Endocrinology, Vol 134, 1213-1218, Copyright © 1994 by Endocrine Society

ARTICLES

Short term effect of prolactin on intracellular calcium in Chinese hamster ovary cells stably transfected with prolactin receptor complementary deoxyribonucleic acid

P Vacher, M Tran Van Chuoi, J Paly, J Djiane and B Dufy
Laboratoire de Neutrophysiologie, Centre National de la Recherche Scientifique URA 1200, Universite de Bordeaux 2, France.

The mechanism of transduction of the PRL signal in target cells is poorly understood. We examined the effects of PRL on the intracellular free Ca2+ concentration in Chinese hamster ovary cells overexpressing functional PRL receptors. [Ca2+]i was determined by dual emission microspectrofluorimetry using indo-1 as the Ca2+ fluorescent probe. We demonstrate that at physiological concentrations (0.5-5 nM), PRL stimulates Ca2+ entry (type I) and/or induces a mobilization of calcium ions stored in intracellular compartments (type II). Two types of Ca2+ mobilization, distinguishable by their onset kinetics, were observed, a slow mobilization (type IIa; transition time to peak, approximately 10 sec) and a fast mobilization (type IIb; transition time to peak, < 2 sec). PRL responses were delayed (15-120 sec) compared to the well known activation by phosphatidylinositol 4,5 bisphosphate hydrolysis- coupled receptors. This suggests that inositol trisphosphate is not involved in PRL response or that phosphatidylinositol 4,5 bisphosphate hydrolysis is not directly coupled to the PRL receptor. The amplitude of the PRL-induced Ca2+ increases (300-1400 nM) would be sufficient to provoke several physiological responses, such as stimulation of secretion, cell proliferation, or gene activation. However, the relation between the increase in Ca2+ and activation of milk protein genes remains to be established.

This article has been cited by other articles:

				I. C. Kokay, P. M. Bull, R. L. Davis, M. Ludwig, and D. R. Grattan Expression of the long form of the prolactin receptor in magnocellular oxytocin neurons is associated with specific prolactin regulation of oxytocin neurons Am J Physiol Regulatory Integrative Comp Physiol, May 1, 2006; 290(5): R1216 - R1225. [Abstract] [Full Text] [PDF]

				F. Y. Ma, D. R. Grattan, V. Goffin, and S. J. Bunn Prolactin-Regulated Tyrosine Hydroxylase Activity and Messenger Ribonucleic Acid Expression in Mediobasal Hypothalamic Cultures: The Differential Role of Specific Protein Kinases Endocrinology, January 1, 2005; 146(1): 93 - 102. [Abstract] [Full Text] [PDF]

				T. Ducret, A.-M. Vacher, and P. Vacher Effects of Prolactin on Ionic Membrane Conductances in the Human Malignant Astrocytoma Cell Line U87-MG J Neurophysiol, March 1, 2004; 91(3): 1203 - 1216. [Abstract] [Full Text] [PDF]

				P. R. Manna, T. El-Hefnawy, J. Kero, and I. T. Huhtaniemi Biphasic Action of Prolactin in the Regulation of Murine Leydig Tumor Cell Functions Endocrinology, January 1, 2001; 142(1): 308 - 318. [Abstract] [Full Text] [PDF]

				N. G. Selvaraj, E. Omi, G. Gibori, and M. C. Rao Janus Kinase 2 (JAK2) Regulates Prolactin-Mediated Chloride Transport in Mouse Mammary Epithelial Cells through Tyrosine Phosphorylation of Na+-K+-2Cl- Cotransporter Mol. Endocrinol., December 1, 2000; 14(12): 2054 - 2065. [Abstract] [Full Text]

				R. M. Touyz, L. Jiang, and M. Ram Sairam Follicle-Stimulating Hormone Mediated Calcium Signaling by the Alternatively Spliced Growth Factor Type I Receptor Biol Reprod, April 1, 2000; 62(4): 1067 - 1074. [Abstract] [Full Text]

				B. A. Miller, D. L. Barber, L. L. Bell, B. K. Beattie, M.-Y. Zhang, B. G. Neel, M. Yoakim, L. I. Rothblum, and J. Y. Cheung Identification of the Erythropoietin Receptor Domain Required for Calcium Channel Activation J. Biol. Chem., July 16, 1999; 274(29): 20465 - 20472. [Abstract] [Full Text] [PDF]

				B. Sorin, O. Goupille, A. M. Vacher, J. Paly, J. Djiane, and P. Vacher Distinct Cytoplasmic Regions of the Prolactin Receptor Are Required for Prolactin-induced Calcium Entry J. Biol. Chem., October 23, 1998; 273(43): 28461 - 28469. [Abstract] [Full Text] [PDF]

				C. Bole-Feysot, V. Goffin, M. Edery, N. Binart, and P. A. Kelly Prolactin (PRL) and Its Receptor: Actions, Signal Transduction Pathways and Phenotypes Observed in PRL Receptor Knockout Mice Endocr. Rev., June 1, 1998; 19(3): 225 - 268. [Abstract] [Full Text]

				N. B. Prevarskaya, R. N. Skryma, P. Vacher, N. Daniel, J. Djiane, and B. Dufy Role of Tyrosine Phosphorylation in Potassium Channel Activation J. Biol. Chem., October 13, 1995; 270(41): 24292 - 24299. [Abstract] [Full Text] [PDF]