메뉴 건너뛰기




Volumn 79, Issue , 2013, Pages 100-113

Mapping sea urchins tube feet proteome - A unique hydraulic mechano-sensory adhesive organ

Author keywords

Adhesive proteins; Glycosylation; Phosphorylation; Proteome; Sea urchin; Tube feet

Indexed keywords

ALPHA ACTININ; ALPHA TUBULIN; APOLIPOPROTEIN B100; CALMODULIN; CALPAIN; CALRETICULIN; CATALASE; CHAPERONIN; CITRATE SYNTHASE; COLLAGEN; CUBILIN; ENDOPHILIN; ENOLASE; FASCIN; FILAMIN A; FLOTILLIN 1; GALECTIN 8; GELSOLIN; GLUTAMATE DEHYDROGENASE; GLUTAMATE RECEPTOR 1; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4; PROTEOME; RIBOSOME PROTEIN; SORCIN; TRANSALDOLASE; TRANSKETOLASE; TROPOMYOSIN;

EID: 84872199761     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.12.004     Document Type: Article
Times cited : (33)

References (51)
  • 1
    • 0023139072 scopus 로고
    • Nature's underwater adhesive specialist
    • Waite J.H. Nature's underwater adhesive specialist. Int J Adhes Adhes 1987, 7:9-14.
    • (1987) Int J Adhes Adhes , vol.7 , pp. 9-14
    • Waite, J.H.1
  • 2
    • 0006219088 scopus 로고
    • Adhesive interactions between the tube feet of a starfish, Leptasterias hexactis, and substrata
    • Thomas L.A., Hermans C.O. Adhesive interactions between the tube feet of a starfish, Leptasterias hexactis, and substrata. Biol Bull 1985, 169:675-688.
    • (1985) Biol Bull , vol.169 , pp. 675-688
    • Thomas, L.A.1    Hermans, C.O.2
  • 3
    • 0001812635 scopus 로고    scopus 로고
    • Adhesion in echinoderms
    • Balkema, Rotterdam
    • Flammang P. Adhesion in echinoderms. Echinoderm studies 1996, vol. 5:1-60. Balkema, Rotterdam.
    • (1996) Echinoderm studies , vol.5 , pp. 1-60
    • Flammang, P.1
  • 4
    • 33746831611 scopus 로고    scopus 로고
    • Morphology and tenacity of the tube foot disc of three common European sea urchin species: a comparative study
    • Santos R., Flammang P. Morphology and tenacity of the tube foot disc of three common European sea urchin species: a comparative study. Biofouling 2006, 22:187-200.
    • (2006) Biofouling , vol.22 , pp. 187-200
    • Santos, R.1    Flammang, P.2
  • 5
    • 21144478194 scopus 로고
    • Functional morphology of coronal and peristomeal podia in Sphaerechinus granularis (Echinodermata Echinoida)
    • Flammang P., Jangoux M. Functional morphology of coronal and peristomeal podia in Sphaerechinus granularis (Echinodermata Echinoida). Zoomorphology 1993, 113:47-60.
    • (1993) Zoomorphology , vol.113 , pp. 47-60
    • Flammang, P.1    Jangoux, M.2
  • 6
    • 0031691654 scopus 로고    scopus 로고
    • A study of the temporary adhesion of the podia in the sea star Asterias rubens (Echinodermata, Asteroidea) through their footprints
    • Flammang P., Michel A., Van Cauwenberge A., Alexandre H., Jangoux M. A study of the temporary adhesion of the podia in the sea star Asterias rubens (Echinodermata, Asteroidea) through their footprints. J Exp Biol 1998, 201:2383-2395.
    • (1998) J Exp Biol , vol.201 , pp. 2383-2395
    • Flammang, P.1    Michel, A.2    Van Cauwenberge, A.3    Alexandre, H.4    Jangoux, M.5
  • 7
    • 70449517481 scopus 로고    scopus 로고
    • First insights into the biochemistry of tube foot adhesive from the sea urchin Paracentrotus lividus (Echinoidea, Echinodermata)
    • Santos R., da Costa G., Franco C., Gomes-Alves P., Flammang P., Coelho A.V. First insights into the biochemistry of tube foot adhesive from the sea urchin Paracentrotus lividus (Echinoidea, Echinodermata). Mar Biotechnol 2009, 11:686-698.
    • (2009) Mar Biotechnol , vol.11 , pp. 686-698
    • Santos, R.1    da Costa, G.2    Franco, C.3    Gomes-Alves, P.4    Flammang, P.5    Coelho, A.V.6
  • 8
    • 34347357100 scopus 로고    scopus 로고
    • Barnacle underwater attachment
    • Springer, Berlin, A.M. Smith, J.A. Callow (Eds.)
    • Kamino K. Barnacle underwater attachment. Biological adhesives 2006, 145-166. Springer, Berlin. A.M. Smith, J.A. Callow (Eds.).
    • (2006) Biological adhesives , pp. 145-166
    • Kamino, K.1
  • 9
    • 36749099994 scopus 로고    scopus 로고
    • Understanding marine mussel adhesion
    • Silverman H.G., Roberto F.F. Understanding marine mussel adhesion. Mar Biotechnol 2007, 9:661-681.
    • (2007) Mar Biotechnol , vol.9 , pp. 661-681
    • Silverman, H.G.1    Roberto, F.F.2
  • 10
    • 33751167773 scopus 로고    scopus 로고
    • The biochemistry and mechanics of gastropod adhesive gels
    • Springer, Berlin, A.M. Smith, J.A. Callow (Eds.)
    • Smith A.M. The biochemistry and mechanics of gastropod adhesive gels. Biological adhesives 2006, 167-182. Springer, Berlin. A.M. Smith, J.A. Callow (Eds.).
    • (2006) Biological adhesives , pp. 167-182
    • Smith, A.M.1
  • 11
    • 79957985249 scopus 로고    scopus 로고
    • Characterisation of the carbohydrate fraction of the temporary adhesive secreted by the tube feet of the sea star Asterias rubens
    • Hennebert E., Wattiez R., Flammang P. Characterisation of the carbohydrate fraction of the temporary adhesive secreted by the tube feet of the sea star Asterias rubens. Mar Biotechnol 2011, 13:484-495.
    • (2011) Mar Biotechnol , vol.13 , pp. 484-495
    • Hennebert, E.1    Wattiez, R.2    Flammang, P.3
  • 12
    • 30044452034 scopus 로고    scopus 로고
    • Cement proteins of the tube-building polychaete Phragmatopoma californica
    • Zhao H., Sun C., Stewart R.J., Waite J.H. Cement proteins of the tube-building polychaete Phragmatopoma californica. J Biol Chem 2005, 280:42938-42944.
    • (2005) J Biol Chem , vol.280 , pp. 42938-42944
    • Zhao, H.1    Sun, C.2    Stewart, R.J.3    Waite, J.H.4
  • 13
    • 69349096579 scopus 로고    scopus 로고
    • Polyphosphoprotein containing marine adhesives
    • Flammang P., Lambert A., Bailly P., Hennebert E. Polyphosphoprotein containing marine adhesives. J Adhes 2009, 85:447-464.
    • (2009) J Adhes , vol.85 , pp. 447-464
    • Flammang, P.1    Lambert, A.2    Bailly, P.3    Hennebert, E.4
  • 14
    • 0035814883 scopus 로고    scopus 로고
    • Polyphosphoprotein from the adhesive pads of Mytilus edulis
    • Waite J.H., Qin X. Polyphosphoprotein from the adhesive pads of Mytilus edulis. Biochemistry 2001, 40:2887-2893.
    • (2001) Biochemistry , vol.40 , pp. 2887-2893
    • Waite, J.H.1    Qin, X.2
  • 15
    • 34547408364 scopus 로고    scopus 로고
    • Histidinoalanine: a crosslinking amino acid
    • Taylor C.M., Wang W. Histidinoalanine: a crosslinking amino acid. Tetrahedron Rep 2007, 63:9033-9047.
    • (2007) Tetrahedron Rep , vol.63 , pp. 9033-9047
    • Taylor, C.M.1    Wang, W.2
  • 16
    • 79953054035 scopus 로고    scopus 로고
    • Exploring the proteome of an echinoderm nervous system: 2DE of the starfish radial nerve cord and the synaptosomal membranes subproteome
    • Franco C., Santos R., Coelho A.V. Exploring the proteome of an echinoderm nervous system: 2DE of the starfish radial nerve cord and the synaptosomal membranes subproteome. Proteomics 2011, 11:1359-1364.
    • (2011) Proteomics , vol.11 , pp. 1359-1364
    • Franco, C.1    Santos, R.2    Coelho, A.V.3
  • 17
    • 80051807647 scopus 로고    scopus 로고
    • Proteome characterization of sea star coelomocytes - the innate immune effector cells of echinoderms
    • Franco C., Santos R., Coelho A.V. Proteome characterization of sea star coelomocytes - the innate immune effector cells of echinoderms. Proteomics 2011, 11:3587-3592.
    • (2011) Proteomics , vol.11 , pp. 3587-3592
    • Franco, C.1    Santos, R.2    Coelho, A.V.3
  • 18
    • 0033006391 scopus 로고    scopus 로고
    • Differences in the composition of adhesive and non-adhesive mucus from the limpet Lottia limatula
    • Smith A.M., Quick T.J., St Peter R.L.S. Differences in the composition of adhesive and non-adhesive mucus from the limpet Lottia limatula. Biol Bull 1999, 196:34-44.
    • (1999) Biol Bull , vol.196 , pp. 34-44
    • Smith, A.M.1    Quick, T.J.2    St Peter, R.L.S.3
  • 19
    • 3142780053 scopus 로고    scopus 로고
    • A glycosylated byssal precursor protein from the green mussel Perna viridis with modified Dopa side-chains
    • Ohkawa K., Nishida A., Yamamoto H., Waite J.H. A glycosylated byssal precursor protein from the green mussel Perna viridis with modified Dopa side-chains. Biofouling 2004, 20:101-115.
    • (2004) Biofouling , vol.20 , pp. 101-115
    • Ohkawa, K.1    Nishida, A.2    Yamamoto, H.3    Waite, J.H.4
  • 20
    • 0033408412 scopus 로고    scopus 로고
    • Monoclonal antibodies to adhesive cell coat glycoproteins secreted by zoospores of the green alga Enteromorpha
    • Stanley M.S., Callow M.E., Callow J.A. Monoclonal antibodies to adhesive cell coat glycoproteins secreted by zoospores of the green alga Enteromorpha. Planta 1999, 210:61-71.
    • (1999) Planta , vol.210 , pp. 61-71
    • Stanley, M.S.1    Callow, M.E.2    Callow, J.A.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff V., Harold N., Ehrhardt W. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 1988, 9:255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Harold, N.2    Ehrhardt, W.3
  • 23
    • 33750995860 scopus 로고    scopus 로고
    • The genome of the sea urchin Strongylocentrotus purpuratus
    • Sea Urchin Genome Sequencing Consortium
    • Sea Urchin Genome Sequencing Consortium The genome of the sea urchin Strongylocentrotus purpuratus. Science 2006, 314:941-952.
    • (2006) Science , vol.314 , pp. 941-952
  • 26
    • 33751539851 scopus 로고    scopus 로고
    • Opsins and clusters of sensory G-protein-coupled receptors in the sea urchin genome
    • Raible F., Tessmar-Raible T., Arboleda E., Kaller T., Bork P., Arendt D., et al. Opsins and clusters of sensory G-protein-coupled receptors in the sea urchin genome. Dev Biol 2006, 300:461-475.
    • (2006) Dev Biol , vol.300 , pp. 461-475
    • Raible, F.1    Tessmar-Raible, T.2    Arboleda, E.3    Kaller, T.4    Bork, P.5    Arendt, D.6
  • 28
    • 80054003658 scopus 로고    scopus 로고
    • Sea urchin tube feet are photosensory organs that express a rhabdomeric-like opsin and PAX6
    • Lesser M.P., Carleton K.L., Böttger S.A., Barry T.M., Walker C.W. Sea urchin tube feet are photosensory organs that express a rhabdomeric-like opsin and PAX6. Proc R Soc B 2011, 278:3371-3379.
    • (2011) Proc R Soc B , vol.278 , pp. 3371-3379
    • Lesser, M.P.1    Carleton, K.L.2    Böttger, S.A.3    Barry, T.M.4    Walker, C.W.5
  • 29
    • 80053270792 scopus 로고    scopus 로고
    • Neurosensory and neuromuscular organization in tube feet of the sea urchin Strongylocentrotus purpuratus
    • Agca C., Elhajj M.C., Klein W.H., Venuti J.M. Neurosensory and neuromuscular organization in tube feet of the sea urchin Strongylocentrotus purpuratus. J Comp Neurol 2011, 519:3566-3579.
    • (2011) J Comp Neurol , vol.519 , pp. 3566-3579
    • Agca, C.1    Elhajj, M.C.2    Klein, W.H.3    Venuti, J.M.4
  • 30
    • 0036707129 scopus 로고    scopus 로고
    • Molecular chaperones in ectothermic marine animals: biochemical function and gene expression
    • Hofmann G.E., Buckley B.A., Place S.P., Zippay M.L. Molecular chaperones in ectothermic marine animals: biochemical function and gene expression. Integr Comp Biol 2002, 42:808-814.
    • (2002) Integr Comp Biol , vol.42 , pp. 808-814
    • Hofmann, G.E.1    Buckley, B.A.2    Place, S.P.3    Zippay, M.L.4
  • 31
    • 0033635891 scopus 로고    scopus 로고
    • Isolation and characterization of a Paracentrotus lividus cDNA encoding a stress-inducible chaperonin
    • Gianguzza F., Ragusa M.A., Roccheri M.C., Di Liegro I., Rinaldi A.M. Isolation and characterization of a Paracentrotus lividus cDNA encoding a stress-inducible chaperonin. Cell Stress Chaperones 2000, 5:87-89.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 87-89
    • Gianguzza, F.1    Ragusa, M.A.2    Roccheri, M.C.3    Di Liegro, I.4    Rinaldi, A.M.5
  • 32
    • 84872189644 scopus 로고    scopus 로고
    • Differences in hsp70 mRNA induction between purple sea urchins (Strongylocentrotus purpuratus) with different thermal histories
    • PART 2
    • Osovitz C.J., Hofmann G.E. Differences in hsp70 mRNA induction between purple sea urchins (Strongylocentrotus purpuratus) with different thermal histories. FASEB J 2005, 19.5(Suppl. S, Part 2):A1652.
    • (2005) FASEB J , Issue.SUPPL. S
    • Osovitz, C.J.1    Hofmann, G.E.2
  • 33
    • 77950221215 scopus 로고    scopus 로고
    • Echinoderms: potential model systems for studies on muscle regeneration
    • García-Arrarás J.E., Dolmatov I.Y. Echinoderms: potential model systems for studies on muscle regeneration. Curr Pharm Des 2010, 16:942-955.
    • (2010) Curr Pharm Des , vol.16 , pp. 942-955
    • García-Arrarás, J.E.1    Dolmatov, I.Y.2
  • 36
    • 61449212918 scopus 로고    scopus 로고
    • Highly variable immune-response proteins (185/333) from the sea urchin, Strongylocentrotus purpuratus: proteomic analysis identifies diversity within and between individuals
    • Dheilly N.M., Nair S.V., Smith L.C., Raftos D.A. Highly variable immune-response proteins (185/333) from the sea urchin, Strongylocentrotus purpuratus: proteomic analysis identifies diversity within and between individuals. J Immunol 2009, 182:2203-2212.
    • (2009) J Immunol , vol.182 , pp. 2203-2212
    • Dheilly, N.M.1    Nair, S.V.2    Smith, L.C.3    Raftos, D.A.4
  • 37
    • 78751581603 scopus 로고    scopus 로고
    • Comparative proteomic analysis of a sea urchin (Heliocidaris erythrogramma) antibacterial response revealed the involvement of apextrin and calreticulin
    • Dheilly N.M., Haynes P.A., Bove U., Nair S.V., Raftos D.A. Comparative proteomic analysis of a sea urchin (Heliocidaris erythrogramma) antibacterial response revealed the involvement of apextrin and calreticulin. J Invertebr Pathol 2011, 106:223-229.
    • (2011) J Invertebr Pathol , vol.106 , pp. 223-229
    • Dheilly, N.M.1    Haynes, P.A.2    Bove, U.3    Nair, S.V.4    Raftos, D.A.5
  • 42
    • 77952579210 scopus 로고    scopus 로고
    • Conventional and unconventional antimicrobials from fish, marine invertebrates and micro-algae
    • Smith V.J., Desbois A.P., Dyrynda E.A. Conventional and unconventional antimicrobials from fish, marine invertebrates and micro-algae. Mar Drugs 2010, 8:1213-1262.
    • (2010) Mar Drugs , vol.8 , pp. 1213-1262
    • Smith, V.J.1    Desbois, A.P.2    Dyrynda, E.A.3
  • 43
    • 84859499654 scopus 로고    scopus 로고
    • Characterization of the protein fraction of the temporary adhesive secreted by the tube feet of the sea star Asterias rubens
    • Hennebert E., Wattiez R., Waite J.H., Flammang P. Characterization of the protein fraction of the temporary adhesive secreted by the tube feet of the sea star Asterias rubens. Biofouling 2012, 28(3):289-303.
    • (2012) Biofouling , vol.28 , Issue.3 , pp. 289-303
    • Hennebert, E.1    Wattiez, R.2    Waite, J.H.3    Flammang, P.4
  • 44
    • 78650169840 scopus 로고    scopus 로고
    • Phylogenetic analysis and homology modelling of Paracentrotus lividus nectin
    • Costa C., Cavalcante C., Zito F., Yokota Y., Matranga V. Phylogenetic analysis and homology modelling of Paracentrotus lividus nectin. Mol Divers 2010, 14:653-665.
    • (2010) Mol Divers , vol.14 , pp. 653-665
    • Costa, C.1    Cavalcante, C.2    Zito, F.3    Yokota, Y.4    Matranga, V.5
  • 46
    • 0037320850 scopus 로고    scopus 로고
    • Of urchins and men: evolution of an alternative splicing unit in fibroblast growth factor receptor genes
    • Mistry N., Harrington W., Lasda E., Wagner E.J., Garcia-Blanco M.A. Of urchins and men: evolution of an alternative splicing unit in fibroblast growth factor receptor genes. RNA 2003, 9:209-217.
    • (2003) RNA , vol.9 , pp. 209-217
    • Mistry, N.1    Harrington, W.2    Lasda, E.3    Wagner, E.J.4    Garcia-Blanco, M.A.5
  • 47
    • 0026734267 scopus 로고
    • Developmental expression of echinonectin, an endogenous lectin of the sea urchin embryo
    • Fuhrman M.H., Suhan J.P., Ettensohn C.A. Developmental expression of echinonectin, an endogenous lectin of the sea urchin embryo. Develop Growth Differ 1992, 34:137-150.
    • (1992) Develop Growth Differ , vol.34 , pp. 137-150
    • Fuhrman, M.H.1    Suhan, J.P.2    Ettensohn, C.A.3
  • 48
    • 0026652444 scopus 로고
    • A new extracellular matrix protein of the sea urchin embryo with properties of a substrate adhesion molecule
    • Matranga V., Di Ferro D., Zito F., Cervello M., Nakano E. A new extracellular matrix protein of the sea urchin embryo with properties of a substrate adhesion molecule. Roux's Arch Dev Biol 1992, 201:173-178.
    • (1992) Roux's Arch Dev Biol , vol.201 , pp. 173-178
    • Matranga, V.1    Di Ferro, D.2    Zito, F.3    Cervello, M.4    Nakano, E.5
  • 49
    • 34648854455 scopus 로고    scopus 로고
    • The toposome, essential for sea urchin cell adhesion and development, is a modified iron-less calcium-binding transferring
    • Noll H., Alcedo J., Daube M., Frei E., Schiltz E., Hunt J., et al. The toposome, essential for sea urchin cell adhesion and development, is a modified iron-less calcium-binding transferring. Dev Biol 2007, 310:54-70.
    • (2007) Dev Biol , vol.310 , pp. 54-70
    • Noll, H.1    Alcedo, J.2    Daube, M.3    Frei, E.4    Schiltz, E.5    Hunt, J.6
  • 50
    • 33845421656 scopus 로고    scopus 로고
    • Interaction of toposome from sea-urchin yolk granules with dimyristoyl phosphatidylserine model membranes: a 2H-NMR study
    • Hayley M., Emberley J., Davis P.J., Morrow M.R., Robinson J.J. Interaction of toposome from sea-urchin yolk granules with dimyristoyl phosphatidylserine model membranes: a 2H-NMR study. Biophys J 2006, 91:4555-4564.
    • (2006) Biophys J , vol.91 , pp. 4555-4564
    • Hayley, M.1    Emberley, J.2    Davis, P.J.3    Morrow, M.R.4    Robinson, J.J.5
  • 51
    • 0022962210 scopus 로고
    • Functional characterization of toposomes from sea urchin blastula embryos by a morphogenetic cell aggregation assay
    • Matranga V., Kuwasakil K., Noll H. Functional characterization of toposomes from sea urchin blastula embryos by a morphogenetic cell aggregation assay. EMBO J 1986, 5(12):3125-3132.
    • (1986) EMBO J , vol.5 , Issue.12 , pp. 3125-3132
    • Matranga, V.1    Kuwasakil, K.2    Noll, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.