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Volumn 3, Issue 9, 1997, Pages 801-809

Cloning and sequence analysis of rat fertilin a and β - Developmental expression, processing and immunolocalization

Author keywords

Disintegrin; Immunocontraception; Metalloproteinase; Oolemma; Spermatozoa

Indexed keywords

ADAM PROTEIN; COMPLEMENTARY DNA; FERTILIN; MEMBRANE PROTEIN; METALLOPROTEINASE;

EID: 0031230679     PISSN: 13609947     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (38)

References (34)
  • 2
    • 0028142697 scopus 로고
    • The contraceptive potential of fertilization: A physiological perspective
    • Bedford, J.M. (1994) The contraceptive potential of fertilization: a physiological perspective. Hum. Reprod., 9, 842-858.
    • (1994) Hum. Reprod. , vol.9 , pp. 842-858
    • Bedford, J.M.1
  • 3
    • 0025371355 scopus 로고
    • Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilisation competence
    • Blobel, C.P., Myles, D.O., Primakoff, P. and White, JM. (1990) Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilisation competence. J. Cell Biol., 111, 69-78.
    • (1990) J. Cell Biol. , vol.111 , pp. 69-78
    • Blobel, C.P.1    Myles, D.O.2    Primakoff, P.3    White, J.M.4
  • 4
    • 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. et al (1992) A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature, 356, 248-252.
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3
  • 5
    • 0025650560 scopus 로고
    • Evidence that an Arg-Gly-Asp adhesion sequence plays a role in mammalian fertilization
    • Bronson, R.A. and Fusi, F. (1990) Evidence that an Arg-Gly-Asp adhesion sequence plays a role in mammalian fertilization. Biol. Reprod., 43, 1019-1025
    • (1990) Biol. Reprod. , vol.43 , pp. 1019-1025
    • Bronson, R.A.1    Fusi, F.2
  • 6
    • 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. and Cowan, A.E. (1995) Surface expression of the pre-β subunit of fertilin is regulated at a post-translational level in guinea pig spermatids. Devel Biol, 168, 429-437.
    • (1995) Devel Biol , vol.168 , pp. 429-437
    • Carroll, D.J.1    Dikegoros, E.2    Koppel, D.E.3    Cowan, A.E.4
  • 7
    • 0023866571 scopus 로고
    • Metalloprotease cleavage of 18.2- and 14.1-kilodalton basic proteins dissociating from rodent myelin membranes generates 10.0- and 5.9-kilodalton C-terminal fragments
    • Chantry, A., Earl, C., Groome, N. and Glynn, P. (1988) Metalloprotease cleavage of 18.2- and 14.1-kilodalton basic proteins dissociating from rodent myelin membranes generates 10.0- and 5.9-kilodalton C-terminal fragments. J. Neurochem., 50, 688-694.
    • (1988) J. Neurochem. , vol.50 , pp. 688-694
    • Chantry, A.1    Earl, C.2    Groome, N.3    Glynn, P.4
  • 8
    • 0027471650 scopus 로고
    • Biogenesis of surface domains during spermiogenesis in the guinea pig
    • Cowan, A.E. and Myles, D.O. (1993) Biogenesis of surface domains during spermiogenesis in the guinea pig. Devel. Biol., 155, 124-133
    • (1993) Devel. Biol. , vol.155 , pp. 124-133
    • Cowan, A.E.1    Myles, D.O.2
  • 9
    • 0029162781 scopus 로고
    • Mouse sperm-egg plasma membrane interactions: Analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) β
    • Evans, J.P., Schultz, R.M. and Kopf, G.S. (1995) Mouse sperm-egg plasma membrane interactions: analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) β. J. Cell Sci., 108, 3267-3278.
    • (1995) J. Cell Sci. , vol.108 , pp. 3267-3278
    • Evans, J.P.1    Schultz, R.M.2    Kopf, G.S.3
  • 10
    • 0026527823 scopus 로고
    • Structure and expression of the rat epididymal secretory protein 1 gene
    • Girorti, M., Jones, R., Emery, D.C. et al. (1992) Structure and expression of the rat epididymal secretory protein 1 gene. Biochem. J., 281, 203-210.
    • (1992) Biochem. J. , vol.281 , pp. 203-210
    • Girorti, M.1    Jones, R.2    Emery, D.C.3
  • 12
    • 0029850171 scopus 로고    scopus 로고
    • Cloning and expression of recombinant rabbit fertilin
    • Hardy, C.M. and Holland, M.K. (1996) Cloning and expression of recombinant rabbit fertilin. Mol. Reprod. Devel., 45, 107-116
    • (1996) Mol. Reprod. Devel. , vol.45 , pp. 107-116
    • Hardy, C.M.1    Holland, M.K.2
  • 13
    • 0028337108 scopus 로고
    • CDNA sequences for four snake venom metalloproteinases: Structure, classification, and their relative relationship to mammalian reproductive proteins
    • Hite, L. A., Jia, L-G., Bjarnason, J.B. and Fox, J.W. (1994) cDNA sequences for four snake venom metalloproteinases: structure, classification, and their relative relationship to mammalian reproductive proteins. Arch. Biochem. Biophys., 308, 182-191.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 182-191
    • Hite, L.A.1    Jia, L.-G.2    Bjarnason, J.B.3    Fox, J.W.4
  • 14
    • 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. et al. (1996) Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types. Biochem. J., 317, 45-50.
    • (1996) Biochem. J. , vol.317 , pp. 45-50
    • Howard, L.1    Lu, X.2    Mitchell, S.3
  • 15
    • 0030630628 scopus 로고    scopus 로고
    • Matrix metalloproteinases as mediators of reproductive function
    • Hulboy, D.L., Rudolph, L.A. and Matrisian, L.M. (1997) Matrix metalloproteinases as mediators of reproductive function. Mol. Hum. Reprod., 3, 27-45.
    • (1997) Mol. Hum. Reprod. , vol.3 , pp. 27-45
    • Hulboy, D.L.1    Rudolph, L.A.2    Matrisian, L.M.3
  • 16
    • 0022492423 scopus 로고
    • Preparation of a plasma membrane-rich fraction from rat spermatozoa
    • Jones, R. (1986) Preparation of a plasma membrane-rich fraction from rat spermatozoa. J. Reprod. Fertil, 77, 435-449.
    • (1986) J. Reprod. Fertil , vol.77 , pp. 435-449
    • Jones, R.1
  • 17
    • 0025340235 scopus 로고
    • Topographical rearrangement of a plasma membrane antigen during capacitation of rat spermatozoa in vitro
    • Jones, R., Shalgi, R., Hoyland, J. and Phillips, D.M. (1990) Topographical rearrangement of a plasma membrane antigen during capacitation of rat spermatozoa in vitro. Devel. Biol., 139, 349-362.
    • (1990) Devel. Biol. , vol.139 , pp. 349-362
    • Jones, R.1    Shalgi, R.2    Hoyland, J.3    Phillips, D.M.4
  • 18
    • 0029861018 scopus 로고    scopus 로고
    • Testicular biosynthesis and epididymal endoproteolytic processing of rat sperm surface antigen 2B1
    • Jones, R., Ma, A., Hou, S.-T. et al. (1996) Testicular biosynthesis and epididymal endoproteolytic processing of rat sperm surface antigen 2B1. J. Cell Sci., 109, 2561-2570.
    • (1996) J. Cell Sci. , vol.109 , pp. 2561-2570
    • Jones, R.1    Ma, A.2    Hou, S.-T.3
  • 19
    • 0028290681 scopus 로고
    • Gamete immunology
    • Jones, W.R. (1994) Gamete immunology. Hum Reprod, 9, 828-841.
    • (1994) Hum Reprod , vol.9 , pp. 828-841
    • Jones, W.R.1
  • 20
    • 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. and Hall, L. (1997) The human fertilin α gene is non-functional: implications for its proposed role in fertilization. Biochem. J., 321, 577-581.
    • (1997) Biochem. J. , vol.321 , pp. 577-581
    • Jury, J.A.1    Frayne, J.2    Hall, L.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0009732037 scopus 로고
    • Definition of the stages of the seminiferous epithelium in the rat
    • Leblond CP, Clermont Y (1952): Definition of the stages of the seminiferous epithelium in the rat. Ann. N.Y. Acad. Sci., 55, 548-573.
    • (1952) Ann. N.Y. Acad. Sci. , vol.55 , pp. 548-573
    • Leblond, C.P.1    Clermont, Y.2
  • 23
    • 2442437625 scopus 로고
    • Monkey fertilin β peptides inhibit sperm-egg binding in vitro and have a contraceptive effect
    • Mwethera, P.O., Perry, A.C.F., Hall, L. et al. (1995) Monkey fertilin β peptides inhibit sperm-egg binding in vitro and have a contraceptive effect. J. Reprod. Fertil. (Abstr. Series), 16, 11.
    • (1995) J. Reprod. Fertil. (Abstr. Series) , vol.16 , pp. 11
    • Mwethera, P.O.1    Perry, A.C.F.2    Hall, L.3
  • 24
    • 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.O. and Primakoff, P. (1997) 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, 320-327.
    • (1997) Biol. Reprod. , vol.56 , pp. 320-327
    • Myles, D.O.1    Primakoff, P.2
  • 25
    • 0028325475 scopus 로고
    • Identification of a binding site in the disintegrin domain of fertilin required for spermegg fusion
    • Myles, D.G., Kimmel, L.H., Blobel, C.P. et al. (1994) Identification of a binding site in the disintegrin domain of fertilin required for spermegg fusion. Proc. Natl. Acad. Sci. USA., 91, 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
  • 26
    • 0026774863 scopus 로고
    • A mammalian epididymal protein with remarkable sequence similarity to snake venom haemorrhagic components
    • Perry, A.C.F., Jones, R., Barker, P.J. and Hall, L. (1992) A mammalian epididymal protein with remarkable sequence similarity to snake venom haemorrhagic components. Biochem. J., 286, 671-675.
    • (1992) Biochem. J. , vol.286 , pp. 671-675
    • Perry, A.C.F.1    Jones, R.2    Barker, P.J.3    Hall, L.4
  • 27
    • 0029021536 scopus 로고
    • Cloning and analysis of monkey fertilin reveals novel a subunit isoforms
    • Perry, A.C.F., Gichuhi, P.M., Jones, R. and Hall, L. (1995a) Cloning and analysis of monkey fertilin reveals novel a subunit isoforms. Biochem. J., 307, 843-850.
    • (1995) Biochem. J. , vol.307 , pp. 843-850
    • Perry, A.C.F.1    Gichuhi, P.M.2    Jones, R.3    Hall, L.4
  • 28
    • 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.F., Jones, R. and Hall, L. (1995b) 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, 239-244.
    • (1995) Biochem. J. , vol.312 , pp. 239-244
    • Perry, A.C.F.1    Jones, R.2    Hall, L.3
  • 29
    • 0023100910 scopus 로고
    • Identification and purification of a sperm surface protein with a potential role in spermegg membrane fusion
    • Primakoff, P., Hyatt, H. and Tredick-Kline, J. (1987) Identification and purification of a sperm surface protein with a potential role in spermegg membrane fusion. J. Cell Biol., 124, 141-149
    • (1987) J. Cell Biol. , vol.124 , pp. 141-149
    • Primakoff, P.1    Hyatt, H.2    Tredick-Kline, J.3
  • 31
    • 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., Blobel, C.P. et al. (1993) 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, 10783-10787.
    • (1993) Proc. Natl Acad. Sci. USA. , vol.90 , pp. 10783-10787
    • Wolfsberg, T.G.1    Bazan, J.F.2    Blobel, C.P.3
  • 32
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain
    • Wolfsberg, T.G., Straight, P.D., Gerena, R.L. et al. (1995) ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Devel. Biol., 169, 378-383.
    • (1995) Devel. Biol. , vol.169 , pp. 378-383
    • Wolfsberg, T.G.1    Straight, P.D.2    Gerena, R.L.3
  • 33
    • 0002302562 scopus 로고
    • Mammalian fertilisation
    • Knobil, Z. and Neill, I.D. (eds) Raven Press, New York
    • Yanagimachi, R. (1994) Mammalian fertilisation. In Knobil, Z. and Neill, I.D. (eds) The Physiology of Reproduction. 2nd edn. Raven Press, New York, pp 189-317.
    • (1994) The Physiology of Reproduction. 2nd Edn. , pp. 189-317
    • Yanagimachi, R.1
  • 34
    • 0030951614 scopus 로고    scopus 로고
    • A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion
    • Yuan, R., Primakoff, P and Myles, D.G. (1997) A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion. J. Cell Biol., 137, 105-112.
    • (1997) J. Cell Biol. , vol.137 , pp. 105-112
    • Yuan, R.1    Primakoff, P.2    Myles, D.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.