Differential Expression of Human High-molecular-weight Salivary Mucin (MG1) and Low-molecular-weight Salivary Mucin (MG2)

Nielsen, Peter Aadal; Mandel, Ulla; Therkildsen, Marianne Hamilton; Clausen, Henrik

doi:10.1177/00220345960750110201

Cited by 65 publications

(55 citation statements)

References 24 publications

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“…The presence of MG2 in submandibular and sublingual serous cells, as described in this study and by Nielsen et al (1996Nielsen et al ( ,1997, but not in parotid serous cells, indicates that protein expression patterns differ among the serous cells of human salivary glands. A similar situation exists for the salivary glands of other species (Hand et al 1999).…”

Section: Resultssupporting

confidence: 54%

“…Immunohis-tochemical (IHC) and in situ hybridization (ISH) studies by Cohen et al (1991) and Khan et al (1998) suggest that MG2 also is present in and produced by mucous cells in the submandibular glands. On the other hand, similar studies by Nielsen et al (1996Nielsen et al ( , 1997 indicate that MG2 is present in a subset of the serous cells of these glands. Using the same antibody and nucleotide probes, Sharma et al (1998) described a differential localization of MG1 and MG2 in mucous and serous cells, respectively, of human bronchial submucosal glands.…”

supporting

confidence: 63%

“…Cohen et al (1990) also found that MG1 was restricted to mucous cells, but noted that some mucous cells were unreactive. A possible explanation for this difference is that the antibody used by Cohen et al (1990) was to a carbohydrate epitope, whereas the antibody used by Nielsen et al (1996) was a monoclonal antibody directed against an epitope on the apomucin. The antibody used in the present study is a polyclonal antibody that recognizes both polypeptide and carbohydrate epitopes (R.F.…”

Section: Resultsmentioning

confidence: 99%

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Electron Microscopic Immunogold Localization of Salivary Mucins MG1 and MG2 in Human Submandibular and Sublingual Glands

Piludu

Rayment²,

Liu³

et al. 2003

J Histochem Cytochem.

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S U M M A R YThe human salivary mucins MG1 and MG2 are well characterized biochemically and functionally. However, there is disagreement regarding their cellular and glandular sources. The aim of this study was to define the localization and distribution of these two mucins in human salivary glands using a postembedding immunogold labeling method. Normal salivary glands obtained at surgery were fixed in 3% paraformaldehyde-0.1% glutaraldehyde and embedded in Lowicryl K4M or LR Gold resin. Thin sections were labeled with rabbit antibodies to MG1 or to an N-terminal synthetic peptide of MG2, followed by gold-labeled goat anti-rabbit IgG. The granules of all mucous cells of the submandibular and sublingual glands were intensely reactive with anti-MG1. No reaction was detected in serous cells. With anti-MG2, the granules of both mucous and serous cells showed reactivity. The labeling was variable in both cell types, with mucous cells exhibiting a stronger reaction in some glands and serous cells in others. In serous granules, the electron-lucent regions were more reactive than the dense cores. Intercalated duct cells near the acini displayed both MG1 and MG2 reactivity in their apical granules. In addition, the basal and lateral membranes of intercalated duct cells were labeled with anti-MG2. These results confirm those of earlier studies on MG1 localization in mucous cells and suggest that MG2 is produced by both mucous and serous cells. They also indicate differences in protein expression patterns among salivary serous cells.

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Section: Resultssupporting

confidence: 54%

supporting

confidence: 63%

Section: Resultsmentioning

confidence: 99%

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Electron Microscopic Immunogold Localization of Salivary Mucins MG1 and MG2 in Human Submandibular and Sublingual Glands

Piludu

Rayment²,

Liu³

et al. 2003

J Histochem Cytochem.

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“…The site of MUC7 synthesis is controversial. One group localized MUC7 to serous acini in SMGs and LGs using immunohistochemistry and in situ hybridization [40,41]; whereas two other groups clearly defined mucous acini as the expression sites using the same techniques [42,43]. Furthermore, electron microscopic immunogold localization detected MUC7 in both serous and mucous cells with varying intensities [44].…”

Section: Muc7 Muc19 and Fcgbp Are Predominantly Expressed In Mucousmentioning

confidence: 99%

Expression Analysis of Human Salivary Glands by Laser Microdissection: Differences Between Submandibular and Labial Glands

Kouznetsova

Gerlach

Zahl

et al. 2010

Cell Physiol Biochem

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Both the major and minor salivary glands are the sources of saliva, a fluid vital for the maintenance of a healthy oral cavity. Here, the expression profiles of human submandibular (SMG) and labial glands (LG) were compared by RT-PCR analysis of laser microdissected mucous and serous cells, respectively. The focus was on trefoil factor family (TFF) genes, but also other genes encoding secretory proteins (mucins, lysozyme, amylase, statherin, and histatins) or aquaporin 5 were included. Immunofluorescence studies concerning TFF1-3, FCGBP, amylase, and lysozyme are also presented. It was shown that LGs clearly contain serous cells and that these cells differ in their expression profiles from serous SMG cells. Furthermore, all three TFF peptides, together with MUC5B, MUC7, MUC19, and FCGBP, were clearly detectable in mucous acini of both LGs and SMGs. In contrast, lysozyme was differentially expressed in LGs and SMGs. It can be expected that labial saliva may play a particularly important role for protecting the teeth.

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“…For such CF studies, the obvious mucins to be considered are those secreted by the bronchioles, but working with bronchial mucins poses special problems: not only are these almost impossible to collect from control individuals but those present in CF sputum will have been modified by the action of bacterial enzymes. Fortunately, two of the lung mucins, MUC-5B and MUC-7, are also expressed by the major salivary glands (known there as MG1 and MG2 respectively [10,11,12]); these glands also express CFTR [13,14]. In this study we tested the defective acidification hypothesis by comparing the glycosylation of MG1, MG2 and the mucin-like glycoprotein GL between CF and control groups.…”

Section: Introductionmentioning

confidence: 99%

Sulphation of the salivary mucin MG1 (MUC-5B) is not correlated to the degree of its sialylation and is unaffected by cystic fibrosis

Shori

Kariyawasam

Knight³

et al. 2001

Pfl�gers Archiv European Journal of Physiology

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Defective acidification of intracellular organelles, particularly the trans-Golgi network, has been proposed to explain the decreased sialylation and increased sulphation of secreted proteins in cystic fibrosis (CF). To test this hypothesis we compared expression of sulphate and sialic acid on three salivary mucins namely MG1 (MUC-5B), MG2 (MUC-7) and GL. Proteins in whole mouth saliva (WMS) from four individuals were separated by fast protein liquid chromatography (FPLC) on a Superdex 200 column and the partially purified mucins slot-blotted and assayed for sulphate content by staining with Alcian Blue. Sulphation varied with the individual and with the mucin: MG1 was the most sulphated and contributed almost the entire sulphate content of WMS. These results allowed us to test small volumes of WMS from 20 CF patients and age- and sex-matched controls for estimates of sulphate content on MG1. Wherever possible sulphate on MG1 was also visualised by staining washed SDS-PAGE gels with Alcian Blue at pH 1.0. To assess the sialic acid content of salivary mucins, electroblots of SDS-PAGE gels were probed with labelled Triticum vulgaris agglutinin. In summary, our results show MG1 to be the main sulphated protein in whole mouth saliva and there are large differences in the expression of sulphate and of sialic acid on this mucin, both in control and CF groups. CF led neither a decrease in sialylation nor an increase in sulphation and direct comparisons of sialic acid content with sulphate in MG1 failed to reveal any obvious link between the two in health or in disease. Our data thus do not support the hypothesis of defective acidification as the underlying cause of altered glycosylation in CF, but point instead to inter-individual differences in expression/functioning of terminal glycosyltransferases for published observations. We thank the European Union Biomed II programme for support.

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Differential Expression of Human High-molecular-weight Salivary Mucin (MG1) and Low-molecular-weight Salivary Mucin (MG2)

Cited by 65 publications

References 24 publications

Electron Microscopic Immunogold Localization of Salivary Mucins MG1 and MG2 in Human Submandibular and Sublingual Glands

Electron Microscopic Immunogold Localization of Salivary Mucins MG1 and MG2 in Human Submandibular and Sublingual Glands

Expression Analysis of Human Salivary Glands by Laser Microdissection: Differences Between Submandibular and Labial Glands

Sulphation of the salivary mucin MG1 (MUC-5B) is not correlated to the degree of its sialylation and is unaffected by cystic fibrosis

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