NDLI: Signal transduction pathways in erythrocyte nitric oxide metabolism under high fibrinogen levels

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Korea-Australia Rheology Journal : Volume 26, Issue 1, February 2014

Korea-Australia Rheology Journal : Volume 25

Korea-Australia Rheology Journal : Volume 24

Korea-Australia Rheology Journal : Volume 23

Signal transduction pathways in erythrocyte nitric oxide metabolism under high fibrinogen levels

Content Provider	Springer Nature Link
Author	Saldanha, Carlota Freitas, T. Lopez de Almeida, J. P. Silva Herdade, A.
Copyright Year	2014
Abstract	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-nitro-glutathione (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.
Starting Page	217
Ending Page	223
Page Count	7
File Format	PDF
ISSN	1226119X
Journal	Korea-Australia Rheology Journal
Volume Number	26
Issue Number	2
e-ISSN	20937660
Language	English
Publisher	Korean Society of Rheology, Australian Society of Rheology
Publisher Date	2014-06-01
Publisher Place	Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	nitric oxide erythrocyte fibrinogen CD47 4N1K Characterization and Evaluation of Materials Polymer Sciences Soft and Granular Matter, Complex Fluids and Microfluidics Mechanical Engineering Food Science
Content Type	Text
Resource Type	Article
Subject	Condensed Matter Physics Materials Science

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