메뉴 건너뛰기




Volumn 80, Issue 5, 2009, Pages 1001-1008

Comprehensive analysis of reproductive ADAMs: Relationship of ADAM4 and ADAM6 with an ADAM complex required for fertilization in mice

Author keywords

Fertilization; Sperm; Sperm maturation; Spermatogenesis; Testis

Indexed keywords

ADAM 24 PROTEIN; ADAM 26 PROTEIN; ADAM 29 PROTEIN; ADAM 4 PROTEIN; ADAM 6 PROTEIN; ADAM PROTEIN; UNCLASSIFIED DRUG;

EID: 65749101619     PISSN: 00063363     EISSN: 15297268     Source Type: Journal    
DOI: 10.1095/biolreprod.108.073700     Document Type: Article
Times cited : (56)

References (34)
  • 1
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain
    • Wolfsberg TG, Straight PD, Gerena RL, Huovila AP, Primakoff P, Myles DG, White JM. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev Biol 1995; 169:378-383.
    • (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
  • 2
    • 0030834283 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNF alpha and Notch
    • Blobel CP. Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNF alpha and Notch. Cell 1997; 90:589-592.
    • (1997) Cell , vol.90 , pp. 589-592
    • Blobel, C.P.1
  • 3
    • 0031698581 scopus 로고    scopus 로고
    • ADAMs: Focus on the protease domain
    • Black RA, White JM. ADAMs: focus on the protease domain. Curr Opin Cell Biol 1998; 10:654-659.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 654-659
    • Black, R.A.1    White, J.M.2
  • 4
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with adhesion and protease activity
    • DOI 10.1016/S0168-9525(99)01926-5, PII S0168952599019265
    • Primakoff P, Myles DG. The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet 2000; 16:83-87. (Pubitemid 30084721)
    • (2000) Trends in Genetics , vol.16 , Issue.2 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 5
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • DOI 10.1101/gad.1039703
    • Seals DF, Courtneidge SA. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 2003; 17:7-30. (Pubitemid 36062504)
    • (2003) Genes and Development , vol.17 , Issue.1 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 6
    • 33645051605 scopus 로고    scopus 로고
    • Mammalian ADAMs with testis-specific or -predominant expression
    • Hooper NM, Lendeckel U (eds.), Dordrecht, The Netherlands: Springer
    • Cho C. Mammalian ADAMs with testis-specific or -predominant expression. In: Hooper NM, Lendeckel U (eds.), The ADAM family of Proteases. Dordrecht, The Netherlands: Springer; 2005:239-259.
    • (2005) The ADAM Family of Proteases , pp. 239-259
    • Cho, C.1
  • 7
    • 0037193685 scopus 로고    scopus 로고
    • The ADAM1a and ADAM1b genes, instead of the ADAM1 (fertilin alpha) gene, are localized on mouse chromosome 5
    • DOI 10.1016/S0378-1119(02)00540-1, PII S0378111902005401
    • Nishimura H, Kim E, Fujimori T, Kashiwabara S, Kuroiwa A, Matsuda Y, Baba T. The ADAM1a and ADAM1b genes, instead of the ADAM1 (fertilin alpha) gene, are localized on mouse chromosome 5. Gene 2002; 291:67-76. (Pubitemid 34722378)
    • (2002) Gene , vol.291 , Issue.1-2 , pp. 67-76
    • Nishimura, H.1    Kim, E.2    Fujimori, T.3    Kashiwabara, S.-I.4    Kuroiwa, A.5    Matsuda, Y.6    Baba, T.7
  • 8
    • 1542719063 scopus 로고    scopus 로고
    • Characterization and comparative genomic analysis of intronless Adams with testicular gene expression
    • DOI 10.1016/j.ygeno.2003.10.001, PII S0888754303003173
    • Choi I, Oh J, Cho BN, Ahnn J, Jung YK, Han Kim D, Cho C. Characterization and comparative genomic analysis of intronless Adams with testicular gene expression. Genomics 2004; 83:636-646. (Pubitemid 38340805)
    • (2004) Genomics , vol.83 , Issue.4 , pp. 636-646
    • Choi, I.1    Oh, J.2    Cho, B.-N.3    Ahnn, J.4    Jung, Y.-K.5    Kim, D.H.6    Cho, C.7
  • 9
    • 0030793567 scopus 로고    scopus 로고
    • Genomic organization of the mouse fertilin beta gene that encodes an ADAM family protein active in sperm-egg fusion
    • DOI 10.1002/(SICI)1520-6408(1997)20:4<320::AID-DVG3>3.0.CO;2-9
    • Cho C, Turner L, Primakoff P, Myles DG. Genomic organization of the mouse fertilin beta gene that encodes an ADAM family protein active in sperm-egg fusion. Dev Genet 1997; 20:320-328. (Pubitemid 27337978)
    • (1997) Developmental Genetics , vol.20 , Issue.4 , pp. 320-328
    • Cho, C.1    Turner, L.2    Primakoff, P.3    Myles, D.G.4
  • 10
    • 0037472673 scopus 로고    scopus 로고
    • Identification and characterization of ADAM32 with testis-predominant gene expression
    • DOI 10.1016/S0378-1119(02)01202-7
    • Choi I, Woo JM, Hong S, Jung YK, Kim do H, Cho C. Identification and characterization of ADAM32 with testis-predominant gene expression. Gene 2003; 304:151-162. (Pubitemid 36142064)
    • (2003) Gene , vol.304 , Issue.1-2 , pp. 151-162
    • Choi, I.1    Woo, J.-M.2    Hong, S.3    Jung, Y.-K.4    Kim, D.H.5    Cho, C.6
  • 12
    • 0028841726 scopus 로고
    • Delayed translation and posttranslational processing of cyritestin, an integral transmembrane protein of the mouse acrosome
    • Linder B, Bammer S, Heinlein UA. Delayed translation and posttranslational processing of cyritestin, an integral transmembrane protein of the mouse acrosome. Exp Cell Res 1995; 221:66-72.
    • (1995) Exp Cell Res , vol.221 , pp. 66-72
    • Linder, B.1    Bammer, S.2    Heinlein, U.A.3
  • 13
    • 0030981901 scopus 로고    scopus 로고
    • Decreased in vitro fertilization efficiencies in the presence of specific cyritestin peptides
    • Linder B, Heinlein UA. Decreased in vitro fertilization efficiencies in the presence of specific cyritestin peptides. Dev Growth Differ 1997; 39:243-247. (Pubitemid 27164330)
    • (1997) Development Growth and Differentiation , vol.39 , Issue.2 , pp. 243-247
    • Linder, B.1    Heinlein, U.A.O.2
  • 14
    • 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
    • DOI 10.1083/jcb.137.1.105
    • Yuan R, Primakoff P, Myles DG. 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 1997; 137:105-112. (Pubitemid 27167299)
    • (1997) Journal of Cell Biology , vol.137 , Issue.1 , pp. 105-112
    • Yuan, R.1    Primakoff, P.2    Myles, D.G.3
  • 15
    • 0032544623 scopus 로고    scopus 로고
    • Fertilization defects in sperm from mice lacking fertilin beta
    • DOI 10.1126/science.281.5384.1857
    • Cho C, Bunch DO, Faure JE, Goulding EH, Eddy EM, Primakoff P, Myles DG. Fertilization defects in sperm from mice lacking fertilin beta. Science 1998; 281:1857-1859. (Pubitemid 28450507)
    • (1998) Science , vol.281 , Issue.5384 , pp. 1857-1859
    • Cho, C.1    Bunch, D.O.2    Faure, J.-E.3    Goulding, E.H.4    Eddy, E.M.5    Primakoff, P.6    Myles, D.C.7
  • 17
    • 0032782655 scopus 로고    scopus 로고
    • Mediation of sperm-egg fusion: Evidence that mouse egg alpha6beta1 integrin is the receptor for sperm fertilinbeta
    • Chen H, Sampson NS. Mediation of sperm-egg fusion: evidence that mouse egg alpha6beta1 integrin is the receptor for sperm fertilinbeta. Chem Biol 1999; 6:1-10.
    • (1999) Chem Biol , vol.6 , pp. 1-10
    • Chen, H.1    Sampson, N.S.2
  • 18
    • 0034660644 scopus 로고    scopus 로고
    • Analysis of mouse fertilin in wild-type and fertilin beta(-/-) sperm: Evidence for C-terminal modification, alpha/beta dimerization, and lack of essential role of fertilin alpha in sperm-egg fusion
    • DOI 10.1006/dbio.2000.9703
    • Cho C, Ge H, Branciforte D, Primakoff P, Myles DG. Analysis of mouse fertilin in wild-type and fertilin beta(-/-) sperm: evidence for C-terminal modification, alpha/beta dimerization, and lack of essential role of fertilin alpha in sperm-egg fusion. Dev Biol 2000; 222:289-295. (Pubitemid 30416367)
    • (2000) Developmental Biology , vol.222 , Issue.2 , pp. 289-295
    • Cho, C.1    Ge, H.2    Branciforte, D.3    Primakoff, P.4    Myles, D.G.5
  • 19
    • 0034657228 scopus 로고    scopus 로고
    • Cloning and characterization of ADAM28: Evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28
    • DOI 10.1042/0264-6021:3480021
    • Howard L, Maciewicz RA, Blobel CP. Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28. Biochem J 2000; 348(Pt 1):21-27. (Pubitemid 30312126)
    • (2000) Biochemical Journal , vol.348 , Issue.1 , pp. 21-27
    • Howard, L.1    Maciewicz, R.A.2    Blobel, C.P.3
  • 20
    • 0035337709 scopus 로고    scopus 로고
    • Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta
    • DOI 10.1006/dbio.2001.0166
    • Nishimura H, Cho C, Branciforte DR, Myles DG, Primakoff P. Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta. Dev Biol 2001; 233:204-213. (Pubitemid 32411305)
    • (2001) Developmental Biology , vol.233 , Issue.1 , pp. 204-213
    • Nishimura, H.1    Cho, C.2    Branciforte, D.R.3    Myles, D.G.4    Primakoff, P.5
  • 21
    • 0035005450 scopus 로고    scopus 로고
    • Testase 1 (ADAM 24) a plasma membrane-anchored sperm protease implicated in sperm function during epididymal maturation or fertilization
    • Zhu GZ, Myles DG, Primakoff P. Testase 1 (ADAM 24) a plasma membrane-anchored sperm protease implicated in sperm function during epididymal maturation or fertilization. J Cell Sci 2001; 114:1787-1794. (Pubitemid 32454676)
    • (2001) Journal of Cell Science , vol.114 , Issue.9 , pp. 1787-1794
    • Zhu, G.-Z.1    Myles, D.G.2    Primakoff, P.3
  • 23
    • 0037414440 scopus 로고    scopus 로고
    • Differential localization of ADAM1a and ADAM1b in the endoplasmic reticulum of testicular germ cells and on the surface of epididymal sperm
    • DOI 10.1016/S0006-291X(03)00588-6
    • Kim E, Nishimura H, Baba T. Differential localization of ADAM1a and ADAM1b in the endoplasmic reticulum of testicular germ cells and on the surface of epididymal sperm. Biochem Biophys Res Commun 2003; 304: 313-319. (Pubitemid 36444571)
    • (2003) Biochemical and Biophysical Research Communications , vol.304 , Issue.2 , pp. 313-319
    • Kim, E.1    Nishimura, H.2    Baba, T.3
  • 24
    • 4544250782 scopus 로고    scopus 로고
    • Possible function of the ADAM1a/ADAM2 fertilin complex in the appearance of ADAM3 on the sperm surface
    • DOI 10.1074/jbc.M314249200
    • Nishimura H, Kim E, Nakanishi T, Baba T. Possible function of the ADAM1a/ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface. J Biol Chem 2004; 279:34957-34962. (Pubitemid 39318132)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34957-34962
    • Nishimura, H.1    Kim, E.2    Nakanishi, T.3    Baba, T.4
  • 25
    • 13444281378 scopus 로고    scopus 로고
    • Synthesis, processing, and subcellular localization of mouse ADAM3 during spermatogenesis and epididymal sperm transport
    • DOI 10.1262/jrd.50.571
    • Kim E, Nishimura H, Iwase S, Yamagata K, Kashiwabara S, Baba T. Synthesis, processing, and subcellular localization of mouse ADAM3 during spermatogenesis and epididymal sperm transport. J Reprod Dev 2004; 50:571-578. (Pubitemid 40631782)
    • (2004) Journal of Reproduction and Development , vol.50 , Issue.5 , pp. 571-578
    • Kim, E.1    Nishimura, H.2    Iwase, S.3    Yamagata, K.4    Kashiwabara, S.-I.5    Baba, T.6
  • 26
    • 27144540547 scopus 로고    scopus 로고
    • Defects in secretory pathway trafficking during sperm development in Adam2 knockout mice
    • DOI 10.1095/biolreprod.105.040972
    • Stein KK, Go JC, Primakoff P, Myles DG. Defects in secretory pathway trafficking during sperm development in Adam2 knockout mice. Biol Reprod 2005; 73:1032-1038. (Pubitemid 41507509)
    • (2005) Biology of Reproduction , vol.73 , Issue.5 , pp. 1032-1038
    • Stein, K.K.1    Go, J.C.2    Primakoff, P.3    Myles, D.G.4
  • 29
    • 34547125812 scopus 로고    scopus 로고
    • Identification of an ADAM2-ADAM3 complex on the surface of mouse testicular germ cells and cauda epididymal sperm
    • DOI 10.1074/jbc.M702268200
    • Nishimura H, Myles DG, Primakoff P. Identification of an ADAM2- ADAM3 complex on the surface of mouse testicular germ cells and cauda epididymal sperm. J Biol Chem 2007; 282:17900-17907. (Pubitemid 47100315)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.24 , pp. 17900-17907
    • Nishimura, H.1    Myles, D.G.2    Primakoff, P.3
  • 30
    • 33750845874 scopus 로고    scopus 로고
    • Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)- And calmegin (Clgn)-deficient mice
    • Yamaguchi R, Yamagata K, Ikawa M, Moss SB, Okabe M. Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)- and calmegin (Clgn)-deficient mice. Biol Reprod 2006; 75:760-766.
    • (2006) Biol Reprod , vol.75 , pp. 760-766
    • Yamaguchi, R.1    Yamagata, K.2    Ikawa, M.3    Moss, S.B.4    Okabe, M.5
  • 31
    • 0025151870 scopus 로고
    • Evidence that proteolysis of the surface is an initial step in the mechanism of formation of sperm cell surface domains
    • Phelps BM, Koppel DE, Primakoff P, Myles DG. Evidence that proteolysis of the surface is an initial step in the mechanism of formation of sperm cell surface domains. J Cell Biol 1990; 111:1839-1847. (Pubitemid 20361292)
    • (1990) Journal of Cell Biology , vol.111 , Issue.5 I , pp. 1839-1847
    • Phelps, B.M.1    Koppel, D.E.2    Primakoff, P.3    Myles, D.G.4
  • 33
    • 0031282021 scopus 로고    scopus 로고
    • Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin
    • Lum L, Blobel CP. Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin. Dev Biol 1997; 191: 131-145. (Pubitemid 27519710)
    • (1997) Developmental Biology , vol.191 , Issue.1 , pp. 131-145
    • Lum, L.1    Blobel, C.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.