Disease relevance of Sublingual Gland

• We here in present a very rare case of primary localized amyloidosis with amyloid A protein of the sublingual gland [1].
• Cervical ranulas, known also as plunging or burrowing ranulas, are an outcome of extravasated sublingual gland mucin that has gained access to the soft tissues of the neck [2].

High impact information on Sublingual Gland

• We have purified and characterized the blarina toxin (BLTX), a lethal mammalian venom with a tissue kallikrein-like activity from the submaxillary and sublingual glands of the short-tailed shrew Blarina brevicauda [3].
• Moreover, one part of this peptide is identical to the 196-amino acid sequence deduced from the cDNA clone pSM2-1, which codes for a part of the high molecular weight mucin MG1 isolated from human sublingual gland [4].
• Morphologic changes were less marked in the sublingual glands, although mucin levels were noticeably depressed by Day 12 of deficiency [5].
• Following the oral dosing of deficient animals (T12) with 350 micrograms retinyl palmitate, all such changes were reversed within 6 days in the trachea and within 10 days in the submaxillary and sublingual glands [5].
• Alkaline borohydride reductive cleavage of the major glycoprotein fraction of rat sublingual gland resulted in the release of a series of reduced oligosaccharides [6].

Biological context of Sublingual Gland

• These findings suggest that epinephrine enhanced oxygen consumption in sublingual gland slices by activation of alpha 2-adrenergic receptors, while carbachol activated muscarinic receptors; activation of both receptors mediated the respiratory response by facilitating the entry of extracellular Ca [7].
• Furthermore, the roles of these amino acids, GABA and glutamate, on salivation were analyzed in the rat submandibular and sublingual glands [8].
• The animals were killed, their sublingual glands dissected, and the glandular tissue used for quantization of TNF-alpha expression and the assays of acinar cells apoptosis employing sandwich enzyme immunoassay for histone-associated DNA fragments [9].
• A human sublingual gland cDNA library was screened with a polyclonal antiserum against deglycosylated MG1 and a positive clone, pSM2-1, was isolated which codes for 196 amino acids in the carboxyl-terminal region of this mucin [10].
• The development of vasoactive intestinal peptide, substance P and calcitonin gene-related peptide in parotid, submandibular and sublingual glands of the male rat was followed by immunochemistry and immunocytochemistry [11].

Anatomical context of Sublingual Gland

• Immunohistochemistry revealed that MUC5B is produced by cells dispersed throughout the human submandibular and sublingual glands, in the airway submucosal glands as well as the goblet cells, and in the epithelium and glands of the endocervix [12].
• UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase was derived from rat parotid, submandibular, and sublingual glands, liver and kidney as well as from human colostrum [13].
• First, submandibular glands had a lower basal activity of nitric oxide synthase than sublingual glands and the concentration-response curve for carbachol was bell-shaped in the former but not in sublingual glands [14].
• Immunoelectron microscopy (IM) revealed antigen (GAA 108) localization in the medial and trans-Golgi cisternae and trans-Golgi network (TGN), including condensing vacuoles, in parotid, exorbital lacrimal, and pancreatic acinar cells, and serous acinar cells of sublingual gland [15].
• AQP5 was found in secretory acinar cells of submandibular, parotid, and sublingual glands, where it was restricted to apical membranes including intercellular secretory canaliculi [16].

Associations of Sublingual Gland with chemical compounds

• Cyclic AMP in the sublingual glands of the mouse [17].
• Selective localization and abundance of the enzyme suggest a previously unrecognized role of the sublingual gland in thyroid hormone physiology [18].
• Analysis of the soluble protein fractions from the rat parotid, submandibular and sublingual glands by polyacrylamide-gel electrophoresis reveals similarities in overall patterns of protein synthesis at birth [19].
• Homogenates from male ddy mouse sublingual glands were incubated with 100 nM [125I]rT3 in the presence of 2 mM dithiothreitol (DTT) [18].
• EGTA prolonged the effect of the PDE-inhibitors, indicating that Ca2+-ions may be involved in the maintenance of the cyclic AMP concentration in the sublingual glands [17].

Gene context of Sublingual Gland

• However, no evidence for proteins derived from an Smgb-like gene was observed in neonatal mouse submandibular or sublingual glands [20].
• Previously, we isolated a clone (pSM2-1) from a human sublingual gland cDNA expression library using an antibody against deglycosylated MG1 (Troxler et al., Biochem. Biophys. Res Commun., 217, 1112-1119, 1995) [21].
• Northern blot analysis also demonstrated that MUC7 is not expressed in the submandibular/sublingual gland complexes of hamster, mouse and rat [22].
• Examination of Nkx2-3 null mice revealed defects in maturation and cellular organisation of the sublingual glands [23].
• Comparative Northern analyses between the major salivary glands demonstrate highly selective Muc19 expression in neonatal and adult sublingual glands, whereas Smgc is expressed in neonatal submandibular and sublingual glands [24].

Analytical, diagnostic and therapeutic context of Sublingual Gland

• Cannulation of sublingual glands in animals receiving high doses of atropine produced no measurable secretion upon pilocarpine stimulation [25].
• 5. Serum-free organ cultures were established, in which SG rudiments that contained SMG and sublingual gland (SLG) primordia (explant 1) and SMG/SLG rudiments with peripheral tissue that included part of the tongue muscle (explant 2) were isolated from E13.5 or E14 embryos [26].
• The concentration of bFGF in the submandibular/sublingual gland, as determined by radioimmunoassay, was approximately 80% that in the brain [27].
• Perfusion of both submandibular and sublingual glands with unlabelled L-serine (25 mM) or L-phenylalanine (30 mM) resulted in a significant decrease in the silver grain density associated with each labelled amino acid [28].
• The mean value for TNF-alpha in sublingual gland of the control group was 22.3 pg/mg of protein and showed a 1.6-fold increase in the chronic ethanol diet group to 36.5 pg/mg of protein [9].

References