Abstract
Calpain, a Ca2+-dependent neutral protease, is highly related to the pathogenesis of a variety of disorders and its inhibitors offer potential for therapeutic intervention. General calpain inhibitors, however, have the disadvantage of a lack of specificity or poor cellular permeability or oxidization under physiological conditions. Here, we developed a membrane-permeable specific calpain inhibitor by fusing calpastatin peptide (CS) and 11 poly-arginine peptides (11R). The 11R-fused CS (11R-CS) effectively penetrated across the plasma membrane of living neurons and significantly inhibited calpain activity in the cells.
| Original language | English |
|---|---|
| Pages (from-to) | 131-135 |
| Number of pages | 5 |
| Journal | Neuroscience Research |
| Volume | 47 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Sep 1 2003 |
| Externally published | Yes |
Keywords
- Apoptosis
- Calpain
- Calpastatin
- Neuronal cell death
- Poly-arginine peptides
- Tat
ASJC Scopus subject areas
- Neuroscience(all)
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Cite this
Wu, H. Y., Tomizawa, K., Matsushita, M., Lu, Y. F., Li, S. T., & Matsui, H. (2003). Poly-arginine-fused calpastatin peptide, a living cell membrane-permeable and specific inhibitor for calpain. Neuroscience Research, 47(1), 131-135. https://doi.org/10.1016/S0168-0102(03)00195-0