Molecular characterization of inhibin-A: Structure and expression analysis in Clarias batrachus

The inhibins are disulphide-linked heterodimeric glycoproteins that belong to the TGFβ superfamily. Inhibins have been well studied in mammals but the information about their structure and function is very limited in lower vertebrates. The aim of the present study was to characterize inhibin-A and to understand its receptor binding interaction, and to evaluate its biological function in Clarias batrachus. Structure prediction of inhibin-A revealed two glycosylation sites on inhibin-α (Asp262 and Asn334). Docking of inhibin-A with its receptor; betaglycan and Act RIIA showed that residues Ser321, Gly324 and Leu325 of inhibin-α are involved in high affinity binding with betaglycan while inhibin-βA bound to Act RIIA by forming hydrogen bonds. The mRNA transcript analysis of various tissues indicated the presence of higher to moderate expression of inhibin-α and inhibin-βA in the gonads and the extra-gonadal tissues. Further, stage specific expression showed decreased levels of inhibin-α in the gonads during the annual reproductive cycles. Inhibin-βA, activin-βB and Act RIIA increased in the brain during spawning while FSHr increased in the gonads during the preparatory phase. Our study provides molecular, structural and functional insights of inhibin-A for the first time in C. batrachus.