Diverse molecular forms of gonadotropin-releasing hormone in an elasmobranch and a teleost fish
- PMID: 3533711
- DOI: 10.1016/0016-6480(86)90184-x
Diverse molecular forms of gonadotropin-releasing hormone in an elasmobranch and a teleost fish
Abstract
Immunoreactive and biologically active gonadotropin-releasing hormones (GnRHs) in dogfish (Poroderma africanum) and teleost (Coris julis) brain extracts were studied by high-performance liquid chromatography (HPLC), radioimmunoassay with region-specific antisera, and assessment of luteinizing hormone (LH)-releasing activity in a chicken dispersed pituitary cell bioassay. In dogfish brain extract, seven GnRH molecular forms with LH-releasing activity were demonstrated. Three of these forms coeluted with synthetic mammalian GnRH; His5,Trp7,Tyr8-GnRH; and Trp7,Leu8-GnRH on HPLC. The peaks coincident with His5,Trp7,Tyr8-GnRH and Trp7,Leu8-GnRH had immunological and biological properties identical to those of the synthetic peptides. However, the molecular form coeluting with mammalian GnRH had immunological and biological properties different from those of mammalian GnRH and is thus a novel molecular variant of GnRH. The four remaining forms are also novel GnRHs or structurally unrelated peptides with LH-releasing activity. Dogfish systemic blood contained immunoreactive GnRH. In teleost brain extract, three biologically active GnRH forms with LH-releasing activity were present. The major peak of GnRH immunoreactivity coeluted with Trp7,Leu8-GnRH, and a second immunoreactive form coeluted with His5,Trp7,Tyr8-GnRH. The third biologically active peak is a novel, early-eluting molecular variant of GnRH or a structurally unrelated peptide with LH-releasing activity.
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