title: Discrepancy between molecular structure and ligand selectivity of a testicular follicle-stimulating hormone receptor of the African catfish (Clarias gariepinus).
abstract: A putative FSH receptor (FSH-R) cDNA was cloned from African catfish testis. Alignment of the deduced amino acid sequence with other (putative) glycoprotein hormone receptors and analysis of the African catfish gene indicated that the cloned receptor belonged to the FSH receptor subfamily. Catfish FSH-R (cfFSH-R) mRNA expression was observed in testis and ovary; abundant mRNA expression was also detected in seminal vesicles. The isolated cDNA encoded a functional receptor since its transient expression in human embryonic kidney (HEK-T) 293 cells resulted in ligand-dependent cAMP production. Remarkably, African catfish LH (cfLH; the catfish FSH-like gonadotropin has not been purified yet) had the highest potency in this system. From the other ligands tested, only human recombinant FSH (hrFSH) was active, showing a fourfold lower potency than cfLH, while hCG and human TSH (hTSH) were inactive. Human CG (as well as cfLH, hrFSH, eCG, but not hTSH) stimulated testicular androgen secretion in vitro but seemed to be unable to bind to the cfFSH-R. However, it was known that hCG is biologically active in African catfish (e.g., induction of ovulation). This indicated that an LH receptor is also expressed in African catfish testis. We conclude that we have cloned a cDNA encoding a functional FSH-R from African catfish testis. The cfFSH-R appears to be less discriminatory for its species-specific LH than its avian and mammalian counterparts.
authors.affiliation: Department of Experimental Zoology, Utrecht University, NL-3584 CH Utrecht, The Netherlands.
authors.forename: J
authors.initials: J
authors.lastname: Bogerd
authors.forename: M
authors.initials: M
authors.lastname: Blomenröhr
authors.forename: E
authors.initials: E
authors.lastname: Andersson
authors.forename: H H
authors.initials: HH
authors.lastname: van der Putten
authors.forename: C P
authors.initials: CP
authors.lastname: Tensen
authors.forename: H F
authors.initials: HF
authors.lastname: Vischer
authors.forename: J C
authors.initials: JC
authors.lastname: Granneman
authors.forename: C
authors.initials: C
authors.lastname: Janssen-Dommerholt
authors.forename: H J
authors.initials: HJ
authors.lastname: Goos
authors.forename: R W
authors.initials: RW
authors.lastname: Schulz
mesh_terms: D000595:Amino Acid Sequence; D000728:Androgens / Q000378:metabolism; D000818:Animals; D001483:Base Sequence; D002397:Catfishes; D002460:Cell Line; D006063:Chorionic Gonadotropin / Q000494:pharmacology; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D004622:Embryo, Mammalian; D004625:Embryo, Nonmammalian; D005260:Female; D005640:Follicle Stimulating Hormone / Q000378:metabolism; D015870:Gene Expression; D006801:Humans; D007295:Inositol Phosphates / Q000096:biosynthesis; D007668:Kidney / Q000737:chemistry; D007986:Luteinizing Hormone / Q000378:metabolism; D008297:Male; D008969:Molecular Sequence Data; D010053:Ovary / Q000737:chemistry; D010802:Phylogeny; D012333:RNA, Messenger / Q000032:analysis; D011962:Receptors, FSH / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D012669:Seminal Vesicles / Q000737:chemistry; D016415:Sequence Alignment; D013045:Species Specificity; D013737:Testis / Q000737:chemistry* / Q000378:metabolism; D014162:Transfection
chemical_list: D000728:Androgens; D006063:Chorionic Gonadotropin; D018076:DNA, Complementary; D007295:Inositol Phosphates; D012333:RNA, Messenger; D011962:Receptors, FSH; D011994:Recombinant Proteins; D007986:Luteinizing Hormone; D005640:Follicle Stimulating Hormone