We recently described the presence of a series of prolactin (PRL)-like molecules (PLMs) in the rat pituitary gland and showed that their formation was not due to artifactual proteolysis of 24 kDa PRL during extraction or to degradation of PRL in lysosomes. In this study we have found (1) in vitro translation of pituitary cell RNA to result in the production of only 24 kDa monomer isoform 2 and no PLMs, (2) that secretion of newly synthesized PLMs is differently regulated than at least a proportion of newly synthesized monomers, (3) that secretion of newly synthesized PLMs occurs after at least a 6 h delay, (4) that cysteamine (a) inhibits the release of the PLMs, (b) causes an increase in their amount versus isoform 2, and (c) causes an intracellular accumulation of pleiomorphic, immature secretory granules, and (5) that cells grown under degranulating culture conditions do not contain PLMs. These results, using normal anterior pituitary cells in primary culture, demonstrate the potential for differential release of the PLMs versus monomer PRL in vivo and are consistent with the production of the PLMs from 24 kDa monomer isoform 2 during secretory granule condensation.
Bibliographical noteFunding Information:
Address for correspondence: Ameae M. Walker, Division of Biomedical Sciences, University of California, Riverside, CA 92521, U.S.A. This work was supported by NIH grants AM 28534 and RR 05816, an ACS grant BC 562, and by a grant from the Riverside Academic Senate. * Postdoctoral fellows on NIH training grant AM-07310. Dr. Oetting’s present address: Institute of Human Genetics, University of Minnesota, Minneapolis, MN 55455-0311, U.S.A.
- Granule condensation, differential release
- Mammotroph, subpopulation