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Volumn 287, Issue 19, 2012, Pages 15776-15785

Novel basic protein, PfN23, functions as key macromolecule during nacre formation

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC PROTEINS; ARAGONITE CRYSTALS; C-TERMINAL REGIONS; CALCIUM CARBONATE CRYSTALS; CALCIUM CARBONATE DEPOSITION; DOUBLE-STRANDED RNA; EXPRESSION PROFILE; FINE MICROSTRUCTURE; IMMUNODETECTION; IMMUNOSTAINING; IN-SITU; IN-VITRO; LARVAL DEVELOPMENT; POSITIVELY CHARGED;

EID: 84860847067     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.341594     Document Type: Article
Times cited : (54)

References (46)
  • 2
    • 61349098891 scopus 로고    scopus 로고
    • Unveiling the formation mechanism of pseudo-single crystal aragonite platelets in nacre
    • Li, X., and Huang, Z. (2009) Unveiling the formation mechanism of pseudo-single crystal aragonite platelets in nacre. Physical. Rev. Lett. 102, 75502
    • (2009) Physical. Rev. Lett. , vol.102 , pp. 75502
    • Li, X.1    Huang, Z.2
  • 3
    • 0030707506 scopus 로고    scopus 로고
    • Biomineralization. A pavement of pearl
    • Addadi, L., and Weiner, S. (1997) Biomineralization. A pavement of pearl. Nature 389, 912-915
    • (1997) Nature , vol.389 , pp. 912-915
    • Addadi, L.1    Weiner, S.2
  • 4
    • 0021533058 scopus 로고
    • Macromolecules in mollusc shells and their functions in biomineralization
    • Weiner, S., and Traub, W. (1984) Macromolecules in mollusc shells and their functions in biomineralization. Philos. Trans. R. Soc. Lond. B Biol. Sci. 304, 425-434
    • (1984) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.304 , pp. 425-434
    • Weiner, S.1    Traub, W.2
  • 5
    • 0017670579 scopus 로고
    • Biomineralization and detoxification
    • Simkiss, K. (1977) Biomineralization and detoxification. Calcif. Tissue Res. 24, 199-200
    • (1977) Calcif. Tissue Res. , vol.24 , pp. 199-200
    • Simkiss, K.1
  • 6
    • 0018662350 scopus 로고
    • Mineralization, paleooceanography, and the evolution of calcareous marine organisms
    • Wilkinson, B. H. (1979) Mineralization, paleooceanography, and the evolution of calcareous marine organisms. Geology 7, 524-527
    • (1979) Geology , vol.7 , pp. 524-527
    • Wilkinson, B.H.1
  • 7
    • 0016861434 scopus 로고
    • Vaterite. A mineralization product of the hard tissues of a marine organism (Ascidiacea)
    • Lowenstam, H. A., and Abbott, D. P. (1975) Vaterite. A mineralization product of the hard tissues of a marine organism (Ascidiacea). Science 188, 363-365
    • (1975) Science , vol.188 , pp. 363-365
    • Lowenstam, H.A.1    Abbott, D.P.2
  • 13
    • 79960148742 scopus 로고    scopus 로고
    • Crystallization pathways in biomineralization
    • Weiner, S., and Addadi, L. (2011) Crystallization pathways in biomineralization. Annu. Rev. Materials Res. 41, 21-40
    • (2011) Annu. Rev. Materials Res. , vol.41 , pp. 21-40
    • Weiner, S.1    Addadi, L.2
  • 14
    • 0029669273 scopus 로고    scopus 로고
    • Control of crystal phase switching and orientation by soluble mollusk-shell proteins
    • Belcher, A. M., Wu, X. H., Christensen, R. J., Hansma, P. K., Stucky, G. D., and Morse, D. E. (1996) Control of crystal phase switching and orientation by soluble mollusk-shell proteins. Nature 381, 56-58
    • (1996) Nature , vol.381 , pp. 56-58
    • Belcher, A.M.1    Wu, X.H.2    Christensen, R.J.3    Hansma, P.K.4    Stucky, G.D.5    Morse, D.E.6
  • 15
    • 0030020380 scopus 로고    scopus 로고
    • Matrix proteins with high affinity for calcium ions are associated with mineralization within the elastic fibers of pseudoxanthoma elasticum dermis
    • Contri, M. B., Boraldi, F., Taparelli, F., De Paepe, A., and Ronchetti, I. P. (1996) Matrix proteins with high affinity for calcium ions are associated with mineralization within the elastic fibers of pseudoxanthoma elasticum dermis. Am. J. Pathol. 148, 569-577 (Pubitemid 26056741)
    • (1996) American Journal of Pathology , vol.148 , Issue.2 , pp. 569-577
    • Contri, M.B.1    Boraldi, F.2    Taparelli, F.3    De Paepe, A.4    Ronchetti, I.P.5
  • 18
    • 0031452642 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Lustrin A, a matrix protein from shell and pearl nacre of Haliotis rufescens
    • DOI 10.1074/jbc.272.51.32472
    • Shen, X., Belcher, A. M., Hansma, P. K., Stucky, G. D., and Morse, D. E. (1997) Molecular cloning and characterization of lustrin A, a matrix protein from shell and pearl nacre of Haliotis rufescens. J. Biol. Chem. 272, 32472-32481 (Pubitemid 28011932)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.51 , pp. 32472-32481
    • Shen, X.1    Belcher, A.M.2    Hansma, P.K.3    Stucky, G.D.4    Morse, D.E.5
  • 19
    • 0032712041 scopus 로고    scopus 로고
    • A new matrix protein family related to the nacreous layer formation of Pinctada fucata
    • Samata, T., Hayashi, N., Kono, M., Hasegawa, K., Horita, C., and Akera, S. (1999) A new matrix protein family related to the nacreous layer formation of Pinctada fucata. FEBS Lett. 462, 225-229
    • (1999) FEBS Lett. , vol.462 , pp. 225-229
    • Samata, T.1    Hayashi, N.2    Kono, M.3    Hasegawa, K.4    Horita, C.5    Akera, S.6
  • 20
    • 4344712499 scopus 로고    scopus 로고
    • Characterization of Prismalin-14, a novel matrix protein from the prismatic layer of the Japanese pearl oyster (Pinctada fucata)
    • DOI 10.1042/BJ20040319
    • Suzuki, M., Murayama, E., Inoue, H., Ozaki, N., Tohse, H., Kogure, T., and Nagasawa, H. (2004) Characterization of Prismalin-14, a novel matrix protein from the prismatic layer of the Japanese pearl oyster (Pinctada fucata). Biochem. J. 382, 205-213 (Pubitemid 39141583)
    • (2004) Biochemical Journal , vol.382 , Issue.1 , pp. 205-213
    • Suzuki, M.1    Murayama, E.2    Inoue, H.3    Ozaki, N.4    Tohse, H.5    Kogure, T.6    Nagasawa, H.7
  • 21
    • 33646501557 scopus 로고    scopus 로고
    • Shematrin.A family of glycine-rich structural proteins in the shell of the pearl oyster Pinctada fucata
    • Yano, M., Nagai, K., Morimoto, K., and Miyamoto, H. (2006) Shematrin.A family of glycine-rich structural proteins in the shell of the pearl oyster Pinctada fucata. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 144, 254-262
    • (2006) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.144 , pp. 254-262
    • Yano, M.1    Nagai, K.2    Morimoto, K.3    Miyamoto, H.4
  • 24
    • 67449106984 scopus 로고    scopus 로고
    • Cloning and characterization of Prisilkin-39, a novel matrix protein serving a dual role in the prismatic layer formation from the oyster Pinctada fucata
    • Kong, Y., Jing, G., Yan, Z., Li, C., Gong, N., Zhu, F., Li, D., Zhang, Y., Zheng, G., Wang, H., Xie, L., and Zhang, R. (2009) Cloning and characterization of Prisilkin-39, a novel matrix protein serving a dual role in the prismatic layer formation from the oyster Pinctada fucata. J. Biol. Chem. 284, 10841-10854
    • (2009) J. Biol. Chem. , vol.284 , pp. 10841-10854
    • Kong, Y.1    Jing, G.2    Yan, Z.3    Li, C.4    Gong, N.5    Zhu, F.6    Li, D.7    Zhang, Y.8    Zheng, G.9    Wang, H.10    Xie, L.11    Zhang, R.12
  • 26
    • 0037560726 scopus 로고    scopus 로고
    • Mollusk shell acidic proteins: In search of individual functions
    • DOI 10.1002/cbic.200200548
    • Gotliv, B. A., Addadi, L., and Weiner, S. (2003) Mollusk shell acidic proteins. In search of individual functions. ChemBioChem 4, 522-529 (Pubitemid 36749623)
    • (2003) ChemBioChem , vol.4 , Issue.6 , pp. 522-529
    • Gotliv, B.-A.1    Addadi, L.2    Weiner, S.3
  • 27
    • 34548224707 scopus 로고    scopus 로고
    • Perlinhibin, a cysteine-, histidine-, and arginine-rich miniprotein from abalone (Haliotis laevigata) nacre, inhibits in vitro calcium carbonate crystallization
    • DOI 10.1529/biophysj.106.100636
    • Mann, K., Siedler, F., Treccani, L., Heinemann, F., and Fritz, M. (2007) Perlinhibin, a cysteine-, histidine-, and arginine-rich miniprotein from abalone (Haliotis laevigata) nacre, inhibits in vitro calcium carbonate crystallization. Biophys. J. 93, 1246-1254 (Pubitemid 47330904)
    • (2007) Biophysical Journal , vol.93 , Issue.4 , pp. 1246-1254
    • Mann, K.1    Siedler, F.2    Treccani, L.3    Heinemann, F.4    Fritz, M.5
  • 28
    • 0035782670 scopus 로고    scopus 로고
    • Structure of the nacreous organic matrix of a bivalve mollusk shell examined in the hydrated state using cryo-TEM
    • Levi-Kalisman, Y., Falini, G., Addadi, L., and Weiner, S. (2001) Structure of the nacreous organic matrix of a bivalve mollusk shell examined in the hydrated state using cryo-TEM. J. Struct. Biol. 135, 8-17
    • (2001) J. Struct. Biol. , vol.135 , pp. 8-17
    • Levi-Kalisman, Y.1    Falini, G.2    Addadi, L.3    Weiner, S.4
  • 29
    • 0036784203 scopus 로고    scopus 로고
    • Mollusc larval shell formation: Amorphous calcium carbonate is a precursor phase for aragonite
    • DOI 10.1002/jez.90004
    • Weiss, I. M., Tuross, N., Addadi, L., and Weiner, S. (2002) Mollusc larval shell formation. Amorphous calcium carbonate is a precursor phase for aragonite. J. Exp. Zool. 293, 478-491 (Pubitemid 35036587)
    • (2002) Journal of Experimental Zoology , vol.293 , Issue.5 , pp. 478-491
    • Weiss, I.M.1    Tuross, N.2    Addadi, L.3    Weiner, S.4
  • 30
    • 31344456451 scopus 로고    scopus 로고
    • Mollusk shell formation. A source of new concepts for understanding biomineralization processes
    • Addadi, L., Joester, D., Nudelman, F., and Weiner, S. (2006) Mollusk shell formation. A source of new concepts for understanding biomineralization processes. CHEM-EUR. J. 12, 981-987
    • (2006) CHEM-EUR. J. , vol.12 , pp. 981-987
    • Addadi, L.1    Joester, D.2    Nudelman, F.3    Weiner, S.4
  • 31
    • 33749436106 scopus 로고    scopus 로고
    • Perlwapin, an abalone nacre protein with three four-disulfide core (whey acidic protein) domains, inhibits the growth of calcium carbonate crystals
    • DOI 10.1529/biophysj.106.086108
    • Treccani, L., Mann, K., Heinemann, F., and Fritz, M. (2006) Perlwapin, an abalone nacre protein with three four-disulfide core (whey acidic protein) domains, inhibits the growth of calcium carbonate crystals. Biophys. J. 91, 2601-2608 (Pubitemid 44511713)
    • (2006) Biophysical Journal , vol.91 , Issue.7 , pp. 2601-2608
    • Treccani, L.1    Mann, K.2    Heinemann, F.3    Fritz, M.4
  • 32
    • 0034614599 scopus 로고    scopus 로고
    • Purification and characterization of perlucin and perlustrin, two new proteins from the shell of the mollusc Haliotis laevigata
    • DOI 10.1006/bbrc.1999.1907
    • Weiss, I. M., Kaufmann, S., Mann, K., and Fritz, M. (2000) Purification and characterization of perlucin and perlustrin, two new proteins from the shell of the mollusc Haliotis laevigata. Biochem. Biophys. Res. Commun. 267, 17-21 (Pubitemid 30072500)
    • (2000) Biochemical and Biophysical Research Communications , vol.267 , Issue.1 , pp. 17-21
    • Weiss, I.M.1    Kaufmann, S.2    Mann, K.3    Fritz, M.4
  • 33
    • 79959806595 scopus 로고    scopus 로고
    • Identification of genes directly involved in shell formation and their functions in pearl oyster, Pinctada fucata
    • Fang, D., Xu, G. R., Hu, Y. L., Pan, C., Xie, L. P., and Zhang, R. Q. (2011) Identification of genes directly involved in shell formation and their functions in pearl oyster, Pinctada fucata. PLoS One 6, e21860
    • (2011) PLoS One , vol.6
    • Fang, D.1    Xu, G.R.2    Hu, Y.L.3    Pan, C.4    Xie, L.P.5    Zhang, R.Q.6
  • 34
    • 35348886006 scopus 로고    scopus 로고
    • Molluscan shell proteins. Primary structure, origin, and evolution
    • Marin, F., Luquet, G., Marie, B., and Medakovic, D. (2008) Molluscan shell proteins. Primary structure, origin, and evolution. Curr. Top. Dev. Biol. 80, 209-276
    • (2008) Curr. Top. Dev. Biol. , vol.80 , pp. 209-276
    • Marin, F.1    Luquet, G.2    Marie, B.3    Medakovic, D.4
  • 35
    • 33846609627 scopus 로고
    • Development and morphology of the pearl oyster larvae, Pinctada fucata
    • Fujimura, T., Wada, K., and Iwaki, T. (1995) Development and morphology of the pearl oyster larvae, Pinctada fucata. Venus Jpn. J. Malacol. 54, 25-48
    • (1995) Venus Jpn. J. Malacol. , vol.54 , pp. 25-48
    • Fujimura, T.1    Wada, K.2    Iwaki, T.3
  • 36
    • 2442535077 scopus 로고    scopus 로고
    • A novel calcium-binding peptide from the cuticle of the crayfish, Procambarus clarkii
    • DOI 10.1016/j.bbrc.2004.04.075, PII S0006291X04008083
    • Inoue, H., Ohira, T., Ozaki, N., and Nagasawa, H. (2004) A novel calcium-binding peptide from the cuticle of the crayfish, Procambarus clarkii. Biochem. Biophys. Res. Commun. 318, 649-654 (Pubitemid 38624203)
    • (2004) Biochemical and Biophysical Research Communications , vol.318 , Issue.3 , pp. 649-654
    • Inoue, H.1    Ohira, T.2    Ozaki, N.3    Nagasawa, H.4
  • 38
    • 34548187477 scopus 로고    scopus 로고
    • A novel extrapallial fluid protein controls the morphology of nacre lamellae in the pearl oyster, Pinctada fucata
    • DOI 10.1074/jbc.M700001200
    • Ma, Z., Huang, J., Sun, J., Wang, G., Li, C., Xie, L., and Zhang, R. (2007) A novel extrapallial fluid protein controls the morphology of nacre lamellae in the pearl oyster, Pinctada fucata. J. Biol. Chem. 282, 23253-23263 (Pubitemid 47311939)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.32 , pp. 23253-23263
    • Ma, Z.1    Huang, J.2    Sun, J.3    Wang, G.4    Li, C.5    Xie, L.6    Zhang, R.7
  • 39
    • 0032567216 scopus 로고    scopus 로고
    • Biomimetic synthesis of macroscopic-scale calcium carbonate thin films. Evidence for a multistep assembly process
    • DOI 10.1021/ja9819108
    • Xu, G. F., Yao, N., Aksay, I. A., and Groves, J. T. (1998) Biomimetic synthesis of macroscopic scale calcium carbonate thin films. Evidence for a multistep process. J. Am. Chem. Soc. 120, 11977-11985 (Pubitemid 29012867)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.46 , pp. 11977-11985
    • Xu, G.1    Yao, N.2    Aksay, I.A.3    Groves, J.T.4
  • 40
    • 84903381547 scopus 로고
    • Molluscan shell matrix phosphoproteins. Correlation of degree of phosphorylation to shell mineral microstructure and to in vitro regulation of mineralization
    • Borbas, J. E., Wheeler, A. P., and Sikes, C. S. (1991) Molluscan shell matrix phosphoproteins. Correlation of degree of phosphorylation to shell mineral microstructure and to in vitro regulation of mineralization. J. Exp. Zool. 258, 1-13
    • (1991) J. Exp. Zool. , vol.258 , pp. 1-13
    • Borbas, J.E.1    Wheeler, A.P.2    Sikes, C.S.3
  • 41
    • 0019392575 scopus 로고
    • Minerals formed by organisms
    • Lowenstam, H. (1981) Minerals formed by organisms. Science 211, 1126-1131
    • (1981) Science , vol.211 , pp. 1126-1131
    • Lowenstam, H.1
  • 43
    • 78649447949 scopus 로고    scopus 로고
    • Patterning a spiralian embryo. A segregated RNA for a Tis11 ortholog is required in the 3a and 3b cells of the Ilyanassa embryo
    • Chan, X. Y., and Lambert, J. D. (2011) Patterning a spiralian embryo. A segregated RNA for a Tis11 ortholog is required in the 3a and 3b cells of the Ilyanassa embryo. Dev. Biol. 349, 102-112
    • (2011) Dev. Biol. , vol.349 , pp. 102-112
    • Chan, X.Y.1    Lambert, J.D.2
  • 44
    • 78149419530 scopus 로고    scopus 로고
    • β-Catenin and early development in the gastropod, Crepidula fornicata
    • Henry, J. Q., Perry, K. J., and Martindale, M. Q. (2010) β-Catenin and early development in the gastropod, Crepidula fornicata. Integr. Comp. Biol. 50, 707-719
    • (2010) Integr. Comp. Biol. , vol.50 , pp. 707-719
    • Henry, J.Q.1    Perry, K.J.2    Martindale, M.Q.3
  • 45
    • 40149099121 scopus 로고    scopus 로고
    • Nanos is required in somatic blast cell lineages in the posterior of a mollusk embryo
    • Rabinowitz, J. S., Chan, X. Y., Kingsley, E. P., Duan, Y., and Lambert, J. D. (2008) Nanos is required in somatic blast cell lineages in the posterior of a mollusk embryo. Curr. Biol. 18, 331-336
    • (2008) Curr. Biol. , vol.18 , pp. 331-336
    • Rabinowitz, J.S.1    Chan, X.Y.2    Kingsley, E.P.3    Duan, Y.4    Lambert, J.D.5
  • 46
    • 0029667586 scopus 로고    scopus 로고
    • Control of aragonite or calcite polymorphism by mollusk shell macromolecules
    • Falini, G., Albeck, S., Weiner, S., and Addadi, L. (1996) Control of aragonite or calcite polymorphism by mollusk shell macromolecules. Science 271, 67-69
    • (1996) Science , vol.271 , pp. 67-69
    • Falini, G.1    Albeck, S.2    Weiner, S.3    Addadi, L.4


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