Reduced calcium and inhibition of protein kinase C mimic the enhancement of ornithine decarboxylase activity of prolactin in Ambystoma tigrinum tissues

• Published in: The Journal of experimental zoology Vol. 260; no. 2; p. 202
• Main Authors: Ibrahim, R H, Platt, J E
• Format: Journal Article
• Language: English
• Published: United States 01.11.1991
• Subjects: Ambystoma; Animals; Calcium - metabolism; Calcium Channel Blockers - pharmacology; Edetic Acid - pharmacology; In Vitro Techniques; Liver - metabolism; Ornithine Decarboxylase - metabolism; Prolactin - physiology; Protein Kinase C - antagonists & inhibitors; Skin - metabolism
• ISSN: 0022-104X
• DOI: 10.1002/jez.1402600209

We previously reported that prolactin (PRL) could increase the activity of ornithine decarboxylase (ODC) in liver slices taken from larval tiger salamanders (Ambystoma tigrinum). This action of the hormone was inhibited by oxytocin (OT), the calcium ionophore A23187, and diacyglycerol (DG) and was duplicated by 10 microM verapamil (VML), a calcium channel blocker. Here, we expand these results to show that 1) a higher dose of VML (50 microM) produces an additive effect with PRL; 2) addition of small amounts of calcium (0.1 mM) to the liver culture medium blocks PRL action; 3) neither nifedipine (NIF), a different type of calcium channel blocker, nor EDTA alter PRL action; and 4) gossypol, a reported inhibitor of protein kinase C, mimics PRL action. Additionally, we show that PRL increases ODC activity in tiger salamander tail skin in vitro, a tissue previously demonstrated to be a PRL target tissue in this species. The same set of treatments which we have shown to modify PRL effects on ODC in liver slices affects PRL action in the tail skin in a parallel manner. Thus, the mechanism whereby PRL enhances ODC activity appears to be the same in both these tissues. These results are discussed in conjunction with the findings from similar studies using mammalian tissues in an attempt to assess the current picture of the mechanism of PRL action and the possible role of inositol phospholipid turnover, calcium, and protein kinase C in the action of this hormone.