Please use this identifier to cite or link to this item: https://doi.org/10.1042/BJ20130599
Title: Characterization of inflamin, the first member of a new family of snake venom proteins that induces inflammation
Authors: Barnwal, B.
Kini, R.M. 
Keywords: Cyclo-oxygenase
Cytotoxic
Inflammation
Oedema
Prostacyclin
Issue Date: 15-Oct-2013
Citation: Barnwal, B., Kini, R.M. (2013-10-15). Characterization of inflamin, the first member of a new family of snake venom proteins that induces inflammation. Biochemical Journal 455 (2) : 239-250. ScholarBank@NUS Repository. https://doi.org/10.1042/BJ20130599
Abstract: Unlike other sea snakes, Aipysurus eydouxii feeds exclusively on fish eggs. This unusual feeding habit prompted us to search for unique transcripts in their venom glands. In the present study we expressed a novel cysteine-rich secretory protein containing 94 amino acid residues that was identified in its cDNA library. As it induced inflammation and writhing in animals, this protein was named inflamin. It induced two waves of prostanoid production. The first wave peaked at 10 min and 6-oxo PGF1a (prostaglandin F1a) (6-keto PGF1a) was the major product. The second wave, specifically of 6-oxo PGF1a and PGE2 (prostanglandin E2), started after 2 h. In RAW 264.7 cells, COX-1 (cyclo-oxygenase-1) activity showed a transient increase at 10 min and is responsible for the first wave, but its expression was unaffected. COX-2 was induced after 3 h and is responsible for the second wave. Using specific inhibitors, we showed that cPLA2 (calcium-dependent phospholipase A2), and not sPLA2 (secretory phospholipase A2), iPLA2 (calcium-independent phospholipase A2) or DAG (diacylglycerol) lipase, plays a key role in arachidonate release. The cPLA2 activity showed a transient increase of 62%at 10 min; this increase was due to its phosphorylation and not due to an increase in its expression. Thus inflamin, the first member of a new family of snake venom proteins, leads to an increase in the cPLA2 and COX-1 activity resulting in inflammation and pain. © 2013 Biochemical Society.
Source Title: Biochemical Journal
URI: http://scholarbank.nus.edu.sg/handle/10635/100245
ISSN: 02646021
DOI: 10.1042/BJ20130599
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