메뉴 건너뛰기




Volumn 12, Issue 4, 2007, Pages 381-388

Cloning and Characterization of an mRNA Encoding F1-ATPase Beta-Subunit Abundant in Epithelial Cells of Mantle and Gill of Pearl Oyster, Pinctada fucata

Author keywords

biomineralization; F1 subunit; gill; mantle; Pinctada fucata

Indexed keywords

DEGENERATED PRIMERS; F1BETASUBUNIT; GILL; MANTLE; PINCTADA FUCATA;

EID: 34447617687     PISSN: 10070214     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1007-0214(07)70057-3     Document Type: Article
Times cited : (5)

References (36)
  • 1
    • 0002297603 scopus 로고
    • Shell formation in mollusks
    • Florkin M., and Scheer B. (Eds), Academic Press, London
    • Wilbur K. Shell formation in mollusks. In: Florkin M., and Scheer B. (Eds). Chemical Zoology Vol. 7 (1972), Academic Press, London 103-145
    • (1972) Chemical Zoology , vol.7 , pp. 103-145
    • Wilbur, K.1
  • 3
    • 0030707506 scopus 로고    scopus 로고
    • Biomineralization: A pavement of pearl
    • Addadi L., and Weiner S. Biomineralization: A pavement of pearl. Nature 389 (1997) 912-914
    • (1997) Nature , vol.389 , pp. 912-914
    • Addadi, L.1    Weiner, S.2
  • 4
    • 0023835389 scopus 로고
    • Molecular recognition in biomineralization
    • Mann S. Molecular recognition in biomineralization. Nature 332 (1988) 119-124
    • (1988) Nature , vol.332 , pp. 119-124
    • Mann, S.1
  • 6
    • 0038460747 scopus 로고    scopus 로고
    • Localization of Hg and Pb in the palps, the digestive gland and the gills in Mytilus galloprovincialis (L.) using autometallography and X-ray microanalysis
    • Dimitriadis V., Domouhtsidou G., and Raftopoulou E. Localization of Hg and Pb in the palps, the digestive gland and the gills in Mytilus galloprovincialis (L.) using autometallography and X-ray microanalysis. Environ. Pollut. 125 (2003) 345-353
    • (2003) Environ. Pollut. , vol.125 , pp. 345-353
    • Dimitriadis, V.1    Domouhtsidou, G.2    Raftopoulou, E.3
  • 7
    • 34447640743 scopus 로고    scopus 로고
    • Microscopic structure of the mantle and palps in the freshwater mussels Velesunio ambiguus and Hyridella depressa (Bivalvia: Hyriidae)
    • Anne E., and Richard P. Microscopic structure of the mantle and palps in the freshwater mussels Velesunio ambiguus and Hyridella depressa (Bivalvia: Hyriidae). Molluscan Research 23 (2003) 1-20
    • (2003) Molluscan Research , vol.23 , pp. 1-20
    • Anne, E.1    Richard, P.2
  • 8
    • 0030787019 scopus 로고    scopus 로고
    • Histochemical and X-ray studies on tissue concretions and shell of Margaritifera margaritifera (Linnaeus)
    • Pekkarinen M., and Valovirta I. Histochemical and X-ray studies on tissue concretions and shell of Margaritifera margaritifera (Linnaeus). J. Shellfish Res. 16 (1997) 169-177
    • (1997) J. Shellfish Res. , vol.16 , pp. 169-177
    • Pekkarinen, M.1    Valovirta, I.2
  • 9
    • 0033836627 scopus 로고    scopus 로고
    • Alterations in hemolymph and extrapallial fluid parameters in the Manila Clam, Ruditapes philippinarum, challenged with the pathogen Vibrio tapetis
    • Allam B., Paillard C., and Auffret M. Alterations in hemolymph and extrapallial fluid parameters in the Manila Clam, Ruditapes philippinarum, challenged with the pathogen Vibrio tapetis. J. of Invertebrate Pathology 76 (2000) 63-69
    • (2000) J. of Invertebrate Pathology , vol.76 , pp. 63-69
    • Allam, B.1    Paillard, C.2    Auffret, M.3
  • 10
    • 5744253985 scopus 로고    scopus 로고
    • Molluscan shell proteins
    • Marin F., and Luquet G. Molluscan shell proteins. Comptes Rendus Palevol 3 6-7 (2004) 469-492
    • (2004) Comptes Rendus Palevol , vol.3 , Issue.6-7 , pp. 469-492
    • Marin, F.1    Luquet, G.2
  • 13
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase-A splendid molecular machine
    • Boyer P. The ATP synthase-A splendid molecular machine. Annual Review in Biochemistry 66 (1997) 717-749
    • (1997) Annual Review in Biochemistry , vol.66 , pp. 717-749
    • Boyer, P.1
  • 14
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams J., Leslie A., Lutter R., and Walker J. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 375 (1994) 621-628
    • (1994) Nature , vol.375 , pp. 621-628
    • Abrahams, J.1    Leslie, A.2    Lutter, R.3    Walker, J.4
  • 15
    • 3543044441 scopus 로고    scopus 로고
    • Structural insight into the cooperativity between catalytic and noncatalytic sites of F1-ATPase
    • Falson P., Goffeau A., Boutry M., and Jault J. Structural insight into the cooperativity between catalytic and noncatalytic sites of F1-ATPase. Biochim. Biophys. Acta. 1658 1-2 (2004) 133-140
    • (2004) Biochim. Biophys. Acta. , vol.1658 , Issue.1-2 , pp. 133-140
    • Falson, P.1    Goffeau, A.2    Boutry, M.3    Jault, J.4
  • 18
    • 8744293655 scopus 로고    scopus 로고
    • Lipid raft proteome reveals ATP synthase complex in the cell surface
    • Bae T.-J., Kim M.-S., Kim J.-W., et al. Lipid raft proteome reveals ATP synthase complex in the cell surface. Proteomics 4 (2004) 3536-3548
    • (2004) Proteomics , vol.4 , pp. 3536-3548
    • Bae, T.-J.1    Kim, M.-S.2    Kim, J.-W.3
  • 20
    • 2442691834 scopus 로고    scopus 로고
    • Endothelial cell surface ATP synthase-triggered caspase-apoptotic pathway is essential for K1-5-induced antiangiogenesis
    • Veitonmaki N., Cao R., Wu L., Moser T., Li B., Pizzo S., Zhivotovsky B., and Cao Y. Endothelial cell surface ATP synthase-triggered caspase-apoptotic pathway is essential for K1-5-induced antiangiogenesis. Cancer Research 64 (2005) 3679-3686
    • (2005) Cancer Research , vol.64 , pp. 3679-3686
    • Veitonmaki, N.1    Cao, R.2    Wu, L.3    Moser, T.4    Li, B.5    Pizzo, S.6    Zhivotovsky, B.7    Cao, Y.8
  • 22
    • 9644301151 scopus 로고    scopus 로고
    • The F1-ATPase β-subunit is the putative enterostatin receptor
    • Park M., Lin L., Thomas S., Braymer H., Smith P., Harrison D., and York D. The F1-ATPase β-subunit is the putative enterostatin receptor. Peptides 25 12 (2004) 2127-2133
    • (2004) Peptides , vol.25 , Issue.12 , pp. 2127-2133
    • Park, M.1    Lin, L.2    Thomas, S.3    Braymer, H.4    Smith, P.5    Harrison, D.6    York, D.7
  • 23
    • 0030581291 scopus 로고    scopus 로고
    • Mitochondrial ATP synthase F-1-beta-subunit is a calcium-binding protein
    • Hubbard M., and McHugh N. Mitochondrial ATP synthase F-1-beta-subunit is a calcium-binding protein. FEBS Lett 391 3 (1996) 323-329
    • (1996) FEBS Lett , vol.391 , Issue.3 , pp. 323-329
    • Hubbard, M.1    McHugh, N.2
  • 24
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tool
    • Thompson J., Gibson T., Plewniak F., et al. The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tool. Nucleic Acids Research 24 (1997) 4876-4882
    • (1997) Nucleic Acids Research , vol.24 , pp. 4876-4882
    • Thompson, J.1    Gibson, T.2    Plewniak, F.3
  • 25
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N., and Nei M. The neighbor-joining method: A new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4 (1987) 406-425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 26
    • 0035793844 scopus 로고    scopus 로고
    • Immunohistochemical and in situ hybridization studies of gonadotropin releasing hormone (GnRH) and its receptor in rat digestive tract
    • Huang W., Yao B., Sun L., Pu R., Wang L., and Zhang R. Immunohistochemical and in situ hybridization studies of gonadotropin releasing hormone (GnRH) and its receptor in rat digestive tract. Life Sci. 68 (2001) 1727-1734
    • (2001) Life Sci. , vol.68 , pp. 1727-1734
    • Huang, W.1    Yao, B.2    Sun, L.3    Pu, R.4    Wang, L.5    Zhang, R.6
  • 27
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • Noji H., Yasuda R., Yoshida M., and Kinosita Jr. K. Direct observation of the rotation of F1-ATPase. Nature 386 6622 (1997) 217-219
    • (1997) Nature , vol.386 , Issue.6622 , pp. 217-219
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita Jr., K.4
  • 28
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J., Saraste M., Runswick M., and Gay N. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1 8 (1982) 945-951
    • (1982) EMBO J. , vol.1 , Issue.8 , pp. 945-951
    • Walker, J.1    Saraste, M.2    Runswick, M.3    Gay, N.4
  • 29
    • 0037412181 scopus 로고    scopus 로고
    • A conformational analysis of Walker motif A [GXXXXGKT (S)] in nucleotide-binding and other proteins
    • Ramakrishnan C., Dani V., and Ramasarma T. A conformational analysis of Walker motif A [GXXXXGKT (S)] in nucleotide-binding and other proteins. Protein Engineering 15 10 (2002) 783-798
    • (2002) Protein Engineering , vol.15 , Issue.10 , pp. 783-798
    • Ramakrishnan, C.1    Dani, V.2    Ramasarma, T.3
  • 30
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh D., Ziegler W., and Parker P. Multiple pathways control protein kinase C phosphorylation. EMBO J. 19 4 (2000) 496-503
    • (2000) EMBO J. , vol.19 , Issue.4 , pp. 496-503
    • Parekh, D.1    Ziegler, W.2    Parker, P.3
  • 31
    • 0027722138 scopus 로고
    • Casein kinase II in signal transduction and cell cycle regulation
    • Litchfield D., and Luscher B. Casein kinase II in signal transduction and cell cycle regulation. Mol. Cell Biochem. 127 (1993) 187-199
    • (1993) Mol. Cell Biochem. , vol.127 , pp. 187-199
    • Litchfield, D.1    Luscher, B.2
  • 32
    • 0022134753 scopus 로고
    • Cyclic AMP and calcium in differential control of Mytilus gill cilia
    • Stommel E., and Stephens R. Cyclic AMP and calcium in differential control of Mytilus gill cilia. J. Comp. Physiol. A 157 (1985) 451-459
    • (1985) J. Comp. Physiol. A , vol.157 , pp. 451-459
    • Stommel, E.1    Stephens, R.2
  • 33
    • 0020034156 scopus 로고
    • Specific localization of scallop gill epithelial calmodulin in cilia
    • Stommel E., Stephens R., Masure H., and Head J. Specific localization of scallop gill epithelial calmodulin in cilia. J. Cell Biol. 92 (1982) 622-628
    • (1982) J. Cell Biol. , vol.92 , pp. 622-628
    • Stommel, E.1    Stephens, R.2    Masure, H.3    Head, J.4
  • 34
    • 3142638636 scopus 로고    scopus 로고
    • Cloning and expression of a pivotal calcium metabolism regulator: calmodulin involved in shell formation from pearl oyster (Pinctada fucata)
    • 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. B 138 3 (2004) 235-243
    • (2004) Comp. Biochem. Physiol. B , vol.138 , Issue.3 , pp. 235-243
    • Li, S.1    Xie, L.2    Zhang, C.3    Zhang, Y.4    Gu, M.5    Zhang, R.6
  • 35
    • 0033692678 scopus 로고    scopus 로고
    • A new model for periostracum and shell formation in Unionidae (Bivalvia, Mollusca)
    • Checa A. A new model for periostracum and shell formation in Unionidae (Bivalvia, Mollusca). Tissue and Cell 32 (2000) 405-416
    • (2000) Tissue and Cell , vol.32 , pp. 405-416
    • Checa, A.1
  • 36
    • 18144377424 scopus 로고    scopus 로고
    • The carbonic anhydrase domain protein nacrein is expressed in the epithelial cells of the mantle and acts as a negative regulator in calcification in the mollusc Pinctada fucata
    • Miyamoto H., Miyoshi F., and Kohno J. The carbonic anhydrase domain protein nacrein is expressed in the epithelial cells of the mantle and acts as a negative regulator in calcification in the mollusc Pinctada fucata. Zoolog. Sci. 22 3 (2005) 311-315
    • (2005) Zoolog. Sci. , vol.22 , Issue.3 , pp. 311-315
    • Miyamoto, H.1    Miyoshi, F.2    Kohno, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.