Dataset Information

Mass spectrometry-based analyses showing the effects of secretor and blood group status on salivary N-glycosylation.

ABSTRACT: BACKGROUND:The carbohydrate portions of salivary glycoproteins play important roles, including mediating bacterial and leukocyte adhesion. Salivary glycosylation is complex. Many of its glycoproteins present ABO and Lewis blood group determinants. An individual's genetic complement and secretor status govern the expression of blood group antigens. We queried the extent to which salivary glycosylation varies according to blood group and secretor status. First, we screened submandibular/sublingual and parotid salivas collected as ductal secretions for reactivity with a panel of 16 lectins. We selected three lectins that reacted with the largest number of glycoproteins and one that recognized uncommon lactosamine-containing structures. Ductal salivas representing a secretor with complex blood group expression and a nonsecretor with a simple pattern were separated by SDS-PAGE. Gel slices were trypsin digested and the glycopeptides were individually separated on each of the four lectins. The bound fractions were de-N-glycosylated. LC-MS/MS identified the original glycosylation sites, the peptide sequences, and the parent proteins. RESULTS:The results revealed novel salivary N-glycosites and glycoproteins not previously reported. As compared to the secretor, nonsecretor saliva had higher levels of N-glycosylation albeit with simpler structures. CONCLUSIONS:Together, the results suggested a molecular basis for inter-individual variations in salivary protein glycosylation with functional implications for oral health.

SUBMITTER: Albertolle ME

PROVIDER: S-EPMC4696288 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Mass spectrometry-based analyses showing the effects of secretor and blood group status on salivary N-glycosylation.

Albertolle Matthew E ME Hassis Maria E ME Ng Connie Jen CJ Cuison Severino S Williams Katherine K Prakobphol Akraporn A Dykstra Andrew B AB Hall Steven C SC Niles Richard K RK Ewa Witkowska H H Fisher Susan J SJ

Clinical proteomics 20151230

<h4>Background</h4>The carbohydrate portions of salivary glycoproteins play important roles, including mediating bacterial and leukocyte adhesion. Salivary glycosylation is complex. Many of its glycoproteins present ABO and Lewis blood group determinants. An individual's genetic complement and secretor status govern the expression of blood group antigens. We queried the extent to which salivary glycosylation varies according to blood group and secretor status. First, we screened submandibular/su ...[more]

PMID: 26719750

Similar Datasets

Project description:BackgroundHuman ABO blood group type and the antigenic secretor status are hypothesized to associate with oral diseases including oral cancer. Secretor status is the ability of individuals to secrete blood group antigens into body fluids. This study aimed to evaluate the secretor status of ABO antigens of saliva in patients with oral cancers or oral potentially malignant disorders (OPMDs) relative to healthy adults.MethodsA systematic and comprehensive online search from inception to April 28, 2022, was carried out in MEDLINE, Embase, PsycInfo, and Emcare. The language was limited to English. Yielded records were screened by two independent reviewers at the title and abstract phase and at full-text screening. Studies investigating adults (≥ 18 years) with oral cancers or oral potentially malignant disorders compared to adults free of oral cancer were included in this study. Data were extracted according to the planned objectives. Methodological quality was assessed, and the findings were analyzed narratively. Meta-analyses were conducted to pool the odds of the non-secretor status of oral cancers and OPMDs compared to healthy adults.ResultsThe search included a total of 34 studies from three databases. Nine duplicates were removed. During the title and abstract screening, 11 irrelevant studies were excluded. Twelve studies were screened during the full-text screening, and eight articles were eligible to be included in the final analysis. A pooled odds ratio (OR) of 3.80 (95%CI, 1.53-9.44) was estimated when pooled 1254 oral cancers and oral potentially malignant disorders patients compared to 666 healthy adults.Discussion and conclusionThe odds of being a non-secretor appear to be approximately 3.8 times higher in patients with oral cancers and oral potentially malignant disorders compared to healthy adults. The lack of ABO blood group antigens in body fluids of non-secretors is more exposed to exogenous antigens than secretors. The host-parasite interactions of secretors and non-secretors underlying oral cancer and other diseases may be evidence to support or refuse them. Clinicians may use the secretor status as a detection test during their regular oral check-ups for high-risk populations for oral cancers. Non-secretors can be given more attention considering them as high-risk groups, and in terms of prognosis, differences between these two groups may be expected.

Project description:Canine oral tumors are relatively common neoplasms in dogs. For disease monitoring and early diagnosis, salivary biomarkers are appropriate because saliva collection is non-invasive and requires no professional skills. In the era of omics, matrix-assisted laser desorption/ionization with time-of-flight mass spectrometry (MALDI-TOF MS) coupled with liquid chromatography-tandem MS (LC-MS/MS) are suitable to identify potential disease-associated peptides and proteins. The present study aimed to use MALDI-TOF MS and LC-MS/MS to search for particular peptide mass fingerprints (PMFs) and conceivable biomarkers in saliva of dogs with early- and late-stage oral melanoma (EOM and LOM, respectively), oral squamous cell carcinoma (OSCC), benign oral tumors (BN), and periodontitis and healthy controls (CP). Pooled saliva samples in each group were used to be representative of population change. Unique PMFs were obtained and specific peptide fragments were sequenced by LC-MS/MS and BLAST-searched with mammalian protein databases. Seven peptide fragments appeared in the tumor groups (EOM, LOM, OSCC and BN) at 1096, 1208, 1322, 1794, 1864, 2354 and 2483 Da, two peptide fragments appeared in the LOM and OSCC groups at 2450 and 3492 Da, and in the CP controls at 2544 and 3026 Da. Also, protein-chemotherapy drug interaction networks were exhibited. Using western blot analysis, the expression of sentrin-specific protease 7 (SENP7), a peptide fragment at 1096 Da, in OSCC was significantly increased, as was the expression of TLR4, a peptide fragment at 3492 Da, in LOM and OSCC, compared with the CP group. The expression of nuclear factor kappa B (NF-κB), a TLR4 partner, was notably increased in OSCC compared with CP, BN and EOM. The expression was also enhanced in LOM compared with EOM. Expressed protein sequences from western blots were verified by LC-MS/MS. Western blots were then performed with individual samples in each group. The results showed the elevated expression of TLR4 in LOM and OSCC, compared with that in CP and BN, the increased expression of NF-κB in LOM and OSCC, compared with CP and in LOM compared with BN, and the enhanced expression of SENP7 in LOM and OSCC, compared with that in CP and BN. In conclusion, discrete clusters of EOM, LOM, OSCC, BN and CP groups and potential protein candidates associated with the diseases were demonstrated by salivary proteomics. Western blot analysis verified SENP7, TLR4 and NF-κB as potential salivary biomarkers of canine oral tumors.

Dataset Information

Mass spectrometry-based analyses showing the effects of secretor and blood group status on salivary N-glycosylation.

Publications

Mass spectrometry-based analyses showing the effects of secretor and blood group status on salivary N-glycosylation.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets