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1 Institut National de la Santé et de la Recherche Médicale, Unité 878, Grenoble, France2 Commissariat à l'Energie Atomique, Institut de Recherches en Technologies et Sciences pour le Vivant, 38054 Grenoble, France3 Université Joseph Fourier, 38054 Grenoble, France
(Correspondence should be addressed to M Thomas who is now at INSERM Unité 878, iRTSV, CEA-G, 17 rue des Martyrs, 38054 Grenoble, Cedex 09, France; Email: michael.thomas{at}cea.fr)
Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) and its homolog Bombina variegata (Bv8), also termed prokineticin-1 and -2 (PK1 and PK2) respectively, are newly identified peptides with specific mitogenic activity on endocrine gland-derived endothelial cells. In the present study, we analyzed the sites of expression of EG-VEGF/PK1, Bv8/PK2, and their receptors (PKR1 and PKR2) in the adrenal cortex and checked for new biological functions of these factors on the endocrine cell compartment. RT-PCR and immunostaining analyses revealed that glomerulosa and fasciculata cells express both factors and both receptors. EG-VEGF/PK1 had no effect on the steroidogenic activity of both bovine glomerulosa and fasciculata cells but appeared to be mitogenic for both cell types. Binding of EG-VEGF/PK1 to fasciculata cells stimulated the phosphorylation of ERK1/2. Pretreatment with pertussis toxin suppressed this effect, indicating that it was Gi mediated. EG-VEGF/PK1 also increased the phosphorylation of Akt in endocrine cells of the adrenal cortex. EG-VEGF/PK1 and Bv8/PK2 thus represent new regulatory peptides acting as autocrine mitogens for endocrine cells.
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A. Hoeflich and M. Bielohuby Mechanisms of adrenal gland growth: signal integration by extracellular signal regulated kinases1/2 J. Mol. Endocrinol., March 1, 2009; 42(3): 191 - 203. [Abstract] [Full Text] [PDF] |
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