Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L

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dc.contributor.authorPuzer, L.
dc.contributor.authorCotrin, S. S.
dc.contributor.authorAlves, MFM
dc.contributor.authorEgborge, T.
dc.contributor.authorAraujo, M. S.
dc.contributor.authorJuliano, M. A.
dc.contributor.authorJuliano, L.
dc.contributor.authorBromme, D.
dc.contributor.authorCarmona, A. K.
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionMt Sinai Sch Med
dc.date.accessioned2016-01-24T12:37:26Z
dc.date.available2016-01-24T12:37:26Z
dc.date.issued2004-10-15
dc.description.abstractCathepsins V and L have high identity and few structural differences. in this paper, we reported a comparative study of the hydrolytic activities of recombinant human cathepsins V and L using fluorescence resonance energy transfer peptides derived from Abz-KLRSSKQ-EDDnp (Abz = ortho-aminobenzoic acid and EDDnp = N-(2,4-dinitrophenyl)ethylenediamine). Five series of peptides were synthesized to map the S-3 to S'(2) subsites. the cathepsin V subsites S-1 and S-3 present a broad specificity while cathepsin L has preference for positively charged residues. the S-2 subsites of both enzymes require hydrophobic residues with preference for Phe and Leu. the S-1' and S-2' subsites of cathepsins V and L are less specific. Based on these data we designed substrates to explore the electrostatic potential differences of them. Finally, the kininogenase activities of these cathepsins were compared using synthetic human kininogen fragments. Cathepsin V preferentially released Lys-bradykinin while cathepsin L released bradykinin. This kininogenase activity by cathepsins V and L was also observed from human high and low molecular weight kininogens. (C) 2004 Elsevier Inc. All rights reserved.en
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 Biochem, BR-04044020 São Paulo, Brazil
dc.description.affiliationMt Sinai Sch Med, Dept Human Genet, New York, NY 10029 USA
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 Biochem, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent274-283
dc.identifierhttp://dx.doi.org/10.1016/j.abb.2004.07.006
dc.identifier.citationArchives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 430, n. 2, p. 274-283, 2004.
dc.identifier.doi10.1016/j.abb.2004.07.006
dc.identifier.issn0003-9861
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/27980
dc.identifier.wosWOS:000224104500019
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofArchives of Biochemistry and Biophysics
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectlysosomal proteasesen
dc.subjectcysteine proteasesen
dc.subjectcathepsin Len
dc.subjectcathepsin Ven
dc.subjectFluorogenic substratesen
dc.subjectbradykininen
dc.subjectkininogenen
dc.titleComparative substrate specificity analysis of recombinant human cathepsin V and cathepsin Len
dc.typeinfo:eu-repo/semantics/article
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