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Prostaglandins. 1996 Jan;51(1):81-5.

Molecular characterization of the 5.2 KB isoform of the human cyclooxygenase-1 transcript.

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Department of Molecular Biology, American Red Cross, Rockville, MD 20855, USA.


Several cDNA clones from human endothelial cells were isolated by expression cloning with the polyclonal antisera against the Ram seminal vesicle cyclooxygenase enzyme (Cox-1). One such clone produced a fusion protein that reacted with two other Cox-1 antiserum (Hla, T., Farrell, M.P., Kumar, A. and Bailey, J.M. (1986) Prostaglandins 32 (6) 829-845). The 2.5 kb cDNA insert was sequenced and contained 60 bp encoding the C-terminal end of the human Cox-1 polypeptide, followed by 2.3 kb of untranslated region. Northern blot analysis of human endothelial cells using the 2.5 kb cDNA insert detected the 2.8 and 5.2 kb Cox-1 transcripts. These data indicated that the isolated clone represented the 5.2 kb isoform of the human Cox-1 mRNA. The presence of the canonical polyadenylation site AAUAAA at 740 bp downstream from the translation termination codon suggests that alternative polyadenylation of the Cox-1 gene gives rise to 5.2 and 2.8 kb isoforms. The sequence of the 3'-UTR of the Cox-1 transcripts is highly divergent from that of the human Cox-2 transcript isoforms, suggesting a distinct function in the regulation of expression at the post-transcriptional and/or translational levels.

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