title: Immunohistochemical localization of cyclooxygenase-1 and cyclooxygenase-2 in the human fetal and adult male reproductive tracts.
abstract: The first rate-limiting step in the conversion of arachidonic acid to PGs is catalyzed by cyclooxygenase (Cox). Two isoforms of Cox have been identified, Cox-1 (constitutively expressed) and Cox-2 (inducible form), which are the products of two different genes. In this study we describe the immunohistochemical localization of Cox-1 and -2 in the human male fetal and adult reproductive tracts. There was no Cox-1 expression in fetal samples (prostate, seminal vesicles, or ejaculatory ducts), and only minimal expression in adult tissues. There was no expression of Cox-2 in the fetal prostate. In a prepubertal prostate there was some Cox-2 expression that localized exclusively to the smooth muscle cells of the transition zone. In adult hyperplastic prostates, Cox-2 was strongly expressed in smooth muscle cells, with no expression in the luminal epithelial cells. Cox-2 was strongly expressed in epithelial cells of both fetal and adult seminal vesicles and ejaculatory ducts. The Cox-2 staining intensity in the fetal ejaculatory ducts during various times of gestation correlated with previously reported testosterone production rates by the fetal testis. These data indicate that Cox-2 is the predominant isoform expressed in the fetal male reproductive tract, and its expression may be regulated by androgens. The distinct cell type-specific expression patterns of Cox-2 in the prostate (smooth muscle) vs. the seminal vesicles and ejaculatory ducts (epithelium) may reflect the different roles of PGs in these tissues.
authors.affiliation: Department of Urology, Mount Sinai School of Medicine, New York, New York 10029, USA.
authors.forename: A
authors.initials: A
authors.lastname: Kirschenbaum
authors.forename: D R
authors.initials: DR
authors.lastname: Liotta
authors.forename: S
authors.initials: S
authors.lastname: Yao
authors.forename: X H
authors.initials: XH
authors.lastname: Liu
authors.forename: A P
authors.initials: AP
authors.lastname: Klausner
authors.forename: P
authors.initials: P
authors.lastname: Unger
authors.forename: E
authors.initials: E
authors.lastname: Shapiro
authors.forename: I
authors.initials: I
authors.lastname: Leav
authors.forename: A C
authors.initials: AC
authors.lastname: Levine
mesh_terms: D000328:Adult; D002648:Child; D051545:Cyclooxygenase 1; D051546:Cyclooxygenase 2; D004543:Ejaculatory Ducts / Q000196:embryology / Q000201:enzymology; D005260:Female; D005837:Genitalia, Male / Q000196:embryology / Q000201:enzymology*; D005865:Gestational Age; D006801:Humans; D007150:Immunohistochemistry; D007527:Isoenzymes / Q000378:metabolism*; D008297:Male; D008565:Membrane Proteins; D009130:Muscle, Smooth / Q000196:embryology / Q000201:enzymology; D011247:Pregnancy; D011451:Prostaglandin-Endoperoxide Synthases / Q000378:metabolism*; D011467:Prostate / Q000196:embryology / Q000201:enzymology; D012669:Seminal Vesicles / Q000196:embryology / Q000201:enzymology
chemical_list: D007527:Isoenzymes; D008565:Membrane Proteins; D051545:Cyclooxygenase 1; D051546:Cyclooxygenase 2; C496511:PTGS1 protein, human; C496540:PTGS2 protein, human; D011451:Prostaglandin-Endoperoxide Synthases