Literature DB >> 26769834

Ultrastructural evidence of a secretory role for melatonin in the human parotid gland.

F Loy1, M Isola2, R Isola2, P Solinas2, M A Lilliu2, R Puxeddu3, J Ekstrom2,4.   

Abstract

In vivo animal studies show that pentagastrin, cholecystokinin and melatonin cause the secretion and synthesis of salivary proteins. Melatonin occurs in large amounts in the gut and is released into the blood on food intake. In vitro experiments suggest that pentagastrin exerts secretory activity in human salivary glands, as judged by ultrastructural changes, reflecting secretion, and an actual protein output. Currently, it is hypothesised that melatonin induces secretory exocytotic events in the human parotid gland. Human parotid tissues were exposed to a high single concentration of melatonin in vitro, processed for high resolution scanning electron microscopy and then assessed morphometrically with the emphasis on the membrane of the intercellular canaliculi, a site of protein secretion. Compared with controls and in terms of density, the melatonin-exposed parotid tissues displayed increases in protrusions (signalling anchored granules) and microbuds (signalling membrane recycling and/or vesicle secretion) and decreases in microvilli (signalling cytoskeletal re-arrangement related to exocytosis), phenomena abolished or very largely reduced by the melatonin receptor blocker, luzindole. In conclusion, acinar serous cells of parotid tissue displayed in vitro exocytotic activity to melatonin, signalling protein secretion. Whether, under physiological conditions, melatonin influences the secretion of human parotid glands remains to be explored, however.

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Year:  2015        PMID: 26769834

Source DB:  PubMed          Journal:  J Physiol Pharmacol        ISSN: 0867-5910            Impact factor:   3.011


  1 in total

1.  Melatonin release by exocytosis in the rat parotid gland.

Authors:  Michela Isola; Jörgen Ekström; Raffaella Isola; Francesco Loy
Journal:  J Anat       Date:  2018-12-10       Impact factor: 2.610

  1 in total

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