메뉴 건너뛰기




Volumn 148, Issue 3, 2007, Pages 231-244

Epidermal secretions of terrestrial flatworms and slugs: Lehmannia valentiana mucus contains matrilin-like proteins

Author keywords

Adhesive locomotion; Flatworm; Gastropod; Glycosaminoglycan; Lehmannia valentiana; Limax valentianus; Tricladida; von Willebrand factor A domain

Indexed keywords

CARBOHYDRATE; COMPLEMENTARY DNA; EPIDERMAL GROWTH FACTOR; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; MATRILIN LIKE PROTEIN; PROTEIN; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR;

EID: 35448949632     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2007.06.001     Document Type: Article
Times cited : (28)

References (58)
  • 1
    • 35448950756 scopus 로고    scopus 로고
    • Abad, R., 1996. Therapeutic and cosmetic compositions for treatment of skin. US Patent 5538740.
  • 2
    • 35448948200 scopus 로고    scopus 로고
    • Aitken, A., 1996. Protein chemistry methods, post-translational modification, consensus sequences. In: Price, N.C. (Ed.), Proteins LabFax, Bios/Academic Press, Oxford, UK, pp.253-285.
  • 4
    • 1842714390 scopus 로고    scopus 로고
    • Partial characterisation of high-molecular weight glycoconjugates in the trail mucus of the freshwater pond snail Lymnaea stagnalis
    • Ballance S., Howard M., White K.N., McCrohan C.R., Thornton D.J., and Sheehan J.K. Partial characterisation of high-molecular weight glycoconjugates in the trail mucus of the freshwater pond snail Lymnaea stagnalis. Comp. Biochem. Physiol. B 137 (2004) 475-486
    • (2004) Comp. Biochem. Physiol. B , vol.137 , pp. 475-486
    • Ballance, S.1    Howard, M.2    White, K.N.3    McCrohan, C.R.4    Thornton, D.J.5    Sheehan, J.K.6
  • 5
    • 0029969360 scopus 로고    scopus 로고
    • The C-terminal domain of cartilage matrix protein assembles into a triple-stranded alpha-helical coiled-coil structure
    • Beck K., Gambee J.E., Bohan C.A., and Bachinger H.P. The C-terminal domain of cartilage matrix protein assembles into a triple-stranded alpha-helical coiled-coil structure. J. Mol. Biol. 256 (1996) 909-923
    • (1996) J. Mol. Biol. , vol.256 , pp. 909-923
    • Beck, K.1    Gambee, J.E.2    Bohan, C.A.3    Bachinger, H.P.4
  • 6
    • 32144461370 scopus 로고    scopus 로고
    • Compatibility in the Biomphalaria glabrata/Echinostoma caproni model: potential involvement of adhesion genes
    • Bouchut A., Roger E., Coustau C., Gourbal B., and Mitta G. Compatibility in the Biomphalaria glabrata/Echinostoma caproni model: potential involvement of adhesion genes. Int. J. Parasitol. 36 (2006) 175-184
    • (2006) Int. J. Parasitol. , vol.36 , pp. 175-184
    • Bouchut, A.1    Roger, E.2    Coustau, C.3    Gourbal, B.4    Mitta, G.5
  • 8
    • 0032815792 scopus 로고    scopus 로고
    • Assembly of a novel cartilage matrix protein filamentous network: molecular basis of differential requirement of von Willebrand factor A domains
    • Chen Q., Zhang Y., Johnson D.M., and Goetinck P.F. Assembly of a novel cartilage matrix protein filamentous network: molecular basis of differential requirement of von Willebrand factor A domains. Mol. Biol. Cell 10 (1999) 2149-2162
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2149-2162
    • Chen, Q.1    Zhang, Y.2    Johnson, D.M.3    Goetinck, P.F.4
  • 9
    • 0027466071 scopus 로고
    • Evidence for GAGs as a major component of trail mucus from the terrestrial slug, Arion ater L
    • Cottrell J.M., Henderson I.F., Pickett J.A., and Wright D.J. Evidence for GAGs as a major component of trail mucus from the terrestrial slug, Arion ater L. Comp. Biochem. Physiol. B 104 (1993) 455-468
    • (1993) Comp. Biochem. Physiol. B , vol.104 , pp. 455-468
    • Cottrell, J.M.1    Henderson, I.F.2    Pickett, J.A.3    Wright, D.J.4
  • 10
    • 0028121023 scopus 로고
    • Studies on the GAG component of trail mucus from the terrestrial slug, Arion ater L
    • Cottrell J.M., Henderson I.F., and Wright D.J. Studies on the GAG component of trail mucus from the terrestrial slug, Arion ater L. Comp. Biochem. Physiol. B 107 (1994) 285-296
    • (1994) Comp. Biochem. Physiol. B , vol.107 , pp. 285-296
    • Cottrell, J.M.1    Henderson, I.F.2    Wright, D.J.3
  • 11
    • 0040973727 scopus 로고    scopus 로고
    • The matrilins: a novel family of oligomeric extracellular matrix proteins
    • Deak F., Wagener R., Kiss I., and Paulsson M. The matrilins: a novel family of oligomeric extracellular matrix proteins. Matrix Biol. 18 (1999) 55-64
    • (1999) Matrix Biol. , vol.18 , pp. 55-64
    • Deak, F.1    Wagener, R.2    Kiss, I.3    Paulsson, M.4
  • 13
    • 0001355493 scopus 로고
    • Molecular biomechanics of molluscan mucous secretions
    • Hochachka P.W. (Ed), Academic Press, N.Y.
    • Denny M.W. Molecular biomechanics of molluscan mucous secretions. In: Hochachka P.W. (Ed). The Molluska vol. 1 (1983), Academic Press, N.Y. 431-465
    • (1983) The Molluska , vol.1 , pp. 431-465
    • Denny, M.W.1
  • 14
    • 0024812526 scopus 로고
    • Invertebrate mucous secretions: functional alternatives to vertebrate paradigms
    • Denny M.W. Invertebrate mucous secretions: functional alternatives to vertebrate paradigms. Symp. Soc. Exp. Biol. 43 (1989) 337-366
    • (1989) Symp. Soc. Exp. Biol. , vol.43 , pp. 337-366
    • Denny, M.W.1
  • 15
    • 0030443596 scopus 로고    scopus 로고
    • Product release by mucous granules of land slugs. 2. Species diversity in triggering of mucous granule rupture
    • Deyrup-Olsen I. Product release by mucous granules of land slugs. 2. Species diversity in triggering of mucous granule rupture. J. Exp. Biol. 276 (1996) 330-334
    • (1996) J. Exp. Biol. , vol.276 , pp. 330-334
    • Deyrup-Olsen, I.1
  • 17
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois M., Gilles K.A., Hamilton J.K., Rebers P.A., and Smith F. Colorimetric method for determination of sugars and related substances. Anal. Chem. 28 (1956) 199-200
    • (1956) Anal. Chem. , vol.28 , pp. 199-200
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 21
    • 34248139762 scopus 로고    scopus 로고
    • Rheological fingerprinting of gastropod pedal mucus and synthetic complex fluids for biomimicking adhesive locomotion
    • Ewoldt R.H., Clasen C., Hosoi A.E., and McKinley G.H. Rheological fingerprinting of gastropod pedal mucus and synthetic complex fluids for biomimicking adhesive locomotion. Soft Matter 3 (2007) 634-643
    • (2007) Soft Matter , vol.3 , pp. 634-643
    • Ewoldt, R.H.1    Clasen, C.2    Hosoi, A.E.3    McKinley, G.H.4
  • 22
    • 0023248639 scopus 로고
    • A heparin-binding domain of human von Willebrand factor. Characterization and localization to a tryptic fragment extending from amino acid residue Val-449 to Lys-728
    • Fujimura Y., Titani K., Holland L.Z., Roberts J.R., Kostel P., Ruggeri Z.M., and Zimmerman T.S. A heparin-binding domain of human von Willebrand factor. Characterization and localization to a tryptic fragment extending from amino acid residue Val-449 to Lys-728. J. Biol. Chem. 262 (1987) 1734-1739
    • (1987) J. Biol. Chem. , vol.262 , pp. 1734-1739
    • Fujimura, Y.1    Titani, K.2    Holland, L.Z.3    Roberts, J.R.4    Kostel, P.5    Ruggeri, Z.M.6    Zimmerman, T.S.7
  • 23
    • 35448991560 scopus 로고    scopus 로고
    • Graham, L.D., 2005. Biological adhesives from nature. In: Encyclopedia of Biomaterials and Biomedical Engineering, Eds. Wnek, G. and Bowlin, G., Marcel Dekker/Taylor and Francis, New York. Online entry, URL: http://www.dekker.com/sdek/abstract~db=enc~content=a713609104.
  • 24
    • 0029551209 scopus 로고
    • Inhibition of platelet heparitinase by phosphorothioate DNA oligonucleotides
    • Graham L.D., Mitchell S.M., and Underwood P.A. Inhibition of platelet heparitinase by phosphorothioate DNA oligonucleotides. Biochem. Mol. Biol. Int. 37 (1995) 239-246
    • (1995) Biochem. Mol. Biol. Int. , vol.37 , pp. 239-246
    • Graham, L.D.1    Mitchell, S.M.2    Underwood, P.A.3
  • 26
    • 35449002727 scopus 로고    scopus 로고
    • Greff, D., 1987. Cosmetic composition containing gastropod glycoprotein, extracted from the mucus and digestive juices, with skin moisturising action. French Patent 2595247.
  • 27
    • 2542484581 scopus 로고    scopus 로고
    • Isolation and evaluation of dextral-specific and dextral-enriched cDNA clones as candidates for the handedness-determining gene in a freshwater gastropod, Lymnaea stagnalis
    • Harada Y., Hosoiri Y., and Kuroda R. Isolation and evaluation of dextral-specific and dextral-enriched cDNA clones as candidates for the handedness-determining gene in a freshwater gastropod, Lymnaea stagnalis. Dev. Genes Evol. 214 (2004) 159-169
    • (2004) Dev. Genes Evol. , vol.214 , pp. 159-169
    • Harada, Y.1    Hosoiri, Y.2    Kuroda, R.3
  • 28
    • 0037032767 scopus 로고    scopus 로고
    • Large amplitude oscillatory shear as a way to classify the complex fluids
    • Hyun K., Kim S.H., Ahn K.H., and Lee S.J. Large amplitude oscillatory shear as a way to classify the complex fluids. J. Non-Newton. Fluid Mech. 107 (2002) 51-65
    • (2002) J. Non-Newton. Fluid Mech. , vol.107 , pp. 51-65
    • Hyun, K.1    Kim, S.H.2    Ahn, K.H.3    Lee, S.J.4
  • 29
  • 30
    • 0035366508 scopus 로고    scopus 로고
    • Novel barnacle underwater adhesive protein is a charged amino acid-rich protein constituted by a Cys-rich repetitive sequence
    • Kamino K. Novel barnacle underwater adhesive protein is a charged amino acid-rich protein constituted by a Cys-rich repetitive sequence. Biochem. J. 356 (2001) 503-507
    • (2001) Biochem. J. , vol.356 , pp. 503-507
    • Kamino, K.1
  • 33
    • 14844296487 scopus 로고    scopus 로고
    • Zebrafish (Danio rerio) matrilins: shared and divergent characteristics with their mammalian counterparts
    • Ko Y.P., Kobbe B., Paulsson M., and Wagener R. Zebrafish (Danio rerio) matrilins: shared and divergent characteristics with their mammalian counterparts. Biochem. J. 386 (2005) 367-379
    • (2005) Biochem. J. , vol.386 , pp. 367-379
    • Ko, Y.P.1    Kobbe, B.2    Paulsson, M.3    Wagener, R.4
  • 34
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)
    • Lee J.O., Rieu P., Arnaout M.A., and Liddington R. Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 80 (1995) 631-638
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 35
    • 35448995554 scopus 로고    scopus 로고
    • Development of slug slime into an adhesive
    • Fall/Winter issue
    • Lee S., and Liu I. Development of slug slime into an adhesive. Can. J. High School Sci. (2001) 23-26 Fall/Winter issue
    • (2001) Can. J. High School Sci. , pp. 23-26
    • Lee, S.1    Liu, I.2
  • 36
    • 34547535343 scopus 로고    scopus 로고
    • Li, D., Graham, L.D., in press. Epiphragmin, the major protein of epiphragm mucus from the vineyard snail, Cernuella virgata. Comp. Biochem. Physiol. B. doi:10.1016/j.cbpb.2007.05.009.
  • 37
    • 0025940727 scopus 로고
    • Ultrastructure and lysis of mucin-containing granules in epidermal secretions of the terrestrial slug, Ariolimax columbianus (Mollusca, Gastropoda, Pulmonata)
    • Luchtel D.L., Deyrup-Olsen I., and Martin A.W. Ultrastructure and lysis of mucin-containing granules in epidermal secretions of the terrestrial slug, Ariolimax columbianus (Mollusca, Gastropoda, Pulmonata). Cell Tissue Res. 266 (1991) 375-383
    • (1991) Cell Tissue Res. , vol.266 , pp. 375-383
    • Luchtel, D.L.1    Deyrup-Olsen, I.2    Martin, A.W.3
  • 40
    • 0002707025 scopus 로고
    • DNA
    • Gribskov M., and Devereux J. (Eds), W.H. Freeman, New York
    • Rice P.M., Elliston K., and Gribskov M. DNA. In: Gribskov M., and Devereux J. (Eds). Sequence Analysis Primer (1992), W.H. Freeman, New York 1-59
    • (1992) Sequence Analysis Primer , pp. 1-59
    • Rice, P.M.1    Elliston, K.2    Gribskov, M.3
  • 42
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • Sadler J.E. Biochemistry and genetics of von Willebrand factor. Ann. Rev. Biochem. 67 (1998) 395-424
    • (1998) Ann. Rev. Biochem. , vol.67 , pp. 395-424
    • Sadler, J.E.1
  • 45
    • 0037730289 scopus 로고    scopus 로고
    • The structure and function of adhesive gels from invertebrates
    • Smith A.M. The structure and function of adhesive gels from invertebrates. Integr. Comp. Biol. 42 (2002) 1164-1171
    • (2002) Integr. Comp. Biol. , vol.42 , pp. 1164-1171
    • Smith, A.M.1
  • 46
    • 33751167773 scopus 로고    scopus 로고
    • The biochemistry and mechanics of gastropod adhesive gels
    • Smith A.M., and Callow J.A. (Eds), Springer-Verlag, Berlin
    • Smith A.M. The biochemistry and mechanics of gastropod adhesive gels. In: Smith A.M., and Callow J.A. (Eds). Biological Adhesives (2006), Springer-Verlag, Berlin 167-182
    • (2006) Biological Adhesives , pp. 167-182
    • Smith, A.M.1
  • 47
    • 0036965269 scopus 로고    scopus 로고
    • Biochemical differences between trail mucus and adhesive mucus from marsh periwinkle snails
    • Smith A.M., and Morin M.C. Biochemical differences between trail mucus and adhesive mucus from marsh periwinkle snails. Biol. Bull. 203 (2002) 338-346
    • (2002) Biol. Bull. , vol.203 , pp. 338-346
    • Smith, A.M.1    Morin, M.C.2
  • 48
    • 0026484847 scopus 로고
    • Structure of recombinant N-terminal globule of type VI collagen alpha 3 chain and its binding to heparin and hyaluronan
    • Specks U., Mayer U., Nischt R., Spissinger T., Mann K., Timpl R., Engel J., and Chu M.L. Structure of recombinant N-terminal globule of type VI collagen alpha 3 chain and its binding to heparin and hyaluronan. EMBO J. 11 (1992) 4281-4290
    • (1992) EMBO J. , vol.11 , pp. 4281-4290
    • Specks, U.1    Mayer, U.2    Nischt, R.3    Spissinger, T.4    Mann, K.5    Timpl, R.6    Engel, J.7    Chu, M.L.8
  • 50
    • 0036281347 scopus 로고    scopus 로고
    • The physical and chemical microstructure of the Achatina fulica epiphragm
    • Struthers M., Rosair G., Buckman J., and Viney C. The physical and chemical microstructure of the Achatina fulica epiphragm. J. Molluscan Stud. 68 (2002) 165-171
    • (2002) J. Molluscan Stud. , vol.68 , pp. 165-171
    • Struthers, M.1    Rosair, G.2    Buckman, J.3    Viney, C.4
  • 51
    • 0036856907 scopus 로고    scopus 로고
    • Collagen-binding matrix proteins from elastomeric extraorganismic byssal fibers
    • Sun C.J., Lucas J.M., and Waite J.H. Collagen-binding matrix proteins from elastomeric extraorganismic byssal fibers. Biomacromolecules 3 (2002) 1240-1248
    • (2002) Biomacromolecules , vol.3 , pp. 1240-1248
    • Sun, C.J.1    Lucas, J.M.2    Waite, J.H.3
  • 52
    • 0034326357 scopus 로고    scopus 로고
    • Elastomeric proteins: biological roles, structures and mechanisms
    • Tatham A.S., and Shewry P.R. Elastomeric proteins: biological roles, structures and mechanisms. Trends Biochem. Sci. 25 (2000) 567-571
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 567-571
    • Tatham, A.S.1    Shewry, P.R.2
  • 53
    • 1342343931 scopus 로고    scopus 로고
    • Acharan sulfate, the new GAG from Achatina fulica Bowdich 1822. Structural heterogeneity, metabolic labeling and localization in the body, mucus and the organic shell matrix
    • Vieira T.C., Costa-Filho A., Salgado N.C., Allodi S., Valente A.P., Nasciutti L.E., and Silva L.C. Acharan sulfate, the new GAG from Achatina fulica Bowdich 1822. Structural heterogeneity, metabolic labeling and localization in the body, mucus and the organic shell matrix. Eur. J. Bicohem. 271 (2004) 845-854
    • (2004) Eur. J. Bicohem. , vol.271 , pp. 845-854
    • Vieira, T.C.1    Costa-Filho, A.2    Salgado, N.C.3    Allodi, S.4    Valente, A.P.5    Nasciutti, L.E.6    Silva, L.C.7
  • 54
    • 0033377652 scopus 로고    scopus 로고
    • Mucus liquid crystallinity: is function related to microstructural domain size?
    • Viney C. Mucus liquid crystallinity: is function related to microstructural domain size?. Biorheology 36 (1999) 319-323
    • (1999) Biorheology , vol.36 , pp. 319-323
    • Viney, C.1
  • 55
    • 0038067927 scopus 로고    scopus 로고
    • Adhesion a la moule
    • Waite J.H. Adhesion a la moule. Integr. Comp. Biol. 42 (2002) 1172-1180
    • (2002) Integr. Comp. Biol. , vol.42 , pp. 1172-1180
    • Waite, J.H.1
  • 56
    • 0001939427 scopus 로고
    • On the variation, nomenclature, distribution, and taxonomical position of Limax (Lehmannia) valentianus Férussac (Gastropoda, Pulmonata)
    • Waldén H.W. On the variation, nomenclature, distribution, and taxonomical position of Limax (Lehmannia) valentianus Férussac (Gastropoda, Pulmonata). Ark. Zool. 15 (1961) 71-95
    • (1961) Ark. Zool. , vol.15 , pp. 71-95
    • Waldén, H.W.1
  • 57
    • 0031423820 scopus 로고    scopus 로고
    • Immunocytochemical localisation of GAG-like activity in the mucus and associated tissues of terrestrial slug species (Gastropoda : Pulmonata)
    • Wright D.J., Matthews C.L., Donaldson I., Martin A.P., and Henderson I.F. Immunocytochemical localisation of GAG-like activity in the mucus and associated tissues of terrestrial slug species (Gastropoda : Pulmonata). Comp. Biochem. Physiol. B 118 (1997) 825-828
    • (1997) Comp. Biochem. Physiol. B , vol.118 , pp. 825-828
    • Wright, D.J.1    Matthews, C.L.2    Donaldson, I.3    Martin, A.P.4    Henderson, I.F.5
  • 58
    • 0031927574 scopus 로고    scopus 로고
    • Cloning and sequencing of three C-type lectins from body surface mucus of the land slug, Incilaria fruhstorferi
    • Yuasa H.J., Furuta E., Nakamura A., and Takagi T. Cloning and sequencing of three C-type lectins from body surface mucus of the land slug, Incilaria fruhstorferi. Comp. Biochem. Physiol. B 119 (1998) 478-484
    • (1998) Comp. Biochem. Physiol. B , vol.119 , pp. 478-484
    • Yuasa, H.J.1    Furuta, E.2    Nakamura, A.3    Takagi, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.