18 research outputs found

    Immunocytochemical and autoradiographic studies of the endocrine cells interacting with GABA in the rat stomach

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    There are now increasing evidences suggesting that GABA is able of direct interaction with certain endocrine cells. In the present study, highly specific anti-GABA-glutaraldehyde antibodies and 3H-GABA uptake were used at the light and electron microscope levels to investigate the occurrence of cells containing endogenous GABA or taking up exogenous GABA in the mucosal antrum and corpus of the rat stomach. Only certain endocrine cell types of both regions were immunostained or grain-labelled. However, the morphology of their secretory granules did not allow to identify the nature of their hormone with certainty but suggested that somatostatin-like cells could interact with GABA. The combination of gastrin and somatostatin immunodetection with 3H-GABA uptake autoradiography at the light microscope level, revealed that a subpopulation of somatostatin-like cells and other still unidentified endocrine cells are able to take up GABA, while the gastrin-like cells are not. These results reinforce the hypothesis that certain endocrine cell types of the diffuse endocrine system of the digestive tract are able to directly interact with GABA

    Class A GPCR: Di/Oligomerization of Glycoprotein Hormone Receptors

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    G protein-coupled receptor (GPCR) dimerization and oligomerization was first described over 2 decades ago, contributing to the recent paradigm shift in GPCR signaling of a simplistic, archetypal view involving single receptors activating specific heterotrimeric G proteins at the cell surface, to one of an increasing complex receptor signaling system. However, our understanding of how dimerization and oligomerization, particularly homomerization, generates functional diversity in GPCR signaling is poorly understood. For the Class A/rhodopsin subfamily of glycoprotein hormone receptors (GpHRs), di/oligomerization has been demonstrated to play a significant role in regulating its signal activity at a cellular and physiological level and even pathophysiologically. Here we will describe and discuss the developments in our understanding of GPCR oligomerization, primarily the role of homomeric receptor complexes, in both health and disease, from the study of this unique and complex subfamily of GPCRs
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