Plasma Kallikrein and Angiotensin I-converting enzyme N- and C-terminal domain activities are modulated by the insertion/deletion polymorphism

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dc.contributor.authorAlmeida, S. S. [UNIFESP]
dc.contributor.authorBarros, C. C. [UNIFESP]
dc.contributor.authorMoraes, M. R. [UNIFESP]
dc.contributor.authorRusso, F. J. [UNIFESP]
dc.contributor.authorHaro, A. S. [UNIFESP]
dc.contributor.authorRosa, T. S. [UNIFESP]
dc.contributor.authorAlves, M. F. [UNIFESP]
dc.contributor.authorPesquero, J. B. [UNIFESP]
dc.contributor.authorCarmona, A. K. [UNIFESP]
dc.contributor.authorBacurau, Reury Frank Pereira
dc.contributor.authorAraujo, R. C. [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2016-01-24T13:59:31Z
dc.date.available2016-01-24T13:59:31Z
dc.date.issued2010-04-01
dc.description.abstractAngiotensin I-converting enzyme (ACE) is recognized as one of the main effector molecules involved in blood pressure regulation. in the last few years some polymorphisms of ACE such as the insertion/deletion (I/D) polymorphism have been described, but their physiologic relevance is poorly understood. in addition, few studies investigated if the specific activity of ACE domain is related to the I/D polymorphism and if it can affect other systems. the aim of this study was to establish a biochemical and functional characterization of the I/D polymorphism and correlate this with the corresponding ACE activity. for this purpose, 119 male brazilian army recruits were genotyped and their ACE plasma activities evaluated from the C- and N-terminal catalytic domains using fluorescence resonance energy transfer (FRET) peptides, specific for the C-domain (Abz-LFK(Dnp)OH), N-domain (Abz-SDK(Dnp)P-OH) and both C- and N-domains (Abz-FRK(Dnp)P-OH). Plasma kallikrein activity was measured using Z-Phe-Arg-AMC as substrate and inhibited by selective plasma kallikrein inhibitor (PKSI). Some physiological parameters previously described related to the I/D polymorphism such as handgrip strength, blood pressure, heart rate and BMI were also evaluated. the genotype distribution was II n = 27, ID n = 64 and DD n = 28. Total plasma ACE activity of both domains in II individuals was significantly lower in comparison to ID and DD. This pattern was also observed for C- and N-domain activities. Difference between ID and DD subjects was observed only with the N-domain specific substrate. Blood pressure, heart rate, handgrip strength and BMI were similar among the genotypes. This polymorphism also affected the plasma kallikrein activity and DD group presents high activity level. Thus, our data demonstrate that the I/D ACE polymorphism affects differently both ACE domains without effects on handgrip strength. Moreover, this polymorphism influences the kallikrein-kinin system of normotensive individuals. (C) 2009 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biophys, São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Sch Arts Sci & Humanities, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biophys, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent139-143
dc.identifierhttp://dx.doi.org/10.1016/j.npep.2009.12.003
dc.identifier.citationNeuropeptides. Edinburgh: Churchill Livingstone, v. 44, n. 2, p. 139-143, 2010.
dc.identifier.doi10.1016/j.npep.2009.12.003
dc.identifier.issn0143-4179
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/32427
dc.identifier.wosWOS:000276001700012
dc.language.isoeng
dc.publisherChurchill Livingstone
dc.relation.ispartofNeuropeptides
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectAngiotensin I-converting enzymeen
dc.subjectI/D polymorphismen
dc.subjectPlasma kallikrein activityen
dc.subjectHandgrip strengthen
dc.titlePlasma Kallikrein and Angiotensin I-converting enzyme N- and C-terminal domain activities are modulated by the insertion/deletion polymorphismen
dc.typeinfo:eu-repo/semantics/article
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