Prolactin variants in the rat adenohypophysis.

Prolactin (PRL) heterogeneity in the rat pituitary gland was first reported in 1978. Since then, multiple forms of the hormone in the rat pituitary gland have been reported by other investigators. Some of these variants have been ascribed to posttranslational modifications, while the origin of the others is as yet undefined. In this study, the nature, distribution and origin(s) of PRL size variants in the rat adenohypophysis were defined by Western blotting, Northern blot hybridization analysis and pulse-chase approaches. Thirteen structurally related variants, grouped into species with apparent molecular weights (Mr) 97-34,000, 31,000, 24,000 and 22-17,000, were consistently obtained on the basis of their electrophoretic mobilities in nonreducing polyacrylamide gels. Many of the Mr forms were disulphide-linked aggregates. Northern blot analysis suggested that the 24,000 monomeric PRL was encoded by the 0.9 kb mRNA species, while the 45,000 variant could be encoded by the 1.9 kb mRNA. Four PRL variants in the Mr range of 25-46,000 were synthesized concurrently by the mammotrophs in culture. Newly synthesized high Mr variants were also released into the medium and could be detected as early as 1 min after synthesis. Collectively these results suggest that structurally related PRL variants in the rat pituitary gland are due to a combination of posttranscriptional and posttranslational modification of a single gene product. In addition high Mr variants are preferentially secreted over low Mr forms, probably through an alternative secretory pathway.