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dc.contributor.authorNakahata, Adriana Miti [UNIFESP]
dc.contributor.authorBueno, Norlene Regina [UNIFESP]
dc.contributor.authorRocha, Hugo Alexandre de Oliveira
dc.contributor.authorFranco, Celia Regina Cavichiolo
dc.contributor.authorChammas, Roger
dc.contributor.authorNakaie, Clovis Ryuichi [UNIFESP]
dc.contributor.authorJasiulionis, Miriam Galvonas [UNIFESP]
dc.contributor.authorNader, Helena Bonciani [UNIFESP]
dc.contributor.authorSantana, Lucimeire Aparecida de [UNIFESP]
dc.contributor.authorSampaio, Misako Uemura [UNIFESP]
dc.contributor.authorOliva, Maria Luiza Vilela [UNIFESP]
dc.date.accessioned2016-01-24T12:41:40Z
dc.date.available2016-01-24T12:41:40Z
dc.date.issued2006-12-15
dc.identifierhttps://dx.doi.org/10.1016/j.ijbiomac.2006.05.008
dc.identifier.citationInternational Journal of Biological Macromolecules. Amsterdam: Elsevier B.V., v. 40, n. 1, p. 22-29, 2006.
dc.identifier.issn0141-8130
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/29314
dc.description.abstractPurified from Bauhinia rufa seeds, BrTI is a Kunitz proteinase inhibitor that contains the RGD sequence. BrTI inhibits trypsin (K-iapp 2.9 nM) and human plasma kallikrein (K-iapp 14.0 nM) but not other related enzymes. the synthetic peptide YLEPVARGDGGLA-NH2 (70 mu M) inhibited the adhesion to fibronectin of B16F10 (high-metastatic B16 murine mouse melanoma cell line) and of Tm5 (murine melanoma cell lines derived from a non-tumorigenic lineage of pigmented murine melanocytes, melan-a). YLEPVARGEGGLA-NH2 in which Asp(9) was changed into Glu does not affect the cell attachment. Moreover, this peptide was functional only when the sequence present in the native protein was preserved, since YLIPVARGDGGLA-NH2 in which Glu(3) was changed into Ile does not interfere with B16F10 and was less effective on Tm5 cell line adhesion. Neither YLEPVARGDGGLA-NH2, YLIPVARGDGGLA-NH2 or YLEPVARGEGGLA-NH2 inhibit the interaction of RAEC (endothelial cell line from rabbit aorta) with fibronectin. (c) 2006 Elsevier B.V. All rights reserved.en
dc.format.extent22-29
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofInternational Journal of Biological Macromolecules
dc.rightsAcesso restrito
dc.subjectBauhiniaen
dc.subjectElastaseen
dc.subjectCell adhesionen
dc.subjectMelanomaen
dc.subjectRGDen
dc.subjectTrypsin inhibitoren
dc.subjectTumoren
dc.titleStructural and inhibitory properties of a plant proteinase inhibitor containing the RGD motifen
dc.typeArtigo
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Fed Rio Grande Norte
dc.contributor.institutionUniv Fed Parana
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biochem, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniv Fed Rio Grande Norte, Dept Biochem, BR-59072970 Natal, RN, Brazil
dc.description.affiliationUniv Fed Parana, Dept Biol Celular, BR-80060000 Curitiba, Parana, Brazil
dc.description.affiliationUniv São Paulo, Fac Med, Dept Radiat Oncol, BR-01246904 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Imunol, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biochem, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Imunol, BR-04044020 São Paulo, Brazil
dc.identifier.doi10.1016/j.ijbiomac.2006.05.008
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000243052100004


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