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Nitric oxide‐dependent protein synthesis in parotid and submandibular glands of anaesthetized rats upon sympathetic stimulation or isoprenaline administration
Author(s) -
Sayardoust Shariel,
Ekström J.
Publication year - 2004
Publication title -
experimental physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.925
H-Index - 101
eISSN - 1469-445X
pISSN - 0958-0670
DOI - 10.1113/expphysiol.2003.002648
Subject(s) - isoprenaline , endocrinology , medicine , stimulation , submandibular gland , nitric oxide synthase , chemistry , leucine , agonist , nitric oxide , receptor , amino acid , biochemistry
In anaesthetized female rats, the β‐adrenoceptor agonist isoprenaline was intravenously infused (20 μg kg −1 min −1 ) for 30 min or the ascending cervical sympathetic nerve trunk was intermittently stimulated (50 Hz, 1 s every tenth second) on one side for 30 min. The incorporation of [ 3 H]leucine into trichloroacetic acid (TCA)‐insoluble material was used as an index of protein synthesis. In response to isoprenaline, the [ 3 H]leucine incorporation increased by 79% in the parotid glands and by 82% in the submandibular glands. The neuronal type NO‐synthase inhibitor N‐PLA, reduced ( P < 0.001) this response to 26% and 20%, respectively. Sympathetic stimulation under α‐adrenoceptor blockade increased the [ 3 H]leucine incorporation by 192% in the parotid glands and by 35% in the submandibular glands. N‐PLA reduced the corresponding percentage figures to 86% ( P < 0.01) and 8% ( P < 0.05). When tested in the parotid glands, the non‐selective NO‐synthase inhibitor L ‐NAME reduced ( P < 0.01) the nerve‐evoked response to 91%. The increase in [ 3 H]leucine incorporation in response to sympathetic stimulation under β‐adrenoceptor blockade was not affected by N‐PLA in the parotid (139% versus 144%) and submandibular glands (39% versus 34%). In non‐stimulated glands, the [ 3 H]leucine incorporation was not influenced by the NO‐synthase inhibitors. In conclusion, β‐adrenoceptor mediated salivary gland protein synthesis is largely dependent on NO generation by neuronal type NO‐synthase, most likely of parenchymal origin.