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A new cell-penetrating peptide that blocks the autoinhibitory XIP domain of NCX1 and enhances antiporter activity.

Mol. Ther.. 2015-03; 
Molinaro Pasquale,Pannaccione Anna,Sisalli Maria José,Secondo Agnese,Cuomo Ornella,Sirabella Rossana,Cantile Maria,Ciccone Roselia,Scorziello Antonella,di Renzo Gianfranco,Annunziato L
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Proteins, Expression, Isolation and Analysis P1Flag protein was expressed in Escherichia coli BL21 and purified to >85% from inclusion bodies by GenScript, Hong Kong, China...The primary antibody for western blot was mouse-anti-his mAb (GenScript; Cat.No.A00186). Get A Quote

摘要

The plasma membrane Na(+)/Ca(2+) exchanger (NCX) is a high-capacity ionic transporter that exchanges 3Na(+) ions for 1Ca(2+) ion. The first 20 amino acids of the f-loop, named exchanger inhibitory peptide (XIP(NCX1)), represent an autoinhibitory region involved in the Na(+)-dependent inactivation of the exchanger. Previous research has shown that an exogenous peptide having the same amino acid sequence as the XIP(NCX1) region exerts an inhibitory effect on NCX activity. In this study, we identified another regulatory peptide, named P1, which corresponds to the 562-688aa region of the exchanger. Patch-clamp analysis revealed that P1 increased the activity of the exchanger, whereas the XIP inhibited i... More

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