[Myr-RKEFAK Peptide Selectively Regulates Outside-in Signaling Transduction-related Functions in Human Platelets].
Zhongguo Shi Yan Xue Ye Xue Za Zhi
; 23(3): 761-7, 2015 Jun.
Article
em Zh
| MEDLINE
| ID: mdl-26117033
ABSTRACT
OBJECTIVE:
To study the effect of interaction of the talin rod domain integrin binding site 2 with integrin ß3 on platelet signal transduction.METHODS:
A peptide that mimics the membrane proximal α helix 6 residues R724 KEFAK729 of the integrin ß3 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.RESULTS:
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.CONCLUSION:
The cell-penetrating peptide myr-RKEFAK causes an inhibitory effect on integrin ß3 outside-in signaling-regulated platelets functions, but did not affect inside-out signaling-regulated platelets functions.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Plaquetas
/
Transdução de Sinais
Limite:
Humans
Idioma:
Zh
Ano de publicação:
2015
Tipo de documento:
Article