{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,26]],"date-time":"2025-10-26T14:01:20Z","timestamp":1761487280204},"reference-count":28,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2005,1,1]]},"abstract":"<jats:p>The two COX (cyclo-oxygenase) isoenzymes COX-1 and -2 catalyse the initial step in the conversion of arachidonic acid into PG (prostaglandin) hormones. The identification of an mRNA transcript encoding a splice variant of human COX-1 was reported more than a decade ago [Diaz, Reginato and Jimenez (1992) J. Biol. Chem. 267, 10816\u201310822], yet catalytic activity and tissue expression of the corresponding spliced protein remained uncharacterized. The splice variant lacks amino acids 396\u2013432, corresponding to the last 37 amino acids of exon 9 of the gene encoding COX-1. These amino acids form a loop at one side of the peroxidase active site of the protein. We expressed the full-length and spliced COX-1 cDNAs in COS-7 and Sf9 insect cells, and determined the PG-forming activity using incubations with radiolabelled arachidonic acid and HPLC analyses. When expressed in either system, abundant PG formation was observed with the full-length COX-1, whereas the spliced protein did not form any detectable product. Peroxidase activity was readily detected in microsomes prepared from COS-7 cells transfected with COX-1 but not with the splice variant. In reverse transcriptase\u2013PCR experiments, we detected the mRNA for the alternatively spliced and full-length COX-1 in human brain, tonsil and colon tissue, yet we were unable to detect expression of the spliced protein in the same tissues using immunoprecipitation and Western-blot analyses. We conclude that, whereas the mRNA transcript for the spliced COX-1 is present in various human tissues, the corresponding protein is either not formed or subject to rapid proteolytic degradation.<\/jats:p>","DOI":"10.1042\/bj20041115","type":"journal-article","created":{"date-parts":[[2004,12,15]],"date-time":"2004-12-15T12:10:58Z","timestamp":1103112658000},"page":"57-64","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["Human cyclo-oxygenase-1 and an alternative splice variant: contrasts in expression of mRNA, protein and catalytic activities"],"prefix":"10.1042","volume":"385","author":[{"given":"Claus","family":"SCHNEIDER","sequence":"first","affiliation":[{"name":"Department of Pharmacology, Vanderbilt University School of Medicine, 23rd Ave. at Pierce, Nashville, TN 37232-6602, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"William\u00a0E.","family":"BOEGLIN","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Vanderbilt University School of Medicine, 23rd Ave. at Pierce, Nashville, TN 37232-6602, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alan\u00a0R.","family":"BRASH","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Vanderbilt University School of Medicine, 23rd Ave. at Pierce, Nashville, TN 37232-6602, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2004,12,14]]},"reference":[{"key":"2021112214124644800_B1","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1146\/annurev.pharmtox.38.1.97","article-title":"Cyclooxygenases 1 and 2","volume":"38","author":"Vane","year":"1998","journal-title":"Annu. 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