Biomineralization: Functions of calmodulin-like protein in the shell formation of pearl oyster

Biochimica et Biophysica Acta - General Subjects

Volumn 1770, Issue 9, 2007, Pages 1338-1344

  Yan, Zhenguang ^a   Fang, Zi ^a   Ma, Zhuojun ^a   Deng, Jinye ^a   Li, Shuo ^a   Xie, Liping ^a   Zhang, Rongqing ^a  

^a TSINGHUA UNIVERSITY   (China)

Author keywords

Biomineralization; Calmodulin like protein; Organic layer; Pearl oyster; Pinctada fucata

Indexed keywords

CALCIUM CARBONATE; CALMODULIN LIKE PROTEIN; EDETIC ACID; PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BIOMINERALIZATION; CONTROLLED STUDY; CRYSTALLIZATION; IMMUNOHISTOLOGY; MOLECULAR WEIGHT; NONHUMAN; OYSTER; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PURIFICATION; REGULATORY MECHANISM;

ANIMALS; CALCIFICATION, PHYSIOLOGIC; CALCIUM CARBONATE; CALMODULIN; IMMUNOHISTOCHEMISTRY; PINCTADA; RECOMBINANT PROTEINS;

PINCTADA; PINCTADA FUCATA;

EID: 34547830943     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2007.06.018     Document Type: Article

References (27)

1. Mann S. Biomineralization. Principles and concepts in bioinorganic materials chemistry (2001), Oxford University Press, Oxford pp. 6-23
2. 3 polymorph mixtures. Chem. Eng. Technol. 29 (2006) 221-225
3. Falini G., Albeck S., Weiner S., and Addadi L. Control of aragonite or calcite polymorphism by mollusk shell macromolecules. Science 271 (1996) 67-69
4. Marin F., and Luquet G. Molluscan shell proteins. C. R. Palevol. 3 (2004) 469-492
5. Zhang C., and Zhang R. Matrix proteins in the outer shells of molluscs. Mar. Biotechnol. 8 (2006) 572-586
6. Marin F., Corstjens P., de Gaulejac B., de Vrind-De Jong E., and Westbroek P. Mucins and molluscan calcification. Molecular characterization of mucoperlin, a novel mucin-like protein from the nacreous shell layer of the fan mussel Pinna nobilis (Bivalvia, pteriomorphia). J. Biol. Chem. 275 (2000) 20667-20675
7. Marin F., and Luquet G. Molluscan biomineralization: the proteinaceous shell constituents of Pinna nobilis L. Mater. Sci. Eng., C, Biomim. Mater., Sens. Syst. 25 (2005) 105-111
8. Li S., Xie L., Zhang C., Zhang Y., Gu M., and Zhang R. Cloning and expression of a pivotal calcium metabolism regulator: calmodulin involved in shell formation from pearl oyster (Pinctada fucata). Comp. Biochem. Physiol., Part B Biochem. Mol. Biol. 138 (2004) 235-243
9. Li S., Xie L., Ma Z., and Zhang R. cDNA cloning and characterization of a novel calmodulin-like protein from pearl oyster Pinctada fucata. FEBS J. 272 (2005) 4899-4910
10. Billingsley M.L., Pennypacker K.R., Hoover C.G., Brigati D.J., and Kincaid R.L. A rapid and sensitive method for detection and quantification of calcineurin and calmodulin-binding proteins using biotinylated calmodulin. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 7585-7589
11. Jahn R., Schiebler W., and Greengard P. A quantitative dot-immunobinding assay for proteins using nitrocellulose membrane filters. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 1684-1687
12. Bhown A.S., and Bennett J.C. High-sensitivity sequence analysis of protein recovered from sodium dodecyl sulfate gel. Methods Enzymol. 91 (1983) 450-455
13. Xu G., Yao N., Aksay I.A., and Groves J.T. Biomimetic synthesis of macroscopic-scale calcium carbonate thin films. Evidence for a multistep assembly process. J. Am. Chem. Soc. 120 (1998) 11977-11985
14. Nudelman F., Gotliv B.A., Addadi L., and Weiner S. Mollusk shell formation: mapping the distribution of organic matrix components underlying a single aragonitic tablet in nacre. J. Struct. Biol. 153 (2006) 176-187
15. Sun L., Blair H.C., Peng Y., Zaidi N., Adebanjo O.A., Wu X.B., Wu X.Y., Iqbal J., Epstein S., Abe E., Moonga B.S., and Zaidi M. Calcineurin regulates bone formation by the osteoblast. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17130-17135
16. Zayzafoon M., Fulzele K., and McDonald J.M. Calmodulin and calmodulin-dependent kinase IIalpha regulate osteoblast differentiation by controlling c-fos expression. J. Biol. Chem. 280 (2005) 7049-7059
17. Zielinski R.E. Calmodulin and calmodulin-binding proteins in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49 (1998) 697-725
18. Mao G.H., Hou L.X., Ding C.B., Cui S.J., and Sun D.Y. Characterization of a cDNA coding for an extracellular calmodulin-binding protein from suspension-cultured cells of Angelica dahurica. Planta 222 (2005) 428-437
19. Crocker G., Dawson R.A., Barton C.H., and MacNeil S. An extracellular role for calmodulin-like activity in cell proliferation. Biochem. J. 253 (1988) 877-884
20. 2+ with the calmodulin-sensitive adenylate cyclase from Bordetella pertussis. J. Biol. Chem. 263 (1988) 6933-6940
21. Michenfelder M., Fu G., Lawrence C., Weaver J.C., Wustman B.A., Taranto L., Evans J.S., and Morse D.E. Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains. Biopolymers 70 (2003) 522-533
22. Matsushiro A., Miyashita T., Miyamoto H., Morimoto K., Tonomura B., Tanaka A., and Sato K. Presence of protein complex is prerequisite for aragonite crystallization in the nacreous layer. Mar. Biotechnol. (NY) 5 (2003) 37-44
23. Kono M., Hayashi N., and Samata T. Molecular mechanism of the nacreous layer formation in Pinctada maxima. Biochem. Biophys. Res. Commun. 269 (2000) 213-218
24. Nelson J.W., Tredgett M.W., Sheehan J.K., Thornton D.J., Notman D., and Govan J.R. Mucinophilic and chemotactic properties of Pseudomonas aeruginosa in relation to pulmonary colonization in cystic fibrosis. Infect. Immun. 58 (1990) 1489-1495
25. Samata T., et al. A new matrix protein family related to the nacreous layer formation of Pinctada fucata. FEBS Lett. 462 (1999) 225-229
26. Belcher A.M., Wu X.H., Christensen R.J., Hansma P.K., Stucky G.D., and Morse D.E. Control of crystal phase switching and orientation by soluble mollusc-shell proteins. Nature 381 (1996) 56-58
27. Weiss I.M., Gohring W., Fritz M., and Mann K. Perlustrin, a Haliotis laevigata (abalone) nacre protein, is homologous to the insulin-like growth factor binding protein N-terminal module of vertebrates. Biochem. Biophys. Res. Commun. 285 (2001) 244-249