Please use this identifier to cite or link to this item:
Title: Functional site of endogenous phospholipase A2 inhibitor from python serum: Phospholipase A2 binding and anti-inflammatory activity
Authors: Thwin, M.-M.
Satish, R.L. 
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
Source: Thwin, M.-M., Satish, R.L., 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
DOI: 10.1046/j.0014-2956.2001.02711.x
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.


checked on Feb 27, 2018


checked on Feb 14, 2018

Page view(s)

checked on Mar 12, 2018

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.