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Carbachol-induced in vitro secretion of certain human submandibular proteins investigated by mass-spectrometry.

Journal article
Authors Tiziana Cabras
Massimo Castagnola
Rosanna Inzitari
Jörgen Ekström
Michela Isola
Alessandro Riva
Irene Messana
Published in Archives of oral biology
Volume 53
Issue 11
Pages 1077-83
ISSN 1879-1506
Publication year 2008
Published at Institute of Neuroscience and Physiology, Department of Pharmacology
Pages 1077-83
Language en
Subject categories Pharmacology and Toxicology


OBJECTIVE: To investigate protein content of saliva produced in vitro by samples of human submandibular gland following stimulation with the muscarinic agent carbachol. DESIGN: Tissue samples, obtained at surgery from seven patients and showing normal morphological appearance, were tested for 30 min: in absence of carbachol and atropine; in presence of carbachol (10 microM); in presence of carbachol (10 microM) and atropine (20 microM); or in presence of just atropine (20 microM). Medium was analysed by high-performance liquid chromatography-mass-spectrometry. Neither before nor during surgery were the patients exposed to drug treatments that were likely to influence the in vitro secretion. RESULTS: Proline-rich proteins (PRP)-1 and -3, peptide PC and PB, statherin, cystatins SN, S1 and S2 were invariably found in control gland tissue medium. Mean concentrations of these proteins/peptides in the medium were non-proportionally elevated following carbachol exposure to the gland tissues. Difference between basal release and carbachol-induced secretion achieved statistical significance as to all the proteins/peptides under study but for statherin. Atropine alone or atropine plus carbachol caused no significant changes compared to the basal release of proteins/peptides. CONCLUSIONS: In vitro studies on salivary glands make it possible to study protein secretion from individual glands and thus, to reveal the contribution of the various types of gland to protein/peptide content of whole saliva. The disproportional responses to carbachol may imply that the proteins/peptides are not confined to the same cells or to the same intracellular locations and are therefore not secreted as packages at parasympathetic cholinergic activity.

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