“…However the significant difference in total amylase secretion between SLIGRL-OH stimulation and pilocarpine stimulation demonstrates the higher activity of pilocarpine to induce salivary secretion and that the intracellular signaling of mAChR and PAR-2 is not completely the same. From these results, we consider that stimulation with SLIGRL-OH induces fluid secretion rather than protein secretion, which is mainly induced by -adrenergic stimulation (Slomiany et al, 1992), although some amount of amylase can be secreted as reported previously (Kawabata et al, 2000b(Kawabata et al, , 2002b. The results also indicate that sympathetic nervous activity is not involved in PAR-2-mediated salivary secretion.…”
Section: Discussionsupporting
confidence: 79%
“…Isoproterenol-induced salivary secretions were much less than pilocarpine-induced secretions: 1.6 Ϯ 0.3 l/g in WT, 1.7 Ϯ 0.1 l/g in M 1 KO, 1.0 Ϯ 0.4 l/g in M 3 KO, 1.3 Ϯ 0.4 l/g in M 1 /M 3 KO, and 1.8 Ϯ 0.2 l/g in PAR-2KO mice, which are consistent with the fact that -adrenergic, sympathetic stimulation evokes water secretion only slightly but mainly induces protein secretion after production of cyclic adenosine monophosphate (Slomiany et al, 1992).…”
supporting
confidence: 84%
“…Regarding the mass of protein secretion in 15 min, total protein in saliva secreted in response to isoproterenol (47.0 Ϯ 12.2 g/15 min g body weight, p Ͻ 0.05 or p Ͻ 0.01, comparing isoproterenol to pilocarpine or SLIGRL-OH) was much higher than that in response to pilocarpine (18.4 Ϯ 3.9 g/15 min g body weight) or SLIGRL-OH (3.3 Ϯ 1.1 g/15 min g body weight). In summary, composition of SLIGRL-OH-induced saliva was similar to that of pilocarpine-induced saliva rather than that of -adrenergic stimulation (isoproterenol)-induced saliva, which contains abundant proteins (Slomiany et al, 1992). However, the ability of SLIGRL-OH to induce salivary secretion was lower than that of pilocarpine as shown in the total amylase activity.…”
Protease-activated receptor-2 (PAR-2) is expressed in the salivary glands and is expected to be a new target for the treatment of exocrine dysfunctions, such as dry mouth; however, the salivary secretory mechanism mediated by PAR-2 remains to be elucidated. Therefore, mechanism of the PAR-2-mediated salivary secretion was investigated in this study. We found that a PAR-2 agonist peptide, SLIGRL-OH, induced salivary flow in vivo and dose-dependent increase in [Ca 2ϩ ] i submandibular gland (SMG) acinar cells in wild-type (WT) mice and mice lacking M 3 or both M 1 and M 3 muscarinic acetylcholine receptors (mAChRs), whereas secretions in PAR-2 knockout (PAR-2KO) mice were completely abolished. The saliva composition secreted by SLIGRL-OH was similar to that secreted by mAChR stimulation. Ca 2ϩ imaging in WT acinar cells and -galactosidase staining in PAR-2KO mice, in which the -galactosidase gene (LacZ) was incorporated into the disrupted gene, revealed a nonubiquitous, sporadic distribution of PAR-2 in the SMG. Furthermore, compared with the secretion in WT mice, PAR-2-mediated salivary secretion and Ca 2ϩ response were enhanced in mice lacking M 3 or both M 1 and M 3 mAChRs, in which mAChR-stimulated secretion and Ca 2ϩ response in acinar cells were severely impaired. Although the mechanism underlying the enhanced PAR-2-mediated salivary secretion in M 3 -deficient mice is not clear, the result suggests the presence of some compensatory mechanism involving PAR-2 in the salivary glands deficient in cholinergic activation. These results indicate that PAR-2 present in the salivary glands mediates Ca 2ϩ -dependent fluid secretion, demonstrating potential usefulness of PAR-2 as a target for dry mouth treatment.
“…However the significant difference in total amylase secretion between SLIGRL-OH stimulation and pilocarpine stimulation demonstrates the higher activity of pilocarpine to induce salivary secretion and that the intracellular signaling of mAChR and PAR-2 is not completely the same. From these results, we consider that stimulation with SLIGRL-OH induces fluid secretion rather than protein secretion, which is mainly induced by -adrenergic stimulation (Slomiany et al, 1992), although some amount of amylase can be secreted as reported previously (Kawabata et al, 2000b(Kawabata et al, , 2002b. The results also indicate that sympathetic nervous activity is not involved in PAR-2-mediated salivary secretion.…”
Section: Discussionsupporting
confidence: 79%
“…Isoproterenol-induced salivary secretions were much less than pilocarpine-induced secretions: 1.6 Ϯ 0.3 l/g in WT, 1.7 Ϯ 0.1 l/g in M 1 KO, 1.0 Ϯ 0.4 l/g in M 3 KO, 1.3 Ϯ 0.4 l/g in M 1 /M 3 KO, and 1.8 Ϯ 0.2 l/g in PAR-2KO mice, which are consistent with the fact that -adrenergic, sympathetic stimulation evokes water secretion only slightly but mainly induces protein secretion after production of cyclic adenosine monophosphate (Slomiany et al, 1992).…”
supporting
confidence: 84%
“…Regarding the mass of protein secretion in 15 min, total protein in saliva secreted in response to isoproterenol (47.0 Ϯ 12.2 g/15 min g body weight, p Ͻ 0.05 or p Ͻ 0.01, comparing isoproterenol to pilocarpine or SLIGRL-OH) was much higher than that in response to pilocarpine (18.4 Ϯ 3.9 g/15 min g body weight) or SLIGRL-OH (3.3 Ϯ 1.1 g/15 min g body weight). In summary, composition of SLIGRL-OH-induced saliva was similar to that of pilocarpine-induced saliva rather than that of -adrenergic stimulation (isoproterenol)-induced saliva, which contains abundant proteins (Slomiany et al, 1992). However, the ability of SLIGRL-OH to induce salivary secretion was lower than that of pilocarpine as shown in the total amylase activity.…”
Protease-activated receptor-2 (PAR-2) is expressed in the salivary glands and is expected to be a new target for the treatment of exocrine dysfunctions, such as dry mouth; however, the salivary secretory mechanism mediated by PAR-2 remains to be elucidated. Therefore, mechanism of the PAR-2-mediated salivary secretion was investigated in this study. We found that a PAR-2 agonist peptide, SLIGRL-OH, induced salivary flow in vivo and dose-dependent increase in [Ca 2ϩ ] i submandibular gland (SMG) acinar cells in wild-type (WT) mice and mice lacking M 3 or both M 1 and M 3 muscarinic acetylcholine receptors (mAChRs), whereas secretions in PAR-2 knockout (PAR-2KO) mice were completely abolished. The saliva composition secreted by SLIGRL-OH was similar to that secreted by mAChR stimulation. Ca 2ϩ imaging in WT acinar cells and -galactosidase staining in PAR-2KO mice, in which the -galactosidase gene (LacZ) was incorporated into the disrupted gene, revealed a nonubiquitous, sporadic distribution of PAR-2 in the SMG. Furthermore, compared with the secretion in WT mice, PAR-2-mediated salivary secretion and Ca 2ϩ response were enhanced in mice lacking M 3 or both M 1 and M 3 mAChRs, in which mAChR-stimulated secretion and Ca 2ϩ response in acinar cells were severely impaired. Although the mechanism underlying the enhanced PAR-2-mediated salivary secretion in M 3 -deficient mice is not clear, the result suggests the presence of some compensatory mechanism involving PAR-2 in the salivary glands deficient in cholinergic activation. These results indicate that PAR-2 present in the salivary glands mediates Ca 2ϩ -dependent fluid secretion, demonstrating potential usefulness of PAR-2 as a target for dry mouth treatment.
“…1 Saliva is formed by many chemical components (among which lipid) that may interact with each other to form a ''dynamic continuum'' responsible for the chemical, physical and biological properties of the saliva. [2][3][4] Salivary lipids may bind non-covalently to mucin so contributing to the visco-elastic properties of mucus. 5,6 Salivary glands synthesize lipids actively, 7 but the factors regulating the lipid levels in saliva are still poorly known, although it has been discovered that the secretion of phospholipids is influenced both quantitatively and qualitatively by either cholinergic or b-adrenergic mediators 4,8,9 and that the acinar cells of salivary glands possess receptors responding to either sympathetic or parasympathetic systems.…”
Section: Introductionmentioning
confidence: 99%
“…10 Moreover, cells from sublingual glands in culture release phospholipids upon isoproterenol stimulation. 4,5,11 Cigarette smoke contains about 4000 chemicals, 400 of which are carcinogens. It also contains oxidants, such as oxygen radicals 12 and volatile aldehydes, 13 held responsible for damaging many biomolecules.…”
Salivary lipids are important for the maintenance of oral cavity health. Elevated salivary lipid levels are associated with an increase of caries incidence, plaque development, calculus formation and periodontal disease. However, the regulation of lipid salivary levels is scarcely known. Cigarette smoke is considered a risk factor for oral cavity diseases. We study how cigarette smoke may affect the secretion of salivary lipids. To this purpose, we determine the salivary levels of cholesterol and of glycerolipids in saliva sampled from smokers and non-smokers at various times of day. We observe an increase of glycerophospholipid and a decrease of cholesterol levels in the smokers’ saliva collected at 10 p.m. On the other hand, unsaturated fatty acids in chief phospholipids of saliva are lower in smokers at 7 a.m. Therefore, for the first time, we demonstrate that cigarette smoke induces variations of saliva lipid pattern in young people even moderately smoking.
The glandular secretions of the oral cavity lining the underlying buccal mucosa are highly specialized fluids which provide lubrication, prevent mechanical damage, protect efficiently against viral and bacterial infections, and promote the clearance of external pollutants. This mucus blanket contains large glycoproteins termed mucins which contribute greatly to the viscoelastic nature of saliva and affect its complex physiological activity. The protein core of mucins consists of repetitive sequences, rich in O-glycosylated serine and threonine, and containing many helix-breaking proline residues. These features account for the extended, somewhat rigid structure of the molecule, a high hydrodynamic volume, its high buoyant density, and high viscosity. The oligosaccharide moiety of salivary mucins accounts for up to 85% of their weight. The oligosaccharide side chains exhibit an astonishing structural diversity. The isolation, composition, structure, molecular characteristics, and functional relevance of salivary mucins and their constituents is discussed in relation to recent advancements in biochemistry and molecular biology.
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