Myr-RKEFAK Peptide Selectively Regulates Outside-in Signaling Transduction-related Functions in Human Platelets / 中国实验血液学杂志
Journal of Experimental Hematology
;
(6): 761-767, 2015.
Artigo
em Chinês
| WPRIM
| ID: wpr-357275
ABSTRACT
<p><b>OBJECTIVE</b>To study the effect of interaction of the talin rod domain integrin binding site 2 with integrin β3 on platelet signal transduction.</p><p><b>METHODS</b>A peptide that mimics the membrane proximal α helix 6 residues R724 KEFAK729 of the integrin β3 cytoplasmic tails was designed and synthesized, to which the myristoylation was covalently linked to the N-terminal of the peptide enabling membrane penetration. The effects of myr-RKEFAK peptide on the typical platelet outside-in signaling ovent (stable adhesion and spreading on immobilized fibrinogen, aggregation, fibrin clot retraction) and inside-out signaling events (soluble fibrinogen binding) were tested.</p><p><b>RESULTS</b>myr-RKEFAK peptide dose-dependently inhibited platelet stable adhesion and spreading on immobilized fibrinogen, irreversible aggregation, as well as fibrin clot retraction, but not soluble fibrinogen binding and reversible phase of platelet aggregation.</p><p><b>CONCLUSION</b>The cell-penetrating peptide myr-RKEFAK causes an inhibitory effect on integrin β3 outside-in signaling-regulated platelets functions, but did not affect inside-out signaling-regulated platelets functions.</p>
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Peptídeos
/
Plaquetas
/
Fibrinogênio
/
Transdução de Sinais
/
Adesividade Plaquetária
/
Agregação Plaquetária
/
Integrina beta3
Limite:
Humanos
Idioma:
Chinês
Revista:
Journal of Experimental Hematology
Ano de publicação:
2015
Tipo de documento:
Artigo
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