Integrated glycomics strategy for the evaluation of glycosylation alterations in salivary proteins associated with type 2 diabetes mellitus. Issue 65 (1st November 2020)
- Record Type:
- Journal Article
- Title:
- Integrated glycomics strategy for the evaluation of glycosylation alterations in salivary proteins associated with type 2 diabetes mellitus. Issue 65 (1st November 2020)
- Main Title:
- Integrated glycomics strategy for the evaluation of glycosylation alterations in salivary proteins associated with type 2 diabetes mellitus
- Authors:
- Yu, Hanjie
Wang, Junhong
Tang, Zhen
Li, Xia
Yin, Mengqi
Zhang, Fan
Shu, Jian
Chen, Wentian
Yang, Shuang
Li, Zheng - Abstract:
- Abstract : The strategy to investigate the altered glycosylation associated with T2DM. Abstract : Glycosylation is involved in several biological processes, and its alterations can reflect the process of certain diseases. Type 2 diabetes mellitus (T2DM) has attained the status of a global pandemic; however, the difference in salivary protein glycosylation between healthy subjects and patients with T2DM has not been fully understood. In the present study, salivary specimens from patients with T2DM ( n = 72) and healthy volunteers (HVs, n = 80) were enrolled and divided into discovery and validation cohorts. A method combining the lectin microarray and lectin blotting was employed to investigate and confirm the altered glycopatterns in salivary glycoproteins. Then, lectin-mediated affinity capture of glycoproteins and MALDI-TOF/TOF-MS were performed to obtain the precise structural information of the altered glycans. As a result, the glycopatterns recognized by 5 lectins (LEL, VVA, Jacalin, RCA120 and DSA) showed significant alteration in the saliva of T2DM patients. Notably, the glycopattern of Galβ-1, 4GlcNAc (LacNAc) recognized by LEL exhibited a significant increase in T2DM patients compared to HVs in both discovery and validation cohorts. The MALDI-TOF/TOF-MS results indicated that there were 10 and 7 LacNAc-containing N / O -glycans ( e.g. m / z 1647.586, 11 688.613 and 1562.470) that were identified only in T2DM patients. Besides, the relative abundance of 3Abstract : The strategy to investigate the altered glycosylation associated with T2DM. Abstract : Glycosylation is involved in several biological processes, and its alterations can reflect the process of certain diseases. Type 2 diabetes mellitus (T2DM) has attained the status of a global pandemic; however, the difference in salivary protein glycosylation between healthy subjects and patients with T2DM has not been fully understood. In the present study, salivary specimens from patients with T2DM ( n = 72) and healthy volunteers (HVs, n = 80) were enrolled and divided into discovery and validation cohorts. A method combining the lectin microarray and lectin blotting was employed to investigate and confirm the altered glycopatterns in salivary glycoproteins. Then, lectin-mediated affinity capture of glycoproteins and MALDI-TOF/TOF-MS were performed to obtain the precise structural information of the altered glycans. As a result, the glycopatterns recognized by 5 lectins (LEL, VVA, Jacalin, RCA120 and DSA) showed significant alteration in the saliva of T2DM patients. Notably, the glycopattern of Galβ-1, 4GlcNAc (LacNAc) recognized by LEL exhibited a significant increase in T2DM patients compared to HVs in both discovery and validation cohorts. The MALDI-TOF/TOF-MS results indicated that there were 10 and 7 LacNAc-containing N / O -glycans ( e.g. m / z 1647.586, 11 688.613 and 1562.470) that were identified only in T2DM patients. Besides, the relative abundance of 3 LacNAc-containing N -glycans and 10 LacNAc-containing O -glycans showed an increase in the glycopattern in T2DM patients. These results indicated that the glycopattern of LacNAc is increased in salivary glycoproteins from T2DM patients, and an increase in LacNAc-containing N / O -glycans may contribute to this alteration. Our findings provide useful information to understand the complex physiological changes in the T2DM patients. … (more)
- Is Part Of:
- RSC advances. Volume 10:Issue 65(2020)
- Journal:
- RSC advances
- Issue:
- Volume 10:Issue 65(2020)
- Issue Display:
- Volume 10, Issue 65 (2020)
- Year:
- 2020
- Volume:
- 10
- Issue:
- 65
- Issue Sort Value:
- 2020-0010-0065-0000
- Page Start:
- 39739
- Page End:
- 39752
- Publication Date:
- 2020-11-01
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d0ra05466f ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 14762.xml