Endocrinology, Vol 127, 2601-2603, Copyright © 1990 by Endocrine Society

ARTICLES

Identification of prolactin-like proteins synthesized by normal murine lymphocytes

DW Montgomery, JA LeFevre, ED Ulrich, CR Adamson and CF Zukoski
Department of Pharmacology, University of Arizona College of Medicine, Tucson 85724.

Cultured murine lymphoid cells release a PRL-like immunoreactive (IR) protein which may be important in immunity, as anti-PRL antisera inhibit lymphocyte proliferation in vitro. We examined culture supernatants (SNs) and cell lysates from concanavalin A (Con A) activated murine thymocytes to identify these proteins. Western blot analysis of cell lysates revealed three specifically-stained PRL-IRs. A doublet of bands at 35.6 and 33.6 kDa was associated with the particulate fraction of the cell. These PRL-IRs were present in lymphocytes independently of mitogen stimulation. In contrast, a 22 kDa PRL-IR was only produced in mitogen stimulated cells, and was specifically immunoprecipitated with anti-PRL antiserum. In addition, all three PRL-like IRs incorporated 35S-methionine in vitro, indicating that they are synthesized by these cells. Only the 22 kDa PRL-like protein was present in culture medium from stimulated cells, suggesting that this may be the PRL bioactivity previously demonstrated in SNs from murine lymphocytes.

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