Search

We describe an antibody-lectin sandwich assay for quantitation of glycoforms of proteins. The assay uses deglycosylated IgG antibody immobilized on a microtiter plate to capture the protein of interest from the sample. The particular glycoform is then identified by reaction with biotin-labeled lectin, which is measured using streptavidin/alkaline phosphatase. The assay can be adapted to quantitate any protein’s glycoforms by simply substituting the antibody and lectin with specific alternatives

The aims of the present study were to investigate whether the tachykinins substance P and neurokinin A were present in gingival crevicular fluid in both periodontal health and disease and to study the relationship with periodontal inflammation. Gingival crevicular fluid (GCF) was collected from a healthy, a gingivitis and a periodontitis site in 20 subjects with periodontitis and from a healthy site in 20 subjects without periodontitis. The volume of GCF was measured and each sample subsequently analysed for substance P and neurokinin A by radioimmunoassay. There were significantly increased levels of substance P-like immunoreactivity (SP-LI) and neurokinin A-like immunoreactivity (NKA-LI) in gingivitis and periodontitis sites compared with healthy sites. Both tachykinins were significantly elevated in periodontitis affected subjects, with significantly more tachykinin-like immunoreactivity at healthy sites in periodontitis affected compared with periodontally-healthy subjects. Despite the considerable individual variation in the levels of SP-LI and NKA-LI, both tachykinins were present at levels at which they could have biological activity. It is concluded that substance P and neurokinin A may have a role in the pathogenesis of periodontal disease and that further investigations could prove useful in clarifying the mechanisms through which neuropeptides could modulate periodontal health and disease.

A. Glasgow1, A. Scott1, M. McCrudden1, D. McLean1, F. Lundy1, C. Irwin2, D. Timson3, M. Tunney4, J.S. Elborn1, S. Weldon1, C. Taggart1. 1Queen’s University Belfast, Centre for Infection and Immunity, Belfast, United Kingdom; 2Queen’s University Belfast, Centre for Dental Education, Belfast, United Kingdom; 3Queen’s University Belfast, School of Biological Sciences, Belfast, United Kingdom; 4Queen’s University Belfast, School of Pharmacy, Belfast, United Kingdom

The aims of the present study were to investigate whether calcitonin gene-related peptide (CGRP) was present in gingival crevicular fluid in both periodontal health and disease and to study the relationship with periodontal inflammation. Gingival crevicular fluid (GCF) was collected from a healthy, a gingivitis and a periodontitis site in 18 subjects with periodontitis and from a healthy site in 19 subjects without periodontitis. The volume of GCF was measured and each sample subsequently analysed for CGRP by radioimmunoassay. In subjects with periodontitis, CGRP immunoreactivity (CGRP-IR) was not detected in any periodontitis sites, nor in 67% of gingivitis and 28% of periodontallyhealthy sites. The total amount of CGRP-IR was significantly elevated in periodontally healthy (p=0.0015) and gingivitis (p=0.027) compared with periodontitis sites. CGRP-IR was present in 89% of the healthy sites sampled in control subjects at comparable levels to those in healthy sites in periodontitis subjects. It is concluded that in periodontal inflammation, particularly in deep pockets, constituents of GCF process and degrade CGRP.

Objective. This study was to investigate the potential role of salivary glycoproteins in burning mouth syndrome. Study design. This study compared major parotid glycoproteins in a group of patients with burning mouth syndrome and age-, sex-, race-matched healthy controls. Results. By use of a glycoprotein detection kit, saliva from both patients and controls exhibited three major parotid glycoprotein banding patterns consisting of either one or two bands, molecular weights 58 kDa and 77 kDa. The strong lectin reactivity of major parotid glycoproteins with Ricinus communis agglutinin suggests that galactose is the most prevalent terminal sugar. In addition, major parotid glycoproteins were shown to express blood group antigen H. On the basis of metachromatic characteristics and immunologic reactivity, major parotid glycoproteins appear to be members of the proline rich protein multigene family, proline rich glycoprotein, genetic polymorphism G1. No qualitative difference was observed in major parotid glycoprotein banding patterns between patients and controls. Conclusion. These findings do not support a role for major parotid glycoproteins in burning mouth syndrome.