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RESEARCH REPORT |
1 Department of Dental Basic Sciences, Academic Centre for Dentistry Amsterdam (ACTA), Van der Boechorststraat 7, 1081 BT Amsterdam, the Netherlands;
2 Department of Oral & Maxillofacial Surgery/Oral Pathology, University Medical Centre Vrije Universiteit (VUMC), Amsterdam, The Netherlands; and
3 Department of Immunology and Microbiology, Institute for Medical Biology, University of Southern Denmark, 5000 Odense C, Denmark;
*corresponding author, fj.bikker.obc.acta{at}med.vu.nl
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ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONMATERIALS & METHODSRESULTSDISCUSSIONREFERENCES |
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KEY WORDS: immunohistochemistry • saliva • salivary gland • scavenger receptors
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONMATERIALS & METHODSRESULTSDISCUSSIONREFERENCES |
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Recently, it has been shown that agglutinin is identical to the lung glycoprotein gp-340, a member of the scavenger receptor cysteine-rich (SRCR) superfamily (Holmskov et al., 1997, 1999; Prakobphol et al., 2000;; Ligtenberg et al., 2001). SRCR domains are found widely in cell surface molecules and in some secreted proteins, where they are thought to mediate ligand binding (Resnick et al., 1994; Aruffo et al., 1997; Gough and Gordon, 2000).
gp-340 is a product of an alternatively spliced form of the DMBT1 gene (Holmskov et al., 1999; Mollenhauer et al., 2000), which codes for 3 distinct conserved protein domains, SRCR, CUB domains, and a zona pellucida (ZP) domain. These domains are involved in embryogenesis and development (Bork and Beckmann, 1993; Romero et al., 1997; Sinowatz et al., 2001). DMBT1, which is involved in epithelial differentiation, is a candidate tumor suppressor gene in medulloblastoma, glioblastoma multiforme, and lung and gastrointestinal tumors caused by homozygous deletions or by a lack of expression (Mollenhauer et al., 1997, 2000; Somerville et al., 1998; Mori et al., 1999; Wu et al., 1999).
Relatively little is known about the localization of agglutinin in salivary glands. In one study with a monoclonal antibody directed against a Lewis Y (LeY) epitope, agglutinin has been localized in the Golgi apparatus and in secretory granules of ductal and acinar cells of human parotid and submandibular salivary glands (Takano et al., 1991). However, the Lewis Y antigen is also present on the proline-rich glycoprotein (Gillece-Castro et al., 1991), which hampers an unambiguous interpretation. In the present study, we used monoclonal antibodies that originally had been raised against lung gp-340. Different localization patterns of agglutinin were found in the serous parotid gland, the seromucous submandibular glands, and the minor, primarily mucous, labial gland.
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MATERIALS & METHODS |
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TOPABSTRACTINTRODUCTIONMATERIALS & METHODSRESULTSDISCUSSIONREFERENCES |
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Collection of Human Saliva
Parotid secretions were collected with a Lashley cup under stimulation with sugar-free candies. Submandibular secretions were collected without conscious stimulation, by means of a custom-fitted device (Veerman et al., 1996). We collected unstimulated labial saliva by pipetting the saliva directly from the labial mucosa after the mucosa of the lower lip was dried. The study was approved by the Institutional Ethical Board of the Academic Hospital Vrije Universiteit at Amsterdam, and informed consent was obtained from all saliva donors. After collection, samples were directly processed for SDS-PAGE analysis.
Antibodies and Lectins
Monoclonal antibody (mAb) 213-1 (Holmskov et al., 1997, 1999) and mAb 213-6, both IgG1 subclass, were raised against gp-340 as described (Holmskov et al., 1997). mAb 5E9 recognizes sialidase-sensitive carbohydrate epitope expressed on salivary mucins (Veerman et al., 1991; Groenink et al., 1996). Rabbit polyclonal antibody CpMG2, evoked against a synthetic peptide corresponding to the C-terminal region of salivary mucin MUC7, recognizes native MUC7 in saliva (Bolscher et al., 1999). Digoxigenin–labeled MAA (Maackia amurensis agglutinin) is specific to N-acetylneuraminic acid (sialic acid) 
-2,3-linked to galactose, and digoxigenin-labeled SNA (Sambucus nigra agglutinin) is specific to N-acetylneuraminic acid -2,6-linked to galactose (Boehringer, Mannheim, Germany). Alkaline phosphatase conjugated to goat anti-rabbit IgG antibody and alkaline phosphatase conjugated to goat anti-mouse IgG antibody were obtained from Sigma (St. Louis, MO, USA).
SDS-PAGE and Western Blotting
Saliva samples were incubated at 100°C for 10 min in sample buffer containing 15 mM Tris-HCl, pH 6.8, 0.5% SDS, 2.5% glycerol, and 0.05% bromophenol blue. Reduced samples were prepared by incubation in sample buffer supplemented with 25 mM dithiothreitol (ICN Biomedicals, Aurora, OH, USA). SDS-PAGE was conducted on a Pharmacia Phast System (Pharmacia-LKB, Uppsala, Sweden) with 7.5% or 4-15% polyacrylamide gels, according to the manufacturer' protocol.
Immunodetection of proteins after SDS-PAGE was essentially as described (Bolscher et al., 1999). Nitrocellulose membranes were incubated with either antibodies or digoxigenin-labeled lectins. Bound antibodies were detected with alkaline phosphatase conjugated to rabbit anti-mouse immunoglobulins (DAKO, Glostrup, Denmark) with 5-bromo-4-chloro-3-indolyl-phosphate (X-P) and nitro blue tetrazolium chloride (NBT) (Boehringer, Mannheim, Germany) as substrate. Bound lectins were detected with anti-digoxigenin conjugated to alkaline phosphatase, in combination with X-P and NBT.
Glycan-affecting Treatments
The carbohydrate residues of agglutinin on Western blots were oxidized by an incubation with 20 mM sodium-meta-periodate (Merck, Darmstadt, Germany) in a 100-mM sodium acetate buffer, pH 4.2 (Woodward et al., 1984). Sialic acid residues were removed by incubation with Vibrio cholerae neuraminidase (0.1 U/mL) (Roche) in 50 mM of sodium acetate buffer containing 4 mM calcium chloride, pH 5.5, at 37°C for 16 hrs.
Immunohistochemistry on Human Tissue Specimens
Sections for immunohistochemistry were obtained from human salivary gland tissues that had been removed for therapeutic or diagnostic purposes by the Department of Oral & Maxillofacial Surgery/Oral Pathology (VUMC). For parotid tissue, N = 2 (male, 46 yrs; female, 65 yrs); for labial tissue, N = 3 (male, 55 yrs; female, 47 and 60 yrs); and for submandibular tissue, N = 2 (male, 69 yrs; female, 72 yrs). The study was approved by the Institutional Ethical Board of the Academic Hospital Vrije Universiteit at Amsterdam, and informed consent was obtained from all tissue donors.
Sections were cut from neutral-buffered formaldehyde-fixed paraffin-embedded tissue blocks and mounted on ChemMate Capillary Gap Slides (DAKO, Glostrup, Denmark), dried at 60°C, deparaffinized, and dehydrated. Antigen retrieval was performed by microwave heating in Target Retrieval Solution (DAKO, Glostrup, Denmark) for 11 min at full power (900 W), and 15 min at 400 W. After being heated, slides remained in the buffer for 15 min. Antigen retrieval was followed by blocking of endogenous biotin, by means of the Dako Biotin-Blocking System (DAKO, Glostrup, Denmark). Incubation with mAb 213-1 and mAb 213-6 (17 µg/mL) was done for 25 min at room temperature. Immunostaining was automated with use of the ChemMate HRP/DAB detection kit, K5001 (DAKO, Glostrup, Denmark) on the TechMate 1000 instrument (DAKO, Glostrup, Denmark). Immunostaining was followed by brief nuclear counter staining in Mayer' hematoxylin. Finally, coverslips were mounted with AquaTex (Merck, Darmstadt, Germany). Controls were performed by replacement of the primary monoclonal antibody with an unrelated monoclonal antibody of the same subclass as the gp–340 antibodies (IgG1).
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RESULTS |
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TOPABSTRACTINTRODUCTIONMATERIALS & METHODSRESULTSDISCUSSIONREFERENCES |
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).
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, lane C). The reaction with SNA lectin, recognizing N-acetylneuraminic acid -2,6-linked to galactose, was negative (not shown), suggesting that agglutinin contains only -2,3-linked sialic acid residues. After treatment of the membrane with meta-periodate, the recognition by mAb 213-1, lectin MAA, and mAb 5E9 was destroyed, whereas the epitope recognized by mAb 213-6 remained intact (Fig. 2, lane P). These results indicate that mAb 213-1, like lectin MAA and mAb 5E9, is directed against a carbohydrate epitope. When sialic acid residues were removed by treatment of the nitrocellulose membranes with neuraminidase, the binding of mAb 213-1, lectin MAA, and mAb 5E9 was lost. This suggests that the presence of sialic acid residues is required for recognition by mAb 213-1. In contrast, the epitope recognized by mAb 213-6 remained intact (Fig. 2, lane N).
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). This shows that the epitope recognition of mAb 213-6 is dependent on the presence of intact disulfide bonds and thereby subject to the native, three-dimensional structure of the protein. Periodate and neuraminidase treatment of agglutinin did not abolish the recognition by mAb 213-6 (Fig. 2). Analysis of these data suggests that mAb 213-6 is directed to peptide domains of agglutinin.
To examine whether mAb 213-1 and mAb 213-6 cross-react with other salivary proteins, we immunoblotted parotid and submandibular saliva with mAb 213-1 and mAb 213-6. In parotid saliva, both mAbs labeled only agglutinin (Fig. 3, lanes 1, 3). Immunoblotting of submandibular saliva with mAb 213-1 revealed an additional band at a lower Mr position (Fig.3, lane 2). Immunoblotting with polyclonal antibody CpMG2 suggested that this band corresponded to MUC7 (Fig. 3, lane 6).
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).
It was found that salivary agglutinin was differentially localized in distinct salivary gland tissues (Fig. 4). Both mAbs gave very similar staining patterns in the serous parotid glandular tissue. Strong cytoplasmic labeling was found in the striated duct cells. The excretory and intercalated ducts were stained as well, albeit less intensely. The serous acini were negative (Figs. 4A-4D).
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). In acinar cells, a diffuse cytoplasmic staining was noted. In addition, cytoplasmic granules were stained. The serous cells that were not labeled did not contain cytoplasmic granules. The duct cells and the mucous acini, which consist of larger cells that are more transparent than the serous acinar cells, were negative.
In the labial gland, mainly the serous demilune and serous acini were stained (Figs. 4G, 4H). Furthermore, staining was also found at the luminal side of duct cells. Again, the mucous acini were negative.
The typical localization patterns were observed in all glandular tissues studied. Controls were negative.
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DISCUSSION |
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TOPABSTRACTINTRODUCTIONMATERIALS & METHODSRESULTSDISCUSSIONREFERENCES |
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Previously, it has been found that removal of N-linked carbohydrates from agglutinin did not affect the binding of mAb 213-1 (Holmskov et al., 1997). The present finding that mAb 213-1 reacts with a neuraminidase-sensitive epitope (Fig. 2) indicates that the epitope of mAb 213-1 is associated with O-linked oligosaccharide chains. Potential O-glycosylation sites, serine and threonin, are abundantly present in agglutinin.
mAb 213-6 recognizes a conformational epitope that is sensitive for reduction of disulfide bonds. Agglutinin consists of numerous domains containing disulfide bonds, including SRCR domains, CUB domains, and a ZP domain (Romero et al., 1997; Bauskin et al., 1999; Hohenester et al., 1999).
Agglutinin could be demonstrated in parotid, submandibular, and labial salivary secretions (Fig. 1). Histochemistry revealed a differential localization pattern of agglutinin in these glands. In all tissues studied, agglutinin was demonstrated in serous cells. However, in parotid gland tissue, agglutinin was present only in striated duct cells, while the serous acini were negative. This result is different from those of Takano and co-workers (1991). They localized agglutinin in both acini and ducts in parotid glandular tissue by using mAb 303, recognizing a LeY epitope. As stated by Gillece-Castro and co-workers (1991), proline-rich glycoproteins (PRG) also contain the LeY epitope (1991). Besides, Lantini and Cossu (1998) studied the distribution of Le-antigens in salivary tissue and found LeY reactivity in both duct cells and acini. Thus, it is possible that the acinar labeling found by Takano et al. reflected the presence of PRG.
In the submandibular gland, staining for agglutinin was found in serous acinar cells and demilune cells, while in this tissue the duct cells were negative. Acini that were negative were devoid of granules, suggesting that, in these cells, release of the intracellular components had taken place, possibly during the processing of the tissue for histochemical examination. In contrast to Takano and co-workers, we did not observe labeling of submandibular duct cells. Again, the discrepancy between their study and the present one might be due to the broader specificity of the anti-LeY antiserum they used. This is corroborated by the finding of Lantini and Cossu (1998), who found anti-LeY immunoreactivity in both duct cells and acinar cells of the submandibular gland.
In the labial gland, mainly serous cells, including the acinar cells, demilune cells, and duct cells were positive for agglutinin, while mucous cells were negative. Similar differences between glandular localization patterns have been reported for lysozyme. It has been demonstrated that, in the parotid gland, lysozyme was expressed only in the intercalated duct cells, not in the acinar cells. On the other hand, in the sublingual glands and in the minor oral glands, both the serous acini and the ducts were positive (Mitani et al., 1989). This suggests that the serous acinar cells of the (sero)mucous glands are less differentiated than those of the parotid gland.
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ACKNOWLEDGMENTS |
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Received June 7, 2001; Last revision December 14, 2001; Accepted December 18, 2001
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