메뉴 건너뛰기




Volumn 287, Issue 52, 2012, Pages 43370-43377

The glaucoma-associated olfactomedin domain of myocilin is a novel calcium binding protein

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC PH; ASPARTATES; CALCIUM BINDING; CALCIUM BINDING PROPERTIES; CALCIUM BINDING PROTEINS; CALCIUM IONS; COFACTORS; DOMAIN STRUCTURE; EXTRACELLULAR MATRIX PROTEIN; EXTRACELLULAR MATRIX TISSUES; HIGH AFFINITY; INTRA OCULAR PRESSURE; MYOCILIN; OLFACTOMEDIN; OPTIC NEUROPATHIES; SECONDARY AND TERTIARY STRUCTURES; TRABECULAR MESHWORKS; WILD TYPES;

EID: 84871564211     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.408906     Document Type: Article
Times cited : (26)

References (54)
  • 2
    • 0030888219 scopus 로고    scopus 로고
    • Structural and functional aspects of calcium binding in extracellular matrix proteins
    • DOI 10.1016/S0945-053X(97)90033-0
    • Maurer, P., and Hohenester, E. (1997) Structural and functional aspects of calcium binding in extracellular matrix proteins. Matrix Biol. 15, 569-580 (Pubitemid 27190032)
    • (1997) Matrix Biology , vol.15 , Issue.8-9 , pp. 569-580
    • Maurer, P.1    Hohenester, E.2
  • 3
    • 84863225073 scopus 로고    scopus 로고
    • Ophthalmic drug discovery: Novel targets and mechanisms for retinal diseases and glaucoma
    • Zhang, K., Zhang, L., and Weinreb, R. N. (2012) Ophthalmic drug discovery: novel targets and mechanisms for retinal diseases and glaucoma. Nat. Rev. Drug Discov. 11, 541-559
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 541-559
    • Zhang, K.1    Zhang, L.2    Weinreb, R.N.3
  • 7
    • 64249159576 scopus 로고    scopus 로고
    • The role of steroids in outflow resistance
    • Clark, A. F., and Wordinger, R. J. (2009) The role of steroids in outflow resistance. Exp. Eye Res. 88, 752-759
    • (2009) Exp. Eye Res. , vol.88 , pp. 752-759
    • Clark, A.F.1    Wordinger, R.J.2
  • 8
    • 64249133288 scopus 로고    scopus 로고
    • Glaucoma-associated myocilin: A better understanding but much more to learn
    • Resch, Z. T., and Fautsch, M. P. (2009) Glaucoma-associated myocilin: a better understanding but much more to learn. Exp. Eye Res. 88, 704-712
    • (2009) Exp. Eye Res. , vol.88 , pp. 704-712
    • Resch, Z.T.1    Fautsch, M.P.2
  • 9
    • 79959806015 scopus 로고    scopus 로고
    • The stability of myocilin olfactomedin domain variants provides new insight into glaucoma as a protein misfolding disorder
    • Burns, J. N., Turnage, K. C., Walker, C. A., and Lieberman, R. L. (2011) The stability of myocilin olfactomedin domain variants provides new insight into glaucoma as a protein misfolding disorder. Biochemistry 50, 5824-5833
    • (2011) Biochemistry , vol.50 , pp. 5824-5833
    • Burns, J.N.1    Turnage, K.C.2    Walker, C.A.3    Lieberman, R.L.4
  • 11
    • 0034842533 scopus 로고    scopus 로고
    • Characterization of myocilinmyocilin interactions
    • Fautsch, M. P., and Johnson, D. H. (2001) Characterization of myocilinmyocilin interactions. Invest. Ophthalmol. Vis. Sci. 42, 2324-2331
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 2324-2331
    • Fautsch, M.P.1    Johnson, D.H.2
  • 12
    • 33646165968 scopus 로고    scopus 로고
    • The identification of myocilin-associated proteins in the human trabecular meshwork
    • Fautsch, M. P., Vrabel, A. M., and Johnson, D. H. (2006) The identification of myocilin-associated proteins in the human trabecular meshwork. Exp. Eye Res. 82, 1046-1052
    • (2006) Exp. Eye Res. , vol.82 , pp. 1046-1052
    • Fautsch, M.P.1    Vrabel, A.M.2    Johnson, D.H.3
  • 13
    • 58149328927 scopus 로고    scopus 로고
    • Myocilin promotes substrate adhesion, spreading and formation of focal contacts in podocytes and mesangial cells
    • Goldwich, A., Scholz, M., and Tamm, E. R. (2009) Myocilin promotes substrate adhesion, spreading and formation of focal contacts in podocytes and mesangial cells. Histochem. Cell Biol. 131, 167-180
    • (2009) Histochem. Cell Biol. , vol.131 , pp. 167-180
    • Goldwich, A.1    Scholz, M.2    Tamm, E.R.3
  • 14
    • 12344256073 scopus 로고    scopus 로고
    • Myocilin binding to Hep II domain of fibronectin inhibits cell spreading and incorporation of paxillin into focal adhesions
    • DOI 10.1016/j.yexcr.2004.09.026, PII S0014482704005762
    • Peters, D. M., Herbert, K., Biddick, B., and Peterson, J. A. (2005) Myocilin binding to Hep II domain of fibronectin inhibits cell spreading and incorporation of paxillin into focal adhesions. Exp. Cell Res. 303, 218-228 (Pubitemid 40126257)
    • (2005) Experimental Cell Research , vol.303 , Issue.2 , pp. 218-228
    • Peters, D.M.1    Herbert, K.2    Biddick, B.3    Peterson, J.A.4
  • 16
    • 73049100386 scopus 로고    scopus 로고
    • Olfactomedin domain-containing proteins: Possible mechanisms of action and functions in normal development and pathology
    • Tomarev, S. I., and Nakaya, N. (2009) Olfactomedin domain-containing proteins: possible mechanisms of action and functions in normal development and pathology. Mol. Neurobiol. 40, 122-138
    • (2009) Mol. Neurobiol. , vol.40 , pp. 122-138
    • Tomarev, S.I.1    Nakaya, N.2
  • 17
    • 35948954725 scopus 로고    scopus 로고
    • Structural features and functional domains of amassin-1, a cell-binding olfactomedin protein
    • DOI 10.1139/O07-055
    • Hillier, B. J., and Vacquier, V. D. (2007) Structural features and functional domains of amassin-1, a cell-binding olfactomedin protein. Biochem. Cell Biol. 85, 552-562 (Pubitemid 350073441)
    • (2007) Biochemistry and Cell Biology , vol.85 , Issue.5 , pp. 552-562
    • Hillier, B.J.1    Vacquier, V.D.2
  • 18
    • 82755171872 scopus 로고    scopus 로고
    • Fibronectin type III-like domains of neurofascin-186 protein mediate gliomedin binding and its clustering at the developing nodes of Ranvier
    • Labasque, M., Devaux, J. J., Lévêque, C., and Faivre-Sarrailh, C. (2011) Fibronectin type III-like domains of neurofascin-186 protein mediate gliomedin binding and its clustering at the developing nodes of Ranvier. J. Biol. Chem. 286, 42426-42434
    • (2011) J. Biol. Chem. , vol.286 , pp. 42426-42434
    • Labasque, M.1    Devaux, J.J.2    Lévêque, C.3    Faivre-Sarrailh, C.4
  • 19
    • 79961103406 scopus 로고    scopus 로고
    • Olfactomedin 4, a novel marker for the differentiation and progression of gastrointestinal cancers
    • Yu, L., Wang, L., and Chen, S. (2011) Olfactomedin 4, a novel marker for the differentiation and progression of gastrointestinal cancers. Neoplasma 58, 9-13
    • (2011) Neoplasma , vol.58 , pp. 9-13
    • Yu, L.1    Wang, L.2    Chen, S.3
  • 20
    • 33846661209 scopus 로고    scopus 로고
    • Olfactomedin 4 promotes S-phase transition in proliferation of pancreatic cancer cells
    • DOI 10.1111/j.1349-7006.2007.00397.x
    • Kobayashi, D., Koshida, S., Moriai, R., Tsuji, N., and Watanabe, N. (2007) Olfactomedin 4 promotes S-phase transition in proliferation of pancreatic cancer cells. Cancer Sci. 98, 334-340 (Pubitemid 46195603)
    • (2007) Cancer Science , vol.98 , Issue.3 , pp. 334-340
    • Kobayashi, D.1    Koshida, S.2    Moriai, R.3    Tsuji, N.4    Watanabe, N.5
  • 21
    • 84859170707 scopus 로고    scopus 로고
    • Depletion of OLFM4 gene inhibits cell growth and increases sensitization to hydrogen peroxide and tumor necrosis factor-α induced apoptosis in gastric cancer cells
    • Liu, R. H., Yang, M. H., Xiang, H., Bao, L. M., Yang, H. A., Yue, L. W., Jiang, X., Ang, N., Wu, L. Y., and Huang, Y. (2012) Depletion of OLFM4 gene inhibits cell growth and increases sensitization to hydrogen peroxide and tumor necrosis factor-α induced apoptosis in gastric cancer cells. J. Biomed. Sci. 19, 38
    • (2012) J. Biomed. Sci. , vol.19 , pp. 38
    • Liu, R.H.1    Yang, M.H.2    Xiang, H.3    Bao, L.M.4    Yang, H.A.5    Yue, L.W.6    Jiang, X.7    Ang, N.8    Wu, L.Y.9    Huang, Y.10
  • 24
    • 0023894794 scopus 로고
    • The calcium and magnesium content of the human lens and aqueous humor. A study in patients with hypocalcemic and senile cataract
    • Ringvold, A., Sagen, E., Bjerve, K. S., and Folling, I. (1988) The calcium and magnesium content of the human lens and aqueous humor. A study in patients with hypocalcemic and senile cataract. Acta Ophthalmol. (Copenh). 66, 153-156
    • (1988) Acta Ophthalmol. (Copenh) , vol.66 , pp. 153-156
    • Ringvold, A.1    Sagen, E.2    Bjerve, K.S.3    Folling, I.4
  • 27
    • 79551529083 scopus 로고    scopus 로고
    • Biophysical characterization of the olfactomedin domain of myocilin, an extracellular matrix protein implicated in inherited forms of glaucoma
    • Orwig, S. D., and Lieberman, R. L. (2011) Biophysical characterization of the olfactomedin domain of myocilin, an extracellular matrix protein implicated in inherited forms of glaucoma. PLoS One 6, e16347
    • (2011) PLoS One , vol.6
    • Orwig, S.D.1    Lieberman, R.L.2
  • 28
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • DOI 10.1038/nprot.2007.321, PII NPROT.2007.321
    • Niesen, F. H., Berglund, H., and Vedadi, M. (2007) The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat. Protoc. 2, 2212-2221 (Pubitemid 351565860)
    • (2007) Nature Protocols , vol.2 , Issue.9 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 29
    • 0021941781 scopus 로고
    • 2+-protein complexes
    • 2+-protein complexes. Biochem. J. 226, 613-616
    • (1985) Biochem. J. , vol.226 , pp. 613-616
    • Bryant, D.T.1
  • 30
    • 34248532415 scopus 로고    scopus 로고
    • PROMALS: Towards accurate multiple sequence alignments of distantly related proteins
    • DOI 10.1093/bioinformatics/btm017
    • Pei, J., and Grishin, N. V. (2007) PROMALS: towards accurate multiple sequence alignments of distantly related proteins. Bioinformatics 23, 802-808 (Pubitemid 47049913)
    • (2007) Bioinformatics , vol.23 , Issue.7 , pp. 802-808
    • Pei, J.1    Grishin, N.V.2
  • 31
    • 33846622066 scopus 로고    scopus 로고
    • Ligand effects on protein thermodynamic stability
    • Sanchez-Ruiz, J. M. (2007) Ligand effects on protein thermodynamic stability. Biophys. Chem. 126, 43-49
    • (2007) Biophys. Chem. , vol.126 , pp. 43-49
    • Sanchez-Ruiz, J.M.1
  • 32
    • 84886640673 scopus 로고
    • A stopped-flow investigation of calcium ion binding by ethylene glycol bis(β-aminoethyl ether)-N,N'-tetraacetic acid
    • DOI 10.1016/0003-2697(84)90575-X
    • Smith, P. D., Liesegang, G. W., Berger, R. L., Czerlinski, G., and Podolsky, R. J. (1984) A stopped-flow investigation of calcium ion binding by ethylene glycol bis(β-aminoethyl ether)-N,N -tetraacetic acid. Anal. Biochem. 143, 188-195 (Pubitemid 15157553)
    • (1984) Analytical Biochemistry , vol.143 , Issue.1 , pp. 188-195
    • Smith, P.D.1    Liesegang, G.W.2    Berger, R.L.3
  • 33
    • 0034856791 scopus 로고    scopus 로고
    • Structural characteristics of protein binding sites for calcium and lanthanide ions
    • DOI 10.1007/s007750100214
    • Pidcock, E., and Moore, G. R. (2001) Structural characteristics of protein binding sites for calcium and lanthanide ions. J. Biol. Inorg. Chem. 6, 479-489 (Pubitemid 32822109)
    • (2001) Journal of Biological Inorganic Chemistry , vol.6 , Issue.5-6 , pp. 479-489
    • Pidcock, E.1    Moore, G.R.2
  • 34
    • 0019005874 scopus 로고
    • Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism
    • Brahms, S., and Brahms, J. (1980) Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138, 149-178
    • (1980) J. Mol. Biol. , vol.138 , pp. 149-178
    • Brahms, S.1    Brahms, J.2
  • 35
    • 0015244842 scopus 로고
    • Active site spin-labeled -chymotrypsin. Guanidine hydrochloride denaturation studies using electron paramagnetic resonance and circular dichroism
    • Morrisett, J. D., and Broomfield, C. A. (1971) Active site spin-labeled -chymotrypsin. Guanidine hydrochloride denaturation studies using electron paramagnetic resonance and circular dichroism. J. Am. Chem. Soc. 93, 7297-7304
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 7297-7304
    • Morrisett, J.D.1    Broomfield, C.A.2
  • 36
    • 5144226338 scopus 로고    scopus 로고
    • The DxDxDG motif for calcium binding: Multiple structural contexts and implications for evolution
    • DOI 10.1016/j.jmb.2004.08.077, PII S0022283604010770
    • Rigden, D. J., and Galperin, M. Y. (2004) The DxDxDG motif for calcium binding: multiple structural contexts and implications for evolution. J. Mol. Biol. 343, 971-984 (Pubitemid 39345957)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.4 , pp. 971-984
    • Rigden, D.J.1    Galperin, M.Y.2
  • 37
    • 79959603758 scopus 로고    scopus 로고
    • New structural and functional contexts of the Dx(DN)xDG linear motif: Insights into evolution of calcium-binding proteins
    • Rigden, D. J., Woodhead, D. D., Wong, P. W., and Galperin, M. Y. (2011) New structural and functional contexts of the Dx(DN)xDG linear motif: insights into evolution of calcium-binding proteins. PLoS One 6, e21507
    • (2011) PLoS One , vol.6
    • Rigden, D.J.1    Woodhead, D.D.2    Wong, P.W.3    Galperin, M.Y.4
  • 38
    • 0025908111 scopus 로고
    • Key residues involved in calcium-binding motifs in EGF-like domains
    • Handford, P. A., Mayhew, M., Baron, M., Winship, P. R., Campbell, I. D., and Brownlee, G. G. (1991) Key residues involved in calcium-binding motifs in EGF-like domains. Nature 351, 164-167 (Pubitemid 21896559)
    • (1991) Nature , vol.351 , Issue.6322 , pp. 164-167
    • Handford, P.A.1    Mayhew, M.2    Baron, M.3    Winship, P.R.4    Campbell, I.D.5    Brownlee, G.G.6
  • 39
    • 84856489442 scopus 로고    scopus 로고
    • HHblits: Light-ning- Fast iterative protein sequence searching by HMM-HMM alignment
    • Remmert, M., Biegert, A., Hauser, A., and Söding, J. (2012) HHblits: light-ning- fast iterative protein sequence searching by HMM-HMM alignment. Nat. Methods 9, 173-175
    • (2012) Nat. Methods , vol.9 , pp. 173-175
    • Remmert, M.1    Biegert, A.2    Hauser, A.3    Söding, J.4
  • 40
    • 79960078022 scopus 로고    scopus 로고
    • Incorporation of evolutionary information into Rosetta comparative modeling
    • Thompson, J., and Baker, D. (2011) Incorporation of evolutionary information into Rosetta comparative modeling. Proteins 79, 2380-2388
    • (2011) Proteins , vol.79 , pp. 2380-2388
    • Thompson, J.1    Baker, D.2
  • 41
    • 0035914434 scopus 로고    scopus 로고
    • Calcium binding properties of γ-crystallin: Calcium ion binds at the Greek key β γ-crystallin fold
    • Rajini, B., Shridas, P., Sundari, C. S., Muralidhar, D., Chandani, S., Thomas, F., and Sharma, Y. (2001) Calcium binding properties of γ-crystallin: calcium ion binds at the Greek key β γ-crystallin fold. J. Biol. Chem. 276, 38464-38471
    • (2001) J. Biol. Chem. , vol.276 , pp. 38464-38471
    • Rajini, B.1    Shridas, P.2    Sundari, C.S.3    Muralidhar, D.4    Chandani, S.5    Thomas, F.6    Sharma, Y.7
  • 42
  • 44
    • 0034459679 scopus 로고    scopus 로고
    • Evolutionary trace analysis of TGF-β and related growth factors: Implications for site-directed mutagenesis
    • Innis, C. A., Shi, J., and Blundell, T. L. (2000) Evolutionary trace analysis of TGF-β and related growth factors: implications for site-directed mutagenesis. Protein Eng. 13, 839-847 (Pubitemid 32233943)
    • (2000) Protein Engineering , vol.13 , Issue.12 , pp. 839-847
    • Innis, C.A.1    Shi, J.2    Blundell, T.L.3
  • 45
    • 0037366128 scopus 로고    scopus 로고
    • Principles governing Mg, Ca, and Zn binding and selectivity in proteins
    • Dudev, T., and Lim, C. (2003) Principles governing Mg, Ca, and Zn binding and selectivity in proteins. Chem. Rev. 103, 773-788
    • (2003) Chem. Rev. , vol.103 , pp. 773-788
    • Dudev, T.1    Lim, C.2
  • 46
    • 0028839859 scopus 로고
    • The C-terminal portion of BM-40 (SPARC/osteonectin) is an autonomously folding and crystallisable domain that binds calcium and collagen IV
    • Maurer, P., Hohenadl, C., Hohenester, E., Göhring, W., Timpl, R., and Engel, J. (1995) The C-terminal portion of BM-40 (SPARC/osteonectin) is an autonomously folding and crystallisable domain that binds calcium and collagen IV. J. Mol. Biol. 253, 347-357
    • (1995) J. Mol. Biol. , vol.253 , pp. 347-357
    • Maurer, P.1    Hohenadl, C.2    Hohenester, E.3    Göhring, W.4    Timpl, R.5    Engel, J.6
  • 48
    • 25644458267 scopus 로고    scopus 로고
    • Identification of flotillin-1 as a protein interacting with myocilin: Implications for the pathogenesis of primary open-angle glaucoma
    • DOI 10.1016/j.bbrc.2005.09.006, PII S0006291X05020000
    • Joe, M. K., Sohn, S., Choi, Y. R., Park, H., and Kee, C. (2005) Identification of flotillin-1 as a protein interacting with myocilin: implications for the pathogenesis of primary open-angle glaucoma. Biochem. Biophys. Res. Commun. 336, 1201-1206 (Pubitemid 41383449)
    • (2005) Biochemical and Biophysical Research Communications , vol.336 , Issue.4 , pp. 1201-1206
    • Myung, K.J.1    Sohn, S.2    Young, R.C.3    Park, H.4    Kee, C.5
  • 49
    • 0037450790 scopus 로고    scopus 로고
    • Amassin, an olfactomedin protein, mediates the massive intercellular adhesion of sea urchin coelomocytes
    • DOI 10.1083/jcb.200210053
    • Hillier, B. J., and Vacquier, V. D. (2003) Amassin, an olfactomedin protein, mediates the massive intercellular adhesion of sea urchin coelomocytes. J. Cell Biol. 160, 597-604 (Pubitemid 36254397)
    • (2003) Journal of Cell Biology , vol.160 , Issue.4 , pp. 597-604
    • Hillier, B.J.1    Vacquier, V.D.2
  • 50
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham, D. E. (2007) Calcium signaling. Cell 131, 1047-1058
    • (2007) Cell , vol.131 , pp. 1047-1058
    • Clapham, D.E.1
  • 53
    • 64449084801 scopus 로고    scopus 로고
    • Evidence for a calcification process in the trabecular meshwork
    • Borrás, T., and Comes, N. (2009) Evidence for a calcification process in the trabecular meshwork. Exp. Eye Res. 88, 738-746
    • (2009) Exp. Eye Res. , vol.88 , pp. 738-746
    • Borrás, T.1    Comes, N.2
  • 54
    • 84866149001 scopus 로고    scopus 로고
    • Cystatin a, a potential common link for mutant myocilin causative glaucoma
    • Kennedy, K. D., AnithaChristy, S. A., Buie, L. K., and Borrás, T. (2012) Cystatin a, a potential common link for mutant myocilin causative glaucoma. PLoS One 7, e36301
    • (2012) PLoS One , vol.7
    • Kennedy, K.D.1    AnithaChristy, S.A.2    Buie, L.K.3    Borrás, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.