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

Becerra, L.; Soares, Rodrigo Villamarim; Bruno, Lucila S; Siqueira, Camille C.; Oppenheim, Frank G.; Offner, Gwynneth D.; Troxler, Robert F.

doi:10.1016/s0003-9969(02)00171-1

Cited by 44 publications

(29 citation statements)

References 28 publications

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“…Previously, we have conducted studies on the physiology of mucin secretion in SMSL [29,30]. Therefore, we asked the question whether the secretory pattern of the split MG2 bands would be influenced by gustatory stimulation and duration of the stimulus.…”

Section: Secretion Patternsmentioning

confidence: 99%

An unusual glycoform of human salivary mucin MG2

et al. 2011

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Since in a previous study we encountered a subject with an unusual split MG2 banding pattern, the aim of this study was to investigate the molecular basis of this observation. Submandibular/sublingual secretion was collected under resting and stimulated conditions and examined on Western blots probed with anti-MG2 antibodies or on gels stained with periodic acid-Schiff reagent. Genomic DNA was isolated and the N-, tandem repeat (TR), and C-terminal regions of MUC7 were amplified by PCR since MG2 is known to display a genetic polymorphism. Although the typical appearance of MG2 on blots and gels is a single 180 kDa band, salivary secretions from the subject exhibited doublet immunoreactive bands of approximately 180 and 125 kDa. Additionally, under resting conditions the 180 kDa band was predominant whereas upon stimulation the 125 kDa band became predominant. Genomic DNA analysis showed that MUC7 in the individual with split MG2 bands was not truncated and that the MUC7 genotype in this individual was (6/6) where both alleles encoded six TRs. The MG2 split banding pattern observed in this subject was not derived from proteolytic degradation of this salivary mucin in whole saliva or from genetic polymorphism. The expression of two isoforms of MG2 could in principle improve or reduce the activity of this key component of the oral host defense system.

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Section: Secretion Patternsmentioning

confidence: 99%

An unusual glycoform of human salivary mucin MG2

et al. 2011

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“…These observations are consistent with the fact that buffering capacity is not dependent on the carbohydrate fraction of salivary glycoproteins, as this part has no measurable buffering value. Thus, the fact that the carbohydrate composition of the salivary mucins can be as high as 80%, whereas it is less than 5% in the case of amylase (Becerra et al 2003), may explain the lack of a correlation. There are many published reports on the concentration levels of salivary proteins.…”

Section: Discussionmentioning

confidence: 99%

“…Saliva contains other glycoproteins that could interfere with mucin detection. The measurement error, however, was assumed to be small, as these glycoproteins contain small carbohydrate fractions or exist at a low concentration in saliva (Becerra et al 2003). The salivary protein concentration of human saliva depends on the measurement technique and the protein standard.…”

Section: Discussionmentioning

confidence: 99%

Role of amylase, mucin, IgA and albumin on salivary protein buffering capacity: A pilot study

Cheaib

Lussi

2013

J Biosci

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It has been suggested that proteins serve as major salivary buffers below pH5. It remains unclear, however, which salivary proteins are responsible for these buffering properties. The aim of this pilot study was to evaluate the correlation between salivary concentration of total protein, amylase, mucin, immunoglobulin A (IgA), albumin and total salivary protein buffering capacity at a pH range of 4-5. In addition, the buffering capacity and the number of carboxylic acid moieties of single proteins were assessed.Stimulated saliva samples were collected at 9:00, 13:00 and 17:00 from 4 healthy volunteers on 3 successive days. The buffering capacities were measured for total salivary protein or for specific proteins. Also, the concentration of total protein, amylase, mucin, IgA and albumin were analysed.Within the limits of the current study, it was found that salivary protein buffering capacity was highly positively correlated with total protein, amylase and IgA concentrations. A weak correlation was observed for both albumin and mucin individually. Furthermore, the results suggest that amylase contributed to 35% of the salivary protein buffering capacity in the pH range of 4-5.

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“…Parotid saliva is a serous fluid whose protein diffuses homogeneously. On the contrary, submandibular/sublingual saliva and whole saliva exhibit viscoelastic properties that have been related to the presence of the MG1 and MG2 mucins and to intermolecular interactions between them and with other salivary macromolecules (29,30). Both salivary subtypes display a biphasic mode of diffusion (25).…”

Section: Discussionmentioning

confidence: 99%

“…Saliva was analyzed for protein concentration, mode of protein diffusion on cellulose membranes, unidimensional sodium dodecylsulfate (SDS)-polyacrylamide gel electrophoresis protein profiles and zymographic profiles of metalloproteinase 2 (MMP-2) and metalloproteinase 9 (MMP-9). Parotid saliva of ICRP patients showed an increased protein concentration, altered mode of protein diffusion, a higher frequency of polypeptide bands of 43, 37,33,29,26,16, and 10 kD, higher asymmetry in the polypeptide profiles of both contralateral parotid saliva, and an increase in the frequency of MMP-2 and MMP-9. Parotid saliva of patients with ICRP is molecularly altered with respect to normal saliva.…”

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confidence: 96%

Molecular Alterations of Parotid Saliva in Infantile Chronic Recurrent Parotitis

et al. 2007

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Infantile chronic recurrent parotitis (ICRP) is an insidious disease whose etiopathogenesis remains an enigma. Alterations in the physical appearance of parotid saliva from ICRP patients have been frequently reported. However, sialochemical studies in regard to ICRP are very rare. The aim of this study was to determine whether saliva of ICRP patients presents major physicochemical and biochemical alterations compared with saliva from paired healthy controls. Parotid, whole, and submandibular/sublingual saliva was collected at an asymptomatic stage from 33 ICRP patients (5-16 y old, both sexes) and from 33 sex-and age-matched healthy controls. Saliva was analyzed for protein concentration, mode of protein diffusion on cellulose membranes, unidimensional sodium dodecylsulfate (SDS)-polyacrylamide gel electrophoresis protein profiles and zymographic profiles of metalloproteinase 2 (MMP-2) and metalloproteinase 9 (MMP-9). Parotid saliva of ICRP patients showed an increased protein concentration, altered mode of protein diffusion, a higher frequency of polypeptide bands of 43, 37,33,29,26,16, and 10 kD, higher asymmetry in the polypeptide profiles of both contralateral parotid saliva, and an increase in the frequency of MMP-2 and MMP-9. Parotid saliva of patients with ICRP is molecularly altered with respect to normal saliva. Some of the molecular differences could be related to the etiopathogenesis of the disease. ICRP is an inflammatory disease associated with nonobstructive glandular sialectasia. It is characterized by recurrent episodes of swelling of one or both parotid glands that alternate with remission intervals lasting for weeks or months in which glands are clinically asymptomatic (1,2). The onset of the disease usually occurs around age 3 y. Symptoms may diminish and disappear spontaneously after puberty. Sometimes the disease may persist until adulthood (1-3).Among the postulated etiological factors of ICRP are congenital ductal malformations, genetic factors, allergies, bacterial infections, local manifestations of autoimmune disease, and immunodeficiencies (1,2,4 -9). However, none of them has been demonstrated to play a causative role in the disease, and to date its etiopathogenesis remains an enigma.Likewise, consensus on the therapeutic management of ICRP has yet to be achieved. Different specialists have opted for different therapies. Among the therapeutic indications described in the specialized literature is a diversity of physical maneuvers to stimulate the salivary flux (1) and pharmacotherapy with nonsteroid anti-inflammatory agents (7) in combination with sialogogues and/or antibiotics (3,6,10). Recently, Nahlieli et al. (11) proposed an interventional approach using a sialendoscope. In cases in which irreversible damage has occurred, ligation of the excretory duct is indicated to produce glandular atrophy (1,2). In severe cases, partial or total parotidectomy is prescribed as a last resource (1,2,12).Studies on glandular tissue obtained from patients with ICRP have shown lymphocyt...

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

Cited by 44 publications

References 28 publications

An unusual glycoform of human salivary mucin MG2

An unusual glycoform of human salivary mucin MG2

Role of amylase, mucin, IgA and albumin on salivary protein buffering capacity: A pilot study

Molecular Alterations of Parotid Saliva in Infantile Chronic Recurrent Parotitis

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