메뉴 건너뛰기




Volumn 232, Issue 1, 2005, Pages 221-231

Metalloprotease-disintegrin ADAM8: Expression analysis and targeted deletion in mice

Author keywords

ADAM; CD156a; Lymphatic development; Metalloprotease disintegrin; MS2

Indexed keywords

DISINTEGRIN; MEMBRANE ENZYME; METALLOPROTEINASE; PROTEIN ADAM8; UNCLASSIFIED DRUG;

EID: 19944428083     PISSN: 10588388     EISSN: None     Source Type: Journal    
DOI: 10.1002/dvdy.20221     Document Type: Article
Times cited : (105)

References (53)
  • 2
    • 0031698581 scopus 로고    scopus 로고
    • ADAMs: Focus on the protease domain
    • Black RA, White JM. 1998. ADAMs: focus on the protease domain. Curr Opin Cell Biol 10:654-659.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 654-659
    • Black, R.A.1    White, J.M.2
  • 5
    • 0035059212 scopus 로고    scopus 로고
    • ADAM8: A novel osteoclast stimulating factor
    • Choi SJ, Han JH, Roodman GD. 2001. ADAM8: a novel osteoclast stimulating factor. J Bone Miner Res 16:814-822.
    • (2001) J Bone Miner Res , vol.16 , pp. 814-822
    • Choi, S.J.1    Han, J.H.2    Roodman, G.D.3
  • 7
    • 0029822416 scopus 로고    scopus 로고
    • The cell surface metalloprotease/disintegrin Kuzbanian is required for axonal extension in Drosophila
    • Fambrough D, Pan D, Rubin GM, Goodman CS. 1996. The cell surface metalloprotease/disintegrin Kuzbanian is required for axonal extension in Drosophila. Proc Natl Acad Sci. USA 93:13233-13238.
    • (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
  • 8
    • 0042232590 scopus 로고    scopus 로고
    • Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23
    • Fourie AM, Coles F, Moreno V, Karlsson L. 2003. Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23. J Biol Chem 278:30469-30477.
    • (2003) J Biol Chem , vol.278 , pp. 30469-30477
    • Fourie, A.M.1    Coles, F.2    Moreno, V.3    Karlsson, L.4
  • 9
    • 0035851124 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1)
    • Garton KJ, Gough PJ, Blobel CP, Murphy G, Greaves DR, Dempsey PJ, Raines EW. 2001. Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1). J Biol Chem 276:37993-38001.
    • (2001) J Biol Chem , vol.276 , pp. 37993-38001
    • Garton, K.J.1    Gough, P.J.2    Blobel, C.P.3    Murphy, G.4    Greaves, D.R.5    Dempsey, P.J.6    Raines, E.W.7
  • 11
    • 0036972233 scopus 로고    scopus 로고
    • CD156 transgenic mice. Different responses between inflammatory types
    • Higuchi Y, Yasui A, Matsuura K, Yamamoto S. 2002. CD156 transgenic mice. Different responses between inflammatory types. Pathobiology 70:47-54.
    • (2002) Pathobiology , vol.70 , pp. 47-54
    • Higuchi, Y.1    Yasui, A.2    Matsuura, K.3    Yamamoto, S.4
  • 12
    • 0042666789 scopus 로고    scopus 로고
    • Microarray analysis of peroxisome proliferator-activated receptor-gamma induced changes in gene expression in macrophages
    • Hodgkinson CP, Ye S. 2003. Microarray analysis of peroxisome proliferator-activated receptor-gamma induced changes in gene expression in macrophages. Biochem Biophys Res Commun 308:505-510.
    • (2003) Biochem Biophys Res Commun , vol.308 , pp. 505-510
    • Hodgkinson, C.P.1    Ye, S.2
  • 13
    • 0033851123 scopus 로고    scopus 로고
    • Protein processing mechanisms: From angiotensin-converting enzyme to Alzheimer's disease
    • Hooper NM, Turner AJ. 2000. Protein processing mechanisms: from angiotensin-converting enzyme to Alzheimer's disease. Biochem Soc Trans 28:441-446.
    • (2000) Biochem Soc Trans , vol.28 , pp. 441-446
    • Hooper, N.M.1    Turner, A.J.2
  • 16
    • 0037507267 scopus 로고    scopus 로고
    • Defective valvulogenesis in HB-EGF and TACE-null mice is associated with aberrant BMP signaling
    • Jackson LF, Qiu TH, Sunnarborg SW, Chang A, Zhang C, Patterson C, Lee DC. 2003. Defective valvulogenesis in HB-EGF and TACE-null mice is associated with aberrant BMP signaling. EMBO J 22:2704-2716.
    • (2003) EMBO J , vol.22 , pp. 2704-2716
    • Jackson, L.F.1    Qiu, T.H.2    Sunnarborg, S.W.3    Chang, A.4    Zhang, C.5    Patterson, C.6    Lee, D.C.7
  • 17
    • 0030850182 scopus 로고    scopus 로고
    • Structure of the murine CD156 gene, characterization of its promoter, and chromosomal location
    • Kataoka M, Yoshiyama K, Matsuura K, Hijiya N, Higuchi Y, Yamamoto S. 1997. Structure of the murine CD156 gene, characterization of its promoter, and chromosomal location. J Biol Chem 272:18209-18215.
    • (1997) J Biol Chem , vol.272 , pp. 18209-18215
    • Kataoka, M.1    Yoshiyama, K.2    Matsuura, K.3    Hijiya, N.4    Higuchi, Y.5    Yamamoto, S.6
  • 19
    • 0037080699 scopus 로고    scopus 로고
    • Kuzbanian-mediated cleavage of Drosophila Notch
    • Lieber T, Kidd S, Young MW. 2002. Kuzbanian-mediated cleavage of Drosophila Notch. Genes Dev 16:209-221.
    • (2002) Genes Dev , vol.16 , pp. 209-221
    • Lieber, T.1    Kidd, S.2    Young, M.W.3
  • 21
    • 0032475960 scopus 로고    scopus 로고
    • Intracellular maturation of the mouse metalloprotease disintegrin MDC15
    • Lum L, Reid MS, Blobel CP. 1998. Intracellular maturation of the mouse metalloprotease disintegrin MDC15. J Biol Chem 273:26236-26247.
    • (1998) J Biol Chem , vol.273 , pp. 26236-26247
    • Lum, L.1    Reid, M.S.2    Blobel, C.P.3
  • 23
    • 0025611985 scopus 로고
    • Gonadal expression of c-kit encoded at the W locus of the mouse
    • Manova K, Nocka K, Besmer P, Bachvarova RF. 1990. Gonadal expression of c-kit encoded at the W locus of the mouse. Development 110:1057-1069.
    • (1990) Development , vol.110 , pp. 1057-1069
    • Manova, K.1    Nocka, K.2    Besmer, P.3    Bachvarova, R.F.4
  • 24
    • 0024296027 scopus 로고
    • Disruption of the proto-oncogene int-2 in mouse embryo-derived cells: A general strategy for targeting mutations to nonselectable genes
    • Mansour SL, Thomas KR, Capecchi MR. 1988. Disruption of the proto-oncogene int-2 in mouse embryo-derived cells: a general strategy for targeting mutations to nonselectable genes. Nature 336:348-352.
    • (1988) Nature , vol.336 , pp. 348-352
    • Mansour, S.L.1    Thomas, K.R.2    Capecchi, M.R.3
  • 25
    • 0035930617 scopus 로고    scopus 로고
    • Metalloprotease-dependent protransforming growth factor-alpha ectodomain shedding in the absence of tumor necrosis factor-alpha-converting enzyme
    • Merlos-Suarez A, Ruiz-Paz S, Baselga J, Arribas J. 2001. Metalloprotease-dependent protransforming growth factor-alpha ectodomain shedding in the absence of tumor necrosis factor-alpha-converting enzyme. J Biol Chem 276:48510-48517.
    • (2001) J Biol Chem , vol.276 , pp. 48510-48517
    • Merlos-Suarez, A.1    Ruiz-Paz, S.2    Baselga, J.3    Arribas, J.4
  • 29
    • 0346458751 scopus 로고    scopus 로고
    • Lymphatic vasculature development
    • Oliver G. 2004. Lymphatic vasculature development. Nat Rev Immunol 4:35-45.
    • (2004) Nat Rev Immunol , vol.4 , pp. 35-45
    • Oliver, G.1
  • 30
    • 0343196671 scopus 로고    scopus 로고
    • KUZBANIAN controls proteolytic processing of NOTCH and mediates lateral inhibition during Drosophila and vertebrate neurogenesis
    • Pan D, Rubin J. 1997. KUZBANIAN controls proteolytic processing of NOTCH and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell 90:271-280.
    • (1997) Cell , vol.90 , pp. 271-280
    • Pan, D.1    Rubin, J.2
  • 32
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with an adhesion and protease activity packed into a single molecule
    • Primakoff P, Myles DG. 2000. The ADAM gene family: surface proteins with an adhesion and protease activity packed into a single molecule. Trends Genet 16:83-87.
    • (2000) Trends Genet , vol.16 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 34
    • 0029788321 scopus 로고    scopus 로고
    • KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis
    • Rooke J, Pan D, Xu T, Rubin GM. 1996. KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis. Science 273:1227-1230.
    • (1996) Science , vol.273 , pp. 1227-1230
    • Rooke, J.1    Pan, D.2    Xu, T.3    Rubin, G.M.4
  • 36
    • 0034332481 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha induces a metalloprotease-disintegrin, ADAM8 (CD 156): Implications for neuron-glia interactions during neurodegeneration
    • Schlomann U, Rathke-Hartlieb S, Yamamoto S, Jockusch H, Bartsch JW. 2000. Tumor necrosis factor alpha induces a metalloprotease-disintegrin, ADAM8 (CD 156): implications for neuron-glia interactions during neurodegeneration. J Neurosci 20:7964-7971.
    • (2000) J Neurosci , vol.20 , pp. 7964-7971
    • Schlomann, U.1    Rathke-Hartlieb, S.2    Yamamoto, S.3    Jockusch, H.4    Bartsch, J.W.5
  • 38
    • 0038541768 scopus 로고    scopus 로고
    • Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE)
    • Schlöndorff J, Becherer JD, Blobel CP. 2000. Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE). Biochem J 347(Pt 1):131-138.
    • (2000) Biochem J , vol.347 , Issue.PART 1 , pp. 131-138
    • Schlöndorff, J.1    Becherer, J.D.2    Blobel, C.P.3
  • 39
    • 0032741143 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Modular proteins capable of promoting cell-cell interactions and triggering signals by protein ectodomain shedding
    • Schlöndorff J, Blobel CP. 1999. Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein ectodomain shedding. J Cell Sci 112:3603-3617.
    • (1999) J Cell Sci , vol.112 , pp. 3603-3617
    • Schlöndorff, J.1    Blobel, C.P.2
  • 40
    • 0032127723 scopus 로고    scopus 로고
    • The disintegrin domain of ADAM 8 enhances protection against rat experimental autoimmune encephalomyelitis, neuritis and uveitis by a polyvalent autoantigen vaccine
    • Schluesener HJ. 1998. The disintegrin domain of ADAM 8 enhances protection against rat experimental autoimmune encephalomyelitis, neuritis and uveitis by a polyvalent autoantigen vaccine. J Neuroimmunol 87:197-202.
    • (1998) J Neuroimmunol , vol.87 , pp. 197-202
    • Schluesener, H.J.1
  • 41
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • Seals DF, Courtneidge SA. 2003. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 17:7-30.
    • (2003) Genes Dev , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 42
    • 0031457037 scopus 로고    scopus 로고
    • The metalloprotease-disintegrin Kuzbanian participates in Notch activation during growth and patterning of Drosophila imaginal discs
    • Sotillos S, Roch F, Campuzano S. 1997. The metalloprotease-disintegrin Kuzbanian participates in Notch activation during growth and patterning of Drosophila imaginal discs. Development 124:4769-4779.
    • (1997) Development , vol.124 , pp. 4769-4779
    • Sotillos, S.1    Roch, F.2    Campuzano, S.3
  • 43
    • 0028969678 scopus 로고
    • The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • Stocker W, Grams F, Baumann U, Reinemer P, Gomis-Ruth FX, McKay DB, Bode W. 1995. The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci 4:823-840.
    • (1995) Protein Sci , vol.4 , pp. 823-840
    • Stocker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Ruth, F.X.5    McKay, D.B.6    Bode, W.7
  • 45
    • 0037474312 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme/ADAM 17 mediates MUC1 shedding
    • Thathiah A, Blobel CP, Carson DD. 2003. Tumor necrosis factor-alpha converting enzyme/ADAM 17 mediates MUC1 shedding. J Biol Chem 278:3386-3394.
    • (2003) J Biol Chem , vol.278 , pp. 3386-3394
    • Thathiah, A.1    Blobel, C.P.2    Carson, D.D.3
  • 46
    • 0022542596 scopus 로고
    • High frequency targeting of genes to specific sites in the mammalian genome
    • Thomas KR, Folger KR, Capecchi MR. 1986. High frequency targeting of genes to specific sites in the mammalian genome. Cell 44:419-428.
    • (1986) Cell , vol.44 , pp. 419-428
    • Thomas, K.R.1    Folger, K.R.2    Capecchi, M.R.3
  • 48
    • 0036170534 scopus 로고    scopus 로고
    • Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life
    • Weskamp G, Cai H, Brodie TA, Higashyama S, Manova K, Ludwig T, Blobel CP. 2002. Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life. Mol Cell Biol 22:1537-1544.
    • (2002) Mol Cell Biol , vol.22 , pp. 1537-1544
    • Weskamp, G.1    Cai, H.2    Brodie, T.A.3    Higashyama, S.4    Manova, K.5    Ludwig, T.6    Blobel, C.P.7
  • 49
    • 1042278167 scopus 로고    scopus 로고
    • Evidence for a critical role of the TNFa convertase (TACE) in ectodomain shedding of the p75 neurotrophin receptor (p75NTR)
    • Weskamp G, Schlöndorff J, Lum L, Saftig P, Hartmann D, Becherer D, Murphy G, Blobel CP. 2004. Evidence for a critical role of the TNFa convertase (TACE) in ectodomain shedding of the p75 neurotrophin receptor (p75NTR). J Biol Chem 279:4241-4249.
    • (2004) J Biol Chem , vol.279 , pp. 4241-4249
    • Weskamp, G.1    Schlöndorff, J.2    Lum, L.3    Saftig, P.4    Hartmann, D.5    Becherer, D.6    Murphy, G.7    Blobel, C.P.8
  • 50
    • 0141533033 scopus 로고    scopus 로고
    • ADAMs: Modulators of cell-cell and cell-matrix interactions
    • White JM. 2003. ADAMs: modulators of cell-cell and cell-matrix interactions. Curr Opin Cell Biol 15:598-606.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 598-606
    • White, J.M.1
  • 51
    • 0025284795 scopus 로고
    • Molecular cloning of cDNA encoding MS2 antigen, a novel cell surface antigen strongly expressed in murine monocytic lineage
    • Yoshida S, Setoguchi M, Higuchi Y, Akizuki S, Yamamoto S. 1990. Molecular cloning of cDNA encoding MS2 antigen, a novel cell surface antigen strongly expressed in murine monocytic lineage. Int Immunol 2:586-591.
    • (1990) Int Immunol , vol.2 , pp. 586-591
    • Yoshida, S.1    Setoguchi, M.2    Higuchi, Y.3    Akizuki, S.4    Yamamoto, S.5
  • 52
    • 0031128165 scopus 로고    scopus 로고
    • CD156 (human ADAM8): Expression, primary amino acid sequence, and gene location
    • Yoshiyama K, Higuchi Y, Kataoka M, Matsuura K, Yamamoto S. 1997. CD156 (human ADAM8): expression, primary amino acid sequence, and gene location. Genomics 41:56-62.
    • (1997) Genomics , vol.41 , pp. 56-62
    • Yoshiyama, K.1    Higuchi, Y.2    Kataoka, M.3    Matsuura, K.4    Yamamoto, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.