| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8295117 | Biochemical and Biophysical Research Communications | 2018 | 25 Pages |
Abstract
A 75 kDa serine protease having prolyl oligopeptidase activity has been purified from Setaria cervi, a bovine filarial parasite. The MALDI-MS/MS analysis of the purified protein revealed 6 peptides showing nearest match S9A (prolyl oligopeptidase) family protein from Plesiocystis pacifica. The ScPOP was found to be unique compared to mammalian POP with respect to its kinetic properties. To elucidate its role, filarial parasites were exposed to specific inhibitor of POP, Z-Pro-prolinal (ZPP) for 8â¯h. The inhibition of POP induced calcium signaling via phospholipase c stimulation which further triggered mitochondrial mediated apoptosis in filarial parasites.
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Authors
Mohit Wadhawan, Savitri Tiwari, Shweta Sharma, Sushma Rathaur,