokoff P., White J. Proteolytic processing of a protein involved in egg-sperm fusion correlates with acquisition of fertilization competence. J. Cell Biol. 111:1990;69-78.
    • (1990) J. Cell Biol. , vol.111 , pp. 69-78
    • Blobel, C.P.1    Myles, D.G.2    Primokoff, P.3    White, J.4
  • 7
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel C.P., Wolfsberg T.G., Turck C.W., Myles D.G., Primakoff P., White J.M. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature. 356:1992;248-252.
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 8
    • 0028987051 scopus 로고
    • Surface expression of the pre-β subunit of fertilin is regulated at a post-translational level in guinea pig spermatids
    • Carroll D.J., Dikegoros E., Koppel D.E., Cowan A.E. Surface expression of the pre-β subunit of fertilin is regulated at a post-translational level in guinea pig spermatids. Dev. Biol. 168:1995;429-437.
    • (1995) Dev. Biol. , vol.168 , pp. 429-437
    • Carroll, D.J.1    Dikegoros, E.2    Koppel, D.E.3    Cowan, A.E.4
  • 9
    • 0030585736 scopus 로고    scopus 로고
    • Chromosomal assignment of four testis-expressed mouse genes from a new family of transmembrane proteins (ADAMs) involved in cell-cell adhesion and fusion
    • Cho C., Primakoff P., White J.M., Myles D.G. Chromosomal assignment of four testis-expressed mouse genes from a new family of transmembrane proteins (ADAMs) involved in cell-cell adhesion and fusion. Genomics. 34:1996;413-417.
    • (1996) Genomics , vol.34 , pp. 413-417
    • Cho, C.1    Primakoff, P.2    White, J.M.3    Myles, D.G.4
  • 10
    • 0027366136 scopus 로고
    • A novel metalloprotease/disintegrin-like gene at 17q21.3 is somatically rearranged in two primary breast cancers
    • Emi M., Katagiri T., Harada Y., Saito H., Inazawa J., Ito I., Kasumi F., Nakamura Y. A novel metalloprotease/disintegrin-like gene at 17q21.3 is somatically rearranged in two primary breast cancers. Nat. Genet. 5:1993;151-157.
    • (1993) Nat. Genet. , vol.5 , pp. 151-157
    • Emi, M.1    Katagiri, T.2    Harada, Y.3    Saito, H.4    Inazawa, J.5    Ito, I.6    Kasumi, F.7    Nakamura, Y.8
  • 11
    • 0031194395 scopus 로고    scopus 로고
    • Characterization of the binding of recombinant mouse sperm fertilin α subunit to mouse eggs: Evidence for function as a cell adhesion molecule in sperm-egg binding
    • Evans J.P., Schutz R.M., Kopf G.S. Characterization of the binding of recombinant mouse sperm fertilin α subunit to mouse eggs: evidence for function as a cell adhesion molecule in sperm-egg binding. Dev. Biol. 187:1997;94-106.
    • (1997) Dev. Biol. , vol.187 , pp. 94-106
    • Evans, J.P.1    Schutz, R.M.2    Kopf, G.S.3
  • 12
    • 0029822416 scopus 로고    scopus 로고
    • The cell surface metalloprotease/disintegrin Kuzbanian is required for axonal extension in Drosophila
    • Fambrough D., Pan D., Rubin G.M., Goodman C.S. The cell surface metalloprotease/disintegrin Kuzbanian is required for axonal extension in Drosophila. Proc. Natl. Acad. Sci. USA. 93:1996;13233-13238.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13233-13238
    • Fambrough, D.1    Pan, D.2    Rubin, G.M.3    Goodman, C.S.4
  • 13
    • 0027421462 scopus 로고
    • Activation of snake venom metalloproteinases by a cysteine switch-like mechanism
    • Grams F., Huber R., Kress L.F., Moroder L., Bode W. Activation of snake venom metalloproteinases by a cysteine switch-like mechanism. FEBS Lett. 335:1993;76-80.
    • (1993) FEBS Lett. , vol.335 , pp. 76-80
    • Grams, F.1    Huber, R.2    Kress, L.F.3    Moroder, L.4    Bode, W.5
  • 15
    • 0029923786 scopus 로고    scopus 로고
    • Update on the Center for Recombinant Gamete Contraceptive Vaccinogens
    • Herr J.C. Update on the Center for Recombinant Gamete Contraceptive Vaccinogens. Am. J. Reprod. Immunol. 35:1996;184-189.
    • (1996) Am. J. Reprod. Immunol. , vol.35 , pp. 184-189
    • Herr, J.C.1
  • 16
    • 0031025031 scopus 로고    scopus 로고
    • Expression of a disintegrin-like protein in cultured human vascular cells and in vivo
    • Herren B., Raines E.W., Ross R. Expression of a disintegrin-like protein in cultured human vascular cells and in vivo. FASEB J. 11:1997;173-180.
    • (1997) FASEB J. , vol.11 , pp. 173-180
    • Herren, B.1    Raines, E.W.2    Ross, R.3
  • 18
    • 0029995478 scopus 로고    scopus 로고
    • Molecular cloning of MADM: A catalytically active mammalian disintegrin-metalloprotease expressed in various cell types
    • Howard L., Lu X., Mitchell S., Griffiths S., Glynn P. Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types. Biochem. J. 317:1996;45-50.
    • (1996) Biochem. J. , vol.317 , pp. 45-50
    • Howard, L.1    Lu, X.2    Mitchell, S.3    Griffiths, S.4    Glynn, P.5
  • 21
    • 0031059822 scopus 로고    scopus 로고
    • The human fertilin α gene is non-functional: Implications for its proposed role in fertilization
    • Jury J.A., Frayne J., Hall L. The human fertilin α gene is non-functional: implications for its proposed role in fertilization. Biochem. J. 321:1997;577-581.
    • (1997) Biochem. J. , vol.321 , pp. 577-581
    • Jury, J.A.1    Frayne, J.2    Hall, L.3
  • 22
    • 0029670028 scopus 로고    scopus 로고
    • Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence
    • Krätzschmar J., Lum L., Blobel C.P. Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence. J. Biol. Chem. 271:1996;4593-4596.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4593-4596
    • Krätzschmar, J.1    Lum, L.2    Blobel, C.P.3
  • 23
    • 0028271015 scopus 로고
    • Chromosomal assignment of three novel mouse genes expressed in testicular cells
    • Lemaire L., Johnson K.R., Bammer S., Pery P., Ruddle F.H., Heinlein U.A. Chromosomal assignment of three novel mouse genes expressed in testicular cells. Genomics. 21:1994;409-414.
    • (1994) Genomics , vol.21 , pp. 409-414
    • Lemaire, L.1    Johnson, K.R.2    Bammer, S.3    Pery, P.4    Ruddle, F.H.5    Heinlein, U.A.6
  • 26
    • 0028146721 scopus 로고
    • A survey of furin substrate specificity using substrate phage display
    • Matthews D.J., Goodman L.J., Gorman C.M., Wells J.A. A survey of furin substrate specificity using substrate phage display. Protein Sci. 3:1994;1197-1205.
    • (1994) Protein Sci. , vol.3 , pp. 1197-1205
    • Matthews, D.J.1    Goodman, L.J.2    Gorman, C.M.3    Wells, J.A.4
  • 29
    • 0028293970 scopus 로고
    • Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion
    • Muga A., Neugebauer W., Hirama T., Surewicz W.K. Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion. Biochemistry. 33:1994;4444-4448.
    • (1994) Biochemistry , vol.33 , pp. 4444-4448
    • Muga, A.1    Neugebauer, W.2    Hirama, T.3    Surewicz, W.K.4
  • 30
    • 0028325475 scopus 로고
    • Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion
    • Myles D.G., Kimmel L.H., Blobel C.P., White J.M., Primakoff P. Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion. Proc. Natl. Acad. Sci. USA. 91:1994;4195-4198.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4195-4198
    • Myles, D.G.1    Kimmel, L.H.2    Blobel, C.P.3    White, J.M.4    Primakoff, P.5
  • 31
    • 0031049748 scopus 로고    scopus 로고
    • Why did the sperm cross the cumulus? To get to the oocyte. Functions of the sperm surface proteins PH-20 and fertilin in arriving at, and fusing with, the egg
    • Myles D.G., Primakoff P. Why did the sperm cross the cumulus? To get to the oocyte. Functions of the sperm surface proteins PH-20 and fertilin in arriving at, and fusing with, the egg. Biol. Reprod. 56:1997;320-327.
    • (1997) Biol. Reprod. , vol.56 , pp. 320-327
    • Myles, D.G.1    Primakoff, P.2
  • 32
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 33
    • 0027931811 scopus 로고
    • Genetic evidence for an additional member of the metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) family of mammalian proteins and its abundant expression in the testis
    • Perry A.C., Barker H.L., Jones R., Hall L. Genetic evidence for an additional member of the metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) family of mammalian proteins and its abundant expression in the testis. Biochim. Biophys. Acta. 1207:1994;134-137.
    • (1994) Biochim. Biophys. Acta , vol.1207 , pp. 134-137
    • Perry, A.C.1    Barker, H.L.2    Jones, R.3    Hall, L.4
  • 34
    • 0029021536 scopus 로고
    • Cloning and analysis of monkey fertilin reveals novel α subunit isoforms
    • Perry A.C., Gichuhi P.M., Jones R., Hall L. Cloning and analysis of monkey fertilin reveals novel α subunit isoforms. Biochem. J. 307:1995;843-850.
    • (1995) Biochem. J. , vol.307 , pp. 843-850
    • Perry, A.C.1    Gichuhi, P.M.2    Jones, R.3    Hall, L.4
  • 35
    • 0028864725 scopus 로고
    • Analysis of transcripts encoding novel members of the mammalian metalloprotease-like, disintegrin-like, cysteine-rich (MDC) protein family and their expression in reproductive and non-reproductive monkey tissues
    • Perry A.C., Jones R., Hall L. Analysis of transcripts encoding novel members of the mammalian metalloprotease-like, disintegrin-like, cysteine-rich (MDC) protein family and their expression in reproductive and non-reproductive monkey tissues. Biochem. J. 312:1995;239-244.
    • (1995) Biochem. J. , vol.312 , pp. 239-244
    • Perry, A.C.1    Jones, R.2    Hall, L.3
  • 36
    • 0029825782 scopus 로고    scopus 로고
    • ADM-1, a protein with metalloprotease- And disintegrin-like domains, is expressed in syncytial organs, sperm, and sheath cells of sensory organs in Caenorhabditis elegans
    • Podbilewicz B. ADM-1, a protein with metalloprotease- and disintegrin-like domains, is expressed in syncytial organs, sperm, and sheath cells of sensory organs in Caenorhabditis elegans. Mol. Biol. Cell. 7:1996;1877-1893.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1877-1893
    • Podbilewicz, B.1
  • 37
    • 0026555152 scopus 로고
    • PCR amplification of long DNA fragments
    • Ponce M.R., Micol J.L. PCR amplification of long DNA fragments. Nucleic Acids Res. 20:1992;623.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 623
    • Ponce, M.R.1    Micol, J.L.2
  • 38
    • 0030069394 scopus 로고    scopus 로고
    • Initial evaluation of fertilin as an immunocontraceptive antigen and molecular cloning of the cynomolgus monkey fertilin β subunit
    • Ramarao C.S., Myles D.G., White J.M., Primakoff P. Initial evaluation of fertilin as an immunocontraceptive antigen and molecular cloning of the cynomolgus monkey fertilin β subunit. Mol. Reprod. Dev. 43:1996;70-75.
    • (1996) Mol. Reprod. Dev. , vol.43 , pp. 70-75
    • Ramarao, C.S.1    Myles, D.G.2    White, J.M.3    Primakoff, P.4
  • 39
  • 40
    • 0029788321 scopus 로고    scopus 로고
    • KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis
    • Rooke J., Pan D., Xu T., Rubin G.M. KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis. Science. 273:1996;1227-1231.
    • (1996) Science , vol.273 , pp. 1227-1231
    • Rooke, J.1    Pan, D.2    Xu, T.3    Rubin, G.M.4
  • 42
    • 0029095760 scopus 로고
    • Structural features of a superfamily of zinc-endopeptidases: The metzincins
    • Stöcker W., Bode W. Structural features of a superfamily of zinc-endopeptidases: the metzincins. Curr. Opin. Struct. Biol. 5:1995;383-390.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 383-390
    • Stöcker, W.1    Bode, W.2
  • 43
    • 0025025442 scopus 로고
    • The cysteine swtich: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • van Wart H.E., Birkedal-Hansen H. The cysteine swtich: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. USA. 87:1990;5578-5582.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 44
    • 0031025409 scopus 로고    scopus 로고
    • Human fertilin β: Identification, characterization, and chromosomal mapping of an ADAM gene family member
    • Vidaeus C.M., von Kap-Herr C., Golden W.L., Eddy R.L., Shows T.B., Herr J.C. Human fertilin β: identification, characterization, and chromosomal mapping of an ADAM gene family member. Mol. Reprod. Dev. 46:1997;363-369.
    • (1997) Mol. Reprod. Dev. , vol.46 , pp. 363-369
    • Vidaeus, C.M.1    Von Kap-Herr, C.2    Golden, W.L.3    Eddy, R.L.4    Shows, T.B.5    Herr, J.C.6
  • 45
    • 0026492542 scopus 로고
    • Membrane fusion
    • White J.M. Membrane fusion. Science. 258:1992;917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 46
    • 0027431501 scopus 로고
    • The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: Structural, functional, and evolutionary implications
    • Wolfsberg T.G., Bazan J.F., Globel C.P., Myles D.G., Primakoff P., White J.M. The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications. Proc. Natl. Acad. Sci. USA. 90:1993;10783-10787.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10783-10787
    • Wolfsberg, T.G.1    Bazan, J.F.2    Globel, C.P.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 47
    • 0028820623 scopus 로고
    • ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: Multipotential functions in cell-cell and cell-matrix interactions
    • Wolfsberg T.G., Primakoff P., Myles D.G., White J.M. ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. J. Cell Biol. 131:1995;275-278.
    • (1995) J. Cell Biol. , vol.131 , pp. 275-278
    • Wolfsberg, T.G.1    Primakoff, P.2    Myles, D.G.3    White, J.M.4
  • 48
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disitingrin and metalloprotease domain
    • Wolfsberg T.G., Straight P.D., Gerena R.L., Huovila A.P., Primakoff P., Myles D.G., White J.M. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disitingrin and metalloprotease domain. Dev. Biol. 169:1995;378-383.
    • (1995) Dev. Biol. , vol.169 , pp. 378-383
    • Wolfsberg, T.G.1    Straight, P.D.2    Gerena, R.L.3    Huovila, A.P.4    Primakoff, P.5    Myles, D.G.6    White, J.M.7
  • 49
    • 0030589505 scopus 로고    scopus 로고
    • ADAMs in fertilization and development
    • Wolfsberg T.G., White J.M. ADAMs in fertilization and development. Dev. Biol. 180:1996;389-401.
    • (1996) Dev. Biol. , vol.180 , pp. 389-401
    • Wolfsberg, T.G.1    White, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.