J. Epelbaum a , F. Agid b , Y. Agid b , A. Beaudet d , P. Bertrand a , A. Enjalbert a , V. Heidet a , C. Kordon a , S. Krantic a , J.F. Léonard a , F. Musset a , E. Moyse a , F. Peillon c , A. Slama a , C. Videau a
28 November 2008
Somatostatin (SRIF) actions in the brain and pituitary are mediated by specific receptors. Using radioiodinated ligands it has been possible to characterize the kinetics of specific binding sites in the brain and pituitary, and to determine their cellular localization by autoradiography. At the pituitary level, the inhibition of growth hormone, prolactin and thyrotropin secretions induced by SRIF is mediated through a single binding site which is coupled to the inhibition of adenylate cyclase. In the brain, SRIF receptors are localized on neurons and glial cells and are also coupled to adenylate cyclase inhibition. Two sites are differentiated in the brain with an analogue of somatostatin, SMS 201995. In humans, SRIF-binding sites have been related to a number of pathologies. At the pituitary level, it has been shown that the number of binding sites was negatively correlated to growth hormone levels in acromegaly. Furthermore, SRIF-binding sites were undetectable in a patient which did not respond to SMS 201995 therapy. In the brain, meningiomas and gliomas are rich in SRIF binding sites. This suggests a possible role for SRIF on glia. In neuro-degenerative diseases, cortical SRIF concentrations are decreased in Alzheimer’s and Parkinson’s disease associated with dementia while SRIF-binding sites are only affected in Alzheimer’s disease. In conclusion, the physiological role of SRIF in the brain and pituitary can be evaluated by studying the receptors of the peptide. Such studies allow to question the implication of SRIF in endocrine and neuropathologies.