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Title: Functional site of endogenous phospholipase A2 inhibitor from python serum: Phospholipase A2 binding and anti-inflammatory activity
Authors: Thwin, M.-M.
Satish L. Ramapatna 
Chan, S.T.F.
Gopalakrishnakone, P.
Keywords: Anti-inflammatory peptide
Phospholipase A2 inhibitors
Phospholipase inhibitor from python PIP
Postsurgical adhesions
Protein-protein interaction
Issue Date: 2002
Citation: Thwin, M.-M., Satish L. Ramapatna, Chan, S.T.F., Gopalakrishnakone, P. (2002). Functional site of endogenous phospholipase A2 inhibitor from python serum: Phospholipase A2 binding and anti-inflammatory activity. European Journal of Biochemistry 269 (2) : 719-727. ScholarBank@NUS Repository.
Abstract: The functional site of 'phospholipase A2 inhibitor from python' (PIP) was predicted based on the hypothesis of proline brackets. Using different sources of secretory phospholipase A2 (sPLA2s) as enzyme, and [3H]arachidonate-labelled Escherichia coli as substrate, short synthetic peptides representing the proposed site were examined for their secretory phospholipase A2 (sPLA2) inhibitory activity. A decapeptide P-PB.III proved to be the most potent of the tested peptides in inhibiting sPLA2 enzymatic activity in vitro, and exhibited striking anti-inflammatory effects in vivo in a mouse paw oedema model. P-PB.III inhibited the enzymatic activity of class I, II and III PLA2s, including that of human synovial fluid from arthritis patients. When tested by ELISA, biotinylated P-PB.III interacted positively with various PLA2s, suggesting that the specific region of PIP corresponding to P-PB.III, is likely to be involved in the PLA2-PLI interaction. The effect of P-PB.III on the peritoneal inflammatory response after surgical trauma in rats was also examined. P-PB.III effectively reduced the extent of postsurgical peritoneal adhesions as compared to controls. sPLA2 levels at seventh postoperative day in the peritoneal tissue of P-PB.III-treated rats were also significantly reduced (P < 0.05) in comparison to those of the untreated controls. The present results shed additional insight on the essential structural elements for PLA2 binding, and may be useful as a basis for the design of novel therapeutic agents.
Source Title: European Journal of Biochemistry
ISSN: 00142956
Appears in Collections:Staff Publications

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