Patterns of secretion of mucins and non-mucin glycoproteins in human submandibular/sublingual secretion

• Published in: Archives of oral biology 2003-02, Vol.48 (2), p.147-154
• Main Authors: Becerra, Laura, Soares, Rodrigo V, Bruno, Lucila S, Siqueira, Camille C, Oppenheim, Frank G, Offner, Gwynneth D, Troxler, Robert F
• Format: Article
• Language: English
• Subjects: Adult; Blotting, Western - methods; Dentistry; Electrophoresis, Polyacrylamide Gel - methods; Female; Glycoprotein; Glycoproteins - isolation & purification; Glycoproteins - metabolism; Humans; Male; MG1; MG2; Mucin-5B; Mucins - isolation & purification; Mucins - metabolism; Saliva - metabolism; Secretion pattern; Secretory Rate; Sublingual Gland - metabolism; Submandibular Gland - metabolism; Submandibular/sublingual gland
• ISSN: 0003-9969; 1879-1506
• DOI: 10.1016/S0003-9969(02)00171-1

The present investigation has characterised the influence of gustatory stimulation and duration of stimulation on the secretion pattern of salivary mucins MG1 and MG2 and non-mucin glycoproteins in submandibular/sublingual secretion (SMSL). Resting SMSL was collected for three 2 min intervals and stimulated SMSL was collected for ten 1 min intervals from six healthy subjects. Flow rates and total protein were significantly different under the two conditions. The secretion patterns of these proteins under resting and stimulated conditions was examined on periodic acid-Schiff reagent (PAS)-stained polyacrylamide gels using a Kodak Digital-Science Image Station. Image analyses revealed that the level of MG1 increased and the level of MG2 remained nearly the same after stimulation. Six other major glycoproteins (designated Band 1–6) were identified on the basis of their electrophoretic mobilities and immuno-reactivity on Western blots. After stimulation the intensity of Band 1 (lactoferrin and peroxidase) and Band 2 (amylase) decreased whereas the intensity of Band 3 (carbonic anhydrase), Band 4 (proline-rich glycoprotein) and Bands 5 and 6 (basic glycosylated proline-rich proteins) increased. These patterns probably reflect secretion from preformed vesicles since de novo synthesis would be unexpected within the time frame of these experiments. The variable patterns observed suggest that mucins and non-mucin glycoproteins in SMSL derive from different subsets of secretory vesicles, some of which may originate in mucous and others in serous acini, as well as in ductal cells. Quantification of mucins was performed by image analysis technology using purified MG1 and MG2 standards. Finally, the present investigation has shown that the secretory patterns of mucins and non-mucin glycoproteins from submandibular/sublingual glands are complex and represent an important aspect of salivary gland physiology.