Suppression of vascular endothelium hyperpermeability by cell-permeating peptide inhibitors of myosin light chain kinase

Autor:	Mikhail V. Samsonov, A. S. Molokoedov, A. A. Az’muko, Asker Y. Khapchaev, Olga A. Kazakova, Maria Sidorova, Elena L. Vilitkevich, Zh. D. Bespalova, Vladimir P. Shirinsky
Rok vydání:	2012
Předmět:	chemistry.chemical_classification Myosin light-chain kinase Endothelium Chemistry Cell Biophysics Peptide Cell biology Endothelial stem cell medicine.anatomical_structure Cell culture medicine Structure–activity relationship Peptide sequence
Zdroj:	Biophysics. 57:587-591
ISSN:	1555-6654 0006-3509
DOI:	10.1134/s0006350912050089
Popis:	Novel peptides originating from the peptide inhibitor of myosin light chain kinase (MLCK), L-PIK (Arg-Lys-Lys-Tyr-Lys-Tyr-Arg-Arg-Lys), have been studied for their ability to attenuate the thrombin-induced hyperpermeability of an endothelial cell monolayer in culture. Peptides [NαMeArg1]-Lys-Lys-Tyr-Lys-Tyr-Arg-(D)Arg8-Lys and H-Arg(NO2)Lys-Lys-Tyr-Lys-Tyr-Arg-Arg-Lys-NH2 (designated PIK2 and PIK4, respectively) appeared to be the most effective inhibitors of endothelial cell monolayer hyperpermeability, and surpassed other known peptide inhibitors of MLCK derived from original L-PIK. Our results validate PIK2 and PIK4 as the leading molecules for the development of novel drugs intended to counteract pathological hyperpermeability of vascular endothelium.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::af0f0d77e8b4126eab802d5a6715768d https://doi.org/10.1134/s0006350912050089 Zobrazit plný text záznamu Full text from SpringerLink