{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,6,25]],"date-time":"2025-06-25T21:08:02Z","timestamp":1750885682804},"reference-count":54,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2013,10,15]]},"abstract":"<jats:p>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\u00a0min and 6-oxo PGF1\u03b1 (prostaglandin F1\u03b1) (6-keto PGF1\u03b1) was the major product. The second wave, specifically of 6-oxo PGF1\u03b1 and PGE2 (prostanglandin E2), started after 2\u00a0h. In RAW 264.7 cells, COX-1 (cyclo-oxygenase-1) activity showed a transient increase at 10\u00a0min and is responsible for the first wave, but its expression was unaffected. COX-2 was induced after 3\u00a0h 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\u00a0min; 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.<\/jats:p>","DOI":"10.1042\/bj20130599","type":"journal-article","created":{"date-parts":[[2013,7,9]],"date-time":"2013-07-09T08:07:56Z","timestamp":1373357276000},"page":"239-250","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Characterization of inflamin, the first member of a new family of snake venom proteins that induces inflammation"],"prefix":"10.1042","volume":"455","author":[{"given":"Bhaskar","family":"Barnwal","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, National University of Singapore, Singapore 117543"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R. Manjunatha","family":"Kini","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, National University of Singapore, Singapore 117543"},{"name":"Department of Biochemistry and Molecular Biophysics, Medical College of Virginia, Virginia Commonwealth University, VA 23298, U.S.A."},{"name":"The School of Pharmacy and Medical Sciences, Division of Health Sciences, University of South Australia, Adelaide 5000, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2013,9,27]]},"reference":[{"key":"2021112217340193700_B1","doi-asserted-by":"crossref","DOI":"10.1007\/978-3-642-66913-2","volume-title":"Snake Venoms.","author":"Lee","year":"1979"},{"key":"2021112217340193700_B2","doi-asserted-by":"crossref","first-page":"40097","DOI":"10.1074\/jbc.M305322200","article-title":"Identification of a novel family of proteins in snake venoms. 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