Cathepsin V, but not cathepsins L, B and K, may release angiostatin-like fragments from plasminogen

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dc.contributor.authorPuzer, Luciano
dc.contributor.authorBarros, Nilana M. T. [UNIFESP]
dc.contributor.authorPaschoalin, Thaysa [UNIFESP]
dc.contributor.authorHirata, Izaura Y. [UNIFESP]
dc.contributor.authorTanaka, Aparecida S. [UNIFESP]
dc.contributor.authorOliveira, Marcelo C.
dc.contributor.authorBroemme, Dieter
dc.contributor.authorCarmona, Adriana K. [UNIFESP]
dc.contributor.institutionUniv British Columbia
dc.contributor.institutionUniversidade Federal de São Carlos (UFSCar)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2016-01-24T13:49:34Z
dc.date.available2016-01-24T13:49:34Z
dc.date.issued2008-02-01
dc.description.abstractCathepsin V is a lysosomal cysteine peptidase highly expressed in corneal epithelium; however, its function in the eye is still unknown. Here, we describe the capability of cathepsin V to hydrolyze plasminogen, which is also expressed in human cornea at levels high enough to produce physiologically relevant amounts of angiostatin-related molecules. the co-localization of these two proteins suggests an important role for the enzyme in the maintenance of corneal avascularity, essential for optimal visual performance. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis of plasminogen digestion by cathepsin V revealed the generation of three major products of 60, 50 and 40 kDa, which were electrotransferred to polyvinylidene difluoride membranes and excised for characterization. NH2-terminal amino acid sequencing of these fragments revealed the sequences EKKVYL, TEQLAP and LLPNVE, respectively. These data are compatible with cleavage sites at plasminogen F94-E95, S358-T359 and V468-L469 peptide bonds generating fragments of the five-kringle domains. in contrast, we did not detect any plasminogen degradation by cathepsins B, K and L. Using a Matrigel assay, we confirmed the angiogenesis inhibition activity on endothelial cells caused by plasminogen processing by cathepsin V. Our results suggest a novel physiological role for cathepsin V related to the control of neovascularization in cornea.en
dc.description.affiliationUniv British Columbia, Fac Dent, Ctr Blood Res, Vancouver, BC V6T 1Z3, Canada
dc.description.affiliationUniv Fed Sao Carlos, Dept Genet & Evolut, BR-13565905 Sao Carlos, SP, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biochem, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Fac Med, Dept Ophthalmol, BR-01246000 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biochem, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent195-200
dc.identifierhttp://dx.doi.org/10.1515/BC.2008.020
dc.identifier.citationBiological Chemistry. Berlin: Walter de Gruyter & Co, v. 389, n. 2, p. 195-200, 2008.
dc.identifier.doi10.1515/BC.2008.020
dc.identifier.issn1431-6730
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/30441
dc.identifier.wosWOS:000252928800011
dc.language.isoeng
dc.publisherWalter de Gruyter & Co
dc.relation.ispartofBiological Chemistry
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectangiogenesisen
dc.subjectangiostatinen
dc.subjectcorneal epitheliumen
dc.subjectcysteine cathepsinsen
dc.subjectplasminogenen
dc.titleCathepsin V, but not cathepsins L, B and K, may release angiostatin-like fragments from plasminogenen
dc.typeinfo:eu-repo/semantics/article
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