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RISS 인기검색어
- 검색키워드
- 저자 : Carlota Saldanha (검색결과 2 건)
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Signal transduction pathways in erythrocyte nitric oxide metabolism under high fibrinogen levels
Saldanha, Carlota,Freitas, T.,de Almeida, J.P. Lopez,Silva-Herdade, A. 한국유변학회 2014 Korea-Australia rheology journal Vol.26 No.2
Previous studies show that the fibrinogen molecule modulates the metabolism of nitric oxide (NO) in erythrocyte. The in vitro induced hiperfibrinogenemia interferes in the metabolism of the NO in the erythrocyte in dependence of the phosphorylation degree of the band 3. The soluble form of fibrinogen binds into CD47 protein present in the erythrocyte membrane. The soluble thrombomodulin is an inflammatory marker that binds to the erythrocyte CD47 in a site with a sequence peptide known as 4N1K. A study done in vitro shows that when hiperfibrinogenemia was induced in the presence of the peptide 4N1K agonist of CD47 it were observed variations in the efflux of NO from erythrocyte and an increase in the concentrations of GSNO, peroxinitrite, nitrite and nitrate of the erythrocytes. The aim of this work was to study the influence of the peptide 4N1K, on the metabolism of NO in the erythrocyte under high fibrinogen concentration and in the presence of inhibitors of the status of phosphorylation of protein band 3. In this in vitro study, whole blood samples were harvested from healthy subjects and NO, peroxynitrite, nitrite, nitrate and S-nitroglutathione (GSNO) were determined in presence of 4N1K, calpeptine, Syk inhibitor and under high fibrinogen concentrations. The results obtained in erythrocytes under high fibrinogen levels when 4N1K is present with the Syk inhibitor or with calpeptine, showed in relation to the control samples increased significant concentrations of efflux of NO and of peroxynitrite, nitrite, nitrate and GSNO. In conclusion it was verified that in the in vitro model of hiperfibrinogenemia the peptide 4N1K, agonist of CD47, induces mobilization of NO in the erythrocyte in dependence of the status of phosphorylation of protein band 3.
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Signal transduction pathways in erythrocyte nitric oxide metabolism under high fibrinogen levels
Carlota Saldanha,T. Freitas,J.P. Lopez de Almeida,A. Silva-Herdade 한국유변학회 2014 Korea-Australia rheology journal Vol.26 No.2
Previous studies show that the fibrinogen molecule modulates the metabolism of nitric oxide (NO) in erythrocyte. The in vitro induced hiperfibrinogenemia interferes in the metabolism of the NO in the erythrocytein dependence of the phosphorylation degree of the band 3. The soluble form of fibrinogen binds into CD47protein present in the erythrocyte membrane. The soluble thrombomodulin is an inflammatory marker thatbinds to the erythrocyte CD47 in a site with a sequence peptide known as 4N1K. A study done in vitroshows that when hiperfibrinogenemia was induced in the presence of the peptide 4N1K agonist of CD47it were observed variations in the efflux of NO from erythrocyte and an increase in the concentrations ofGSNO, peroxinitrite, nitrite and nitrate of the erythrocytes. The aim of this work was to study the influenceof the peptide 4N1K, on the metabolism of NO in the erythrocyte under high fibrinogen concentration andin the presence of inhibitors of the status of phosphorylation of protein band 3. In this in vitro study, wholeblood samples were harvested from healthy subjects and NO, peroxynitrite, nitrite, nitrate and S-nitroglutathione(GSNO) were determined in presence of 4N1K, calpeptine, Syk inhibitor and under high fibrinogenconcentrations. The results obtained in erythrocytes under high fibrinogen levels when 4N1K ispresent with the Syk inhibitor or with calpeptine, showed in relation to the control samples increased significantconcentrations of efflux of NO and of peroxynitrite, nitrite, nitrate and GSNO. In conclusion it wasverified that in the in vitro model of hiperfibrinogenemia the peptide 4N1K, agonist of CD47, induces mobilizationof NO in the erythrocyte in dependence of the status of phosphorylation of protein band 3.
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