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J. Biol. Chem., Vol. 279, Issue 14, 13624-13633, April 2, 2004

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On the Evolutionary Origin of Cyclooxygenase (COX) Isozymes

CHARACTERIZATION OF MARINE INVERTEBRATE COX GENES POINTS TO INDEPENDENT DUPLICATION EVENTS IN VERTEBRATE AND INVERTEBRATE LINEAGES^*

Reet Järving, Ivar Järving, Reet Kurg, Alan R. Brash¶, and Nigulas Samel||

From the Department of Chemistry, Tallinn Technical University, Akadeemia tee 15, Tallinn 12618, Institute of Technology, Tartu University, 23 Riia Street, Tartu 51010, Estonia, and the ^¶Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-6602

In vertebrates, COX-1 and COX-2, two cyclooxygenase isozymes with different physiological functions and gene regulation, catalyze identical reactions in prostaglandin synthesis. It is still not understood why there are multiple forms of COX enzyme in the same cell type and when the evolutionary duplication of the COX gene occurred. Here we report the structure of two genes encoding for COX isozymes in the coral Gersemia fruticosa, the first non-vertebrate organism from which a cyclooxygenase was characterized. Both genes are about 20 kb in size and consist of nine exons. Intron/exon boundaries are well conserved between coral and mammalian COX genes. mRNAs of the previously reported G. fruticosa COX-A (GenBank^TM accession number AY004222) and the novel COX-B share 94% sequence identity in the coding regions and less than 30% in the 5'- and 3'-untranslated region. Transcripts of both COX genes are detectable in coral cells, although the transcriptional level of COX-A is 2 orders of magnitude higher than COX-B. Expression of both coral genes in mammalian cells gave functional proteins with similar catalytic properties. By data base analyses we also detected and constructed different pairs of COX genes from the primitive chordates, Ciona savignyi and Ciona intestinalis. These two gene pairs encode proteins with 50% intra-species and only 70% cross-species sequence identity. Our results suggest that invertebrate COX gene pairs do not correspond to vertebrate COX-1 and COX-2 and are consistent with duplication of the COX gene having occurred independently in corals, ascidians, and vertebrates. It is evident that due to the importance and complexity of its regulatory role, COX has multiple isoforms in all organisms known to express it, and the genes encoding for the isozymes may to be regulated differently.

Received for publication, December 4, 2003 , and in revised form, January 14, 2004.

^* This work was supported by Estonian Science Foundation Grants 5639 (to N. S.) and 5100 (to I. J.) and National Institutes of Health Grant GM-53638 (to A. R. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence should be addressed: Dept. of Chemistry, Tallinn Technical University, Akadeemia tee 15, Tallinn 12618, Estonia. Tel.: 372-620-4376; Fax: 372-670-3683; E-mail: samel{at}chemnet.ee.

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