Arachidonate Stimulates Prolactin Releasein Vitro: A Role for the Fatty Acid and Its Metabolites as Intracellular Regulator(s) in Mammotrophs*

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Abstract
The involvement of arachidonate in the PRL [prolactin] secretory process was investigated using 3 experimental systems: hemipituitary glands incubated in vitro, cultured pituitary cells and dispersed anterior pituitary cells perifused in columns. Arachidonate (100 .mu.M) significantly (P < 0.05) stimulated PRL release in the former system and stimulated PRL secretion in a dose-related manner in cultured cells. In hemipituitary glands, indomethacin, a cyclooxygenase inhibitor, potentiated the arachidonate-mediated stimulation; nordihydroguaiaretic acid or BW755c [3-amino-1[m-(trifluoromethyl)phenyl]-2-pyrazoline] abolished it. The latter 2 agents, but not indomethacin, abolished the effect of phospholipase A2 on PRL release in vitro. BW755c also inhibited the stimulatory effect of TRH on PRL release in both experimental systems. The stimulation of PRL release by phorbol myristate acetate (PMA), although significantly reduced, was not abolished by either nordihydroguaiaretic acid or BW755c. Quinacrine, a phospholipase A2 inhibitor, also abolished the stimulatory effect of phospholipase A2 or TRH on PRL release. In cultured cells, quinacrine inhibits basal PRL release, but does not affect PRL release induced by arachidonate or dibutyl cAMP. These results more firmly establish a role for arachidonate as an intracellular mediator of PRL release and suggest the involvement of an arachidonate metabolic pathway(s) (lipoxygenase and epoxygenase) other than prostaglandin or thromboxane formation. The effect of PMA on PRL release may be attributable only in part to an increase in the production of arachidonate metabolites, and most of PMA effect on PRL release may relate to its activation of protein kinase C.

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