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Volumn 18, Issue 19, 2009, Pages 3673-3683

Matriptase-2 mutations in iron-refractory iron deficiency anemia patients provide new insights into protease activation mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

MATRIPTASE 2; MEMBRANE PROTEIN; SERINE PROTEINASE;

EID: 70350757743     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddp315     Document Type: Article
Times cited : (61)

References (46)
  • 2
    • 43049128477 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases in development and disease
    • Szabo, R. and Bugge, T.H. (2008) Type II transmembrane serine proteases in development and disease. Int. J. Biochem. Cell Biol., 40, 1297-1316.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1297-1316
    • Szabo, R.1    Bugge, T.H.2
  • 3
    • 0035846933 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes
    • Hooper, J.D., Clements, J.A., Quigley, J.P. and Antalis, T.M. (2001) Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes. J. Biol. Chem., 276, 857-860.
    • (2001) J. Biol. Chem. , vol.276 , pp. 857-860
    • Hooper, J.D.1    Clements, J.A.2    Quigley, J.P.3    Antalis, T.M.4
  • 4
    • 0037688169 scopus 로고    scopus 로고
    • Membrane anchored serine proteases: a rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer
    • Netzel-Arnett, S., Hooper, J.D., Szabo, R., Madison, E.L., Quigley, J.P., Bugge, T.H. and Antalis, T.M. (2003) Membrane anchored serine proteases: a rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer. Cancer Metastasis Rev., 22, 237-258.
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 237-258
    • Netzel-Arnett, S.1    Hooper, J.D.2    Szabo, R.3    Madison, E.L.4    Quigley, J.P.5    Bugge, T.H.6    Antalis, T.M.7
  • 5
    • 45549086117 scopus 로고    scopus 로고
    • Kallikrein-related peptidase 4 (KLK4) initiates intracellular signaling via protease-activated receptors (PARs). KLK4 and PAR-2 are co-expressed during prostate cancer progression
    • Ramsay, A.J., Dong, Y., Hunt, M.L., Linn, M., Samaratunga, H., Clements, J.A. and Hooper, J.D. (2008) Kallikrein-related peptidase 4 (KLK4) initiates intracellular signaling via protease-activated receptors (PARs). KLK4 and PAR-2 are co-expressed during prostate cancer progression. J. Biol. Chem., 283, 12293-12304.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12293-12304
    • Ramsay, A.J.1    Dong, Y.2    Hunt, M.L.3    Linn, M.4    Samaratunga, H.5    Clements, J.A.6    Hooper, J.D.7
  • 6
    • 47549086134 scopus 로고    scopus 로고
    • Prostatic trypsin-like kallikrein-related peptidases (KLKs) and other prostate-expressed tryptic proteinases as regulators of signalling via proteinase-activated receptors (PARs)
    • Ramsay, A.J., Reid, J.C., Adams, M.N., Samaratunga, H., Dong, Y., Clements, J.A. and Hooper, J.D. (2008) Prostatic trypsin-like kallikrein-related peptidases (KLKs) and other prostate-expressed tryptic proteinases as regulators of signalling via proteinase-activated receptors (PARs). Biol. Chem., 389, 653-668.
    • (2008) Biol. Chem. , vol.389 , pp. 653-668
    • Ramsay, A.J.1    Reid, J.C.2    Adams, M.N.3    Samaratunga, H.4    Dong, Y.5    Clements, J.A.6    Hooper, J.D.7
  • 7
    • 0028111631 scopus 로고
    • Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains
    • Kitamoto, Y., Yuan, X., Wu, Q., McCourt, D.W. and Sadler, J.E. (1994) Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains. Proc. Natl Acad. Sci. USA, 91, 7588-7592.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7588-7592
    • Kitamoto, Y.1    Yuan, X.2    Wu, Q.3    McCourt, D.W.4    Sadler, J.E.5
  • 8
    • 14144253541 scopus 로고    scopus 로고
    • Hypertension in mice lacking the proatrial natriuretic peptide convertase corin
    • Chan, J.C., Knudson, O., Wu, F., Morser, J., Dole, W.P. and Wu, Q. (2005) Hypertension in mice lacking the proatrial natriuretic peptide convertase corin. Proc. Natl Acad. Sci. USA, 102, 785-790.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 785-790
    • Chan, J.C.1    Knudson, O.2    Wu, F.3    Morser, J.4    Dole, W.P.5    Wu, Q.6
  • 10
    • 38149089484 scopus 로고    scopus 로고
    • An integrated genetic and functional analysis of the role of type II transmembrane serine proteases (TMPRSSs) in hearing loss
    • Guipponi, M., Toh, M.Y., Tan, J., Park, D., Hanson, K., Ballana, E., Kwong, D., Cannon, P.Z., Wu, Q., Gout, A. et al. (2008) An integrated genetic and functional analysis of the role of type II transmembrane serine proteases (TMPRSSs) in hearing loss. Hum. Mutat., 29, 130-141.
    • (2008) Hum. Mutat. , vol.29 , pp. 130-141
    • Guipponi, M.1    Toh, M.Y.2    Tan, J.3    Park, D.4    Hanson, K.5    Ballana, E.6    Kwong, D.7    Cannon, P.Z.8    Wu, Q.9    Gout, A.10
  • 11
    • 0037020169 scopus 로고    scopus 로고
    • Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins
    • Velasco, G., Cal, S., Quesada, V., Sanchez, L.M. and Lopez-Otin, C. (2002) Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins. J. Biol. Chem., 277, 37637-37646.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37637-37646
    • Velasco, G.1    Cal, S.2    Quesada, V.3    Sanchez, L.M.4    Lopez-Otin, C.5
  • 12
    • 0041567036 scopus 로고    scopus 로고
    • Mouse matriptase-2: identification, characterization and comparative mRNA expression analysis with mouse hepsin in adult and embryonic tissues
    • Hooper, J.D., Campagnolo, L., Goodarzi, G., Truong, T.N., Stuhlmann, H. and Quigley, J.P. (2003) Mouse matriptase-2: identification, characterization and comparative mRNA expression analysis with mouse hepsin in adult and embryonic tissues. Biochem. J., 373, 689-702.
    • (2003) Biochem. J. , vol.373 , pp. 689-702
    • Hooper, J.D.1    Campagnolo, L.2    Goodarzi, G.3    Truong, T.N.4    Stuhlmann, H.5    Quigley, J.P.6
  • 13
    • 38449120396 scopus 로고    scopus 로고
    • The type II transmembrane serine protease matriptase-2-identification, structural features, enzymology, expression pattern and potential roles
    • Ramsay, A.J., Reid, J.C., Velasco, G., Quigley, J.P. and Hooper, J.D. (2008) The type II transmembrane serine protease matriptase-2-identification, structural features, enzymology, expression pattern and potential roles. Front. Biosci., 13, 569-579.
    • (2008) Front. Biosci. , vol.13 , pp. 569-579
    • Ramsay, A.J.1    Reid, J.C.2    Velasco, G.3    Quigley, J.P.4    Hooper, J.D.5
  • 14
    • 56449096622 scopus 로고    scopus 로고
    • The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin
    • Silvestri, L., Pagani, A., Nai, A., De Domenico, I., Kaplan, J. and Camaschella, C. (2008) The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin. Cell Metab., 8, 502-511.
    • (2008) Cell Metab. , vol.8 , pp. 502-511
    • Silvestri, L.1    Pagani, A.2    Nai, A.3    De Domenico, I.4    Kaplan, J.5    Camaschella, C.6
  • 16
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • Nemeth, E., Tuttle, M.S., Powelson, J., Vaughn, M.B., Donovan, A., Ward, D.M., Ganz, T. and Kaplan, J. (2004) Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science, 306, 2090-2093.
    • (2004) Science , vol.306 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.B.4    Donovan, A.5    Ward, D.M.6    Ganz, T.7    Kaplan, J.8
  • 23
    • 33750133047 scopus 로고    scopus 로고
    • Regulation of iron metabolism by hepcidin
    • Nemeth, E. and Ganz, T. (2006) Regulation of iron metabolism by hepcidin. Annu. Rev. Nutr., 26, 323-342.
    • (2006) Annu. Rev. Nutr. , vol.26 , pp. 323-342
    • Nemeth, E.1    Ganz, T.2
  • 25
    • 54349094273 scopus 로고    scopus 로고
    • A mutation in the TMPRSS6 gene, encoding a transmembrane serine protease that suppresses hepcidin production, in familial iron deficiency anemia refractory to oral iron
    • Melis, M.A., Cau, M., Congiu, R., Sole, G., Barella, S., Cao, A., Westerman, M., Cazzola, M. and Galanello, R. (2008) A mutation in the TMPRSS6 gene, encoding a transmembrane serine protease that suppresses hepcidin production, in familial iron deficiency anemia refractory to oral iron. Haematologica, 93, 1473-1479.
    • (2008) Haematologica , vol.93 , pp. 1473-1479
    • Melis, M.A.1    Cau, M.2    Congiu, R.3    Sole, G.4    Barella, S.5    Cao, A.6    Westerman, M.7    Cazzola, M.8    Galanello, R.9
  • 26
    • 52649096861 scopus 로고    scopus 로고
    • Two nonsense mutations in the TMPRSS6 gene in a patient with microcytic anemia and iron deficiency
    • Guillem, F., Lawson, S., Kannengiesser, C., Westerman, M., Beaumont, C. and Grandchamp, B. (2008) Two nonsense mutations in the TMPRSS6 gene in a patient with microcytic anemia and iron deficiency. Blood, 112, 2089-2091.
    • (2008) Blood , vol.112 , pp. 2089-2091
    • Guillem, F.1    Lawson, S.2    Kannengiesser, C.3    Westerman, M.4    Beaumont, C.5    Grandchamp, B.6
  • 27
    • 30044448792 scopus 로고    scopus 로고
    • Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin
    • Macao, B., Johansson, D.G., Hansson, G.C. and Hard, T. (2006) Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin. Nat. Struct. Mol. Biol., 13, 71-76.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 71-76
    • Macao, B.1    Johansson, D.G.2    Hansson, G.C.3    Hard, T.4
  • 28
    • 67049134745 scopus 로고    scopus 로고
    • Molecular mechanisms of the defective hepcidin inhibition in TMPRSS6 mutations associated with iron-refractory iron deficiency anemia
    • Silvestri, L., Guillem, F., Pagani, A., Nai, A., Oudin, C., Silva, M., Toutain, F., Kannengiesser, C., Beaumont, C., Camaschella, C. et al. (2009) Molecular mechanisms of the defective hepcidin inhibition in TMPRSS6 mutations associated with iron-refractory iron deficiency anemia. Blood, 113, 5605-5608.
    • (2009) Blood , vol.113 , pp. 5605-5608
    • Silvestri, L.1    Guillem, F.2    Pagani, A.3    Nai, A.4    Oudin, C.5    Silva, M.6    Toutain, F.7    Kannengiesser, C.8    Beaumont, C.9    Camaschella, C.10
  • 29
    • 0043122919 scopus 로고    scopus 로고
    • SIFT: Predicting amino acid changes that affect protein function
    • Ng, P.C. and Henikoff, S. (2003) SIFT: Predicting amino acid changes that affect protein function. Nucleic Acids Res., 31, 3812-3814.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3812-3814
    • Ng, P.C.1    Henikoff, S.2
  • 31
    • 0027941427 scopus 로고
    • Intravenous iron therapy for severe anaemia in systemic-onset juvenile chronic arthritis
    • Martini, A., Ravelli, A., Di Fuccia, G., Rosti, V., Cazzola, M. and Barosi, G. (1994) Intravenous iron therapy for severe anaemia in systemic-onset juvenile chronic arthritis. Lancet, 344, 1052-1054.
    • (1994) Lancet , vol.344 , pp. 1052-1054
    • Martini, A.1    Ravelli, A.2    Di Fuccia, G.3    Rosti, V.4    Cazzola, M.5    Barosi, G.6
  • 33
    • 0031466897 scopus 로고    scopus 로고
    • Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain
    • Lu, D., Yuan, X., Zheng, X. and Sadler, J.E. (1997) Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain. J. Biol. Chem., 272, 31293-31300.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31293-31300
    • Lu, D.1    Yuan, X.2    Zheng, X.3    Sadler, J.E.4
  • 34
    • 0346732305 scopus 로고    scopus 로고
    • Functional analysis of the transmembrane domain and activation cleavage of human corin: design and characterization of a soluble corin
    • Knappe, S., Wu, F., Masikat, M.R., Morser, J. and Wu, Q. (2003) Functional analysis of the transmembrane domain and activation cleavage of human corin: design and characterization of a soluble corin. J. Biol. Chem., 278, 52363-52370.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52363-52370
    • Knappe, S.1    Wu, F.2    Masikat, M.R.3    Morser, J.4    Wu, Q.5
  • 35
    • 4544273338 scopus 로고    scopus 로고
    • Identification of domain structures in the propeptide of corin essential for the processing of proatrial natriuretic peptide
    • Knappe, S., Wu, F., Madlansacay, M.R. and Wu, Q. (2004) Identification of domain structures in the propeptide of corin essential for the processing of proatrial natriuretic peptide. J. Biol. Chem., 279, 34464-34471.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34464-34471
    • Knappe, S.1    Wu, F.2    Madlansacay, M.R.3    Wu, Q.4
  • 36
    • 0038035877 scopus 로고    scopus 로고
    • The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor
    • Oberst, M.D., Williams, C.A., Dickson, R.B., Johnson, M.D. and Lin, C.Y. (2003) The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor. J. Biol. Chem., 278, 26773-26779.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26773-26779
    • Oberst, M.D.1    Williams, C.A.2    Dickson, R.B.3    Johnson, M.D.4    Lin, C.Y.5
  • 37
    • 0035976996 scopus 로고    scopus 로고
    • N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease
    • Cho, E.G., Kim, M.G., Kim, C., Kim, S.R., Seong, I.S., Chung, C., Schwartz, R.H. and Park, D. (2001) N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease. J. Biol. Chem., 276, 44581-44589.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44581-44589
    • Cho, E.G.1    Kim, M.G.2    Kim, C.3    Kim, S.R.4    Seong, I.S.5    Chung, C.6    Schwartz, R.H.7    Park, D.8
  • 38
    • 27844596295 scopus 로고    scopus 로고
    • Filamin is essential for shedding of the transmembrane serine protease, epithin
    • Kim, C., Cho, Y., Kang, C.H., Kim, M.G., Lee, H., Cho, E.G. and Park, D. (2005) Filamin is essential for shedding of the transmembrane serine protease, epithin. EMBO Rep., 6, 1045-1051.
    • (2005) EMBO Rep. , vol.6 , pp. 1045-1051
    • Kim, C.1    Cho, Y.2    Kang, C.H.3    Kim, M.G.4    Lee, H.5    Cho, E.G.6    Park, D.7
  • 40
    • 46749158788 scopus 로고    scopus 로고
    • Hemojuvelin regulates hepcidin expression via a selective subset of BMP ligands and receptors independently of neogenin
    • Xia, Y., Babitt, J.L., Sidis, Y., Chung, R.T. and Lin, H.Y. (2008) Hemojuvelin regulates hepcidin expression via a selective subset of BMP ligands and receptors independently of neogenin. Blood, 111, 5195-5204.
    • (2008) Blood , vol.111 , pp. 5195-5204
    • Xia, Y.1    Babitt, J.L.2    Sidis, Y.3    Chung, R.T.4    Lin, H.Y.5
  • 41
    • 34447137331 scopus 로고    scopus 로고
    • Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance
    • Babitt, J.L., Huang, F.W., Xia, Y., Sidis, Y., Andrews, N.C. and Lin, H.Y. (2007) Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance. J. Clin. Invest., 117, 1933-1939.
    • (2007) J. Clin. Invest. , vol.117 , pp. 1933-1939
    • Babitt, J.L.1    Huang, F.W.2    Xia, Y.3    Sidis, Y.4    Andrews, N.C.5    Lin, H.Y.6


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