» Articles » PMID: 34368082

Recent Advances in Mass Spectrometry-Based Glycomic and Glycoproteomic Studies of Pancreatic Diseases

Overview
Journal Front Chem
Specialty Chemistry
Date 2021 Aug 9
PMID 34368082
Citations 10
Authors
Affiliations
Soon will be listed here.
Abstract

Modification of proteins by glycans plays a crucial role in mediating biological functions in both healthy and diseased states. Mass spectrometry (MS) has emerged as the most powerful tool for glycomic and glycoproteomic analyses advancing knowledge of many diseases. Such diseases include those of the pancreas which affect millions of people each year. In this review, recent advances in pancreatic disease research facilitated by MS-based glycomic and glycoproteomic studies will be examined with a focus on diabetes and pancreatic cancer. The last decade, and especially the last five years, has witnessed developments in both discovering new glycan or glycoprotein biomarkers and analyzing the links between glycans and disease pathology through MS-based studies. The strength of MS lies in the specificity and sensitivity of liquid chromatography-electrospray ionization MS for measuring a wide range of biomolecules from limited sample amounts from many sample types, greatly enhancing and accelerating the biomarker discovery process. Furthermore, imaging MS of glycans enabled by matrix-assisted laser desorption/ionization has proven useful in complementing histology and immunohistochemistry to monitor pancreatic disease progression. Advances in biological understanding and analytical techniques, as well as challenges and future directions for the field, will be discussed.

Citing Articles

Clinical glycoproteomics: methods and diseases.

Wang Y, Lei K, Zhao L, Zhang Y MedComm (2020). 2024; 5(10):e760.

PMID: 39372389 PMC: 11450256. DOI: 10.1002/mco2.760.


Joint modeling of an outcome variable and integrated omics datasets using GLM-PO2PLS.

Gu Z, Uh H, Houwing-Duistermaat J, El Bouhaddani S J Appl Stat. 2024; 51(13):2627-2651.

PMID: 39290359 PMC: 11404385. DOI: 10.1080/02664763.2024.2313458.


Molecular-level architecture of Chlamydomonas reinhardtii's glycoprotein-rich cell wall.

Poulhazan A, Arnold A, Mentink-Vigier F, Muszynski A, Azadi P, Halim A Nat Commun. 2024; 15(1):986.

PMID: 38307857 PMC: 10837150. DOI: 10.1038/s41467-024-45246-7.


Advances in Mass Spectrometry-Metabolomics Based Approaches.

Lima N, Santos G, Lima G, Vaz B Adv Exp Med Biol. 2023; 1439:101-122.

PMID: 37843807 DOI: 10.1007/978-3-031-41741-2_5.


Proteogenomic data and resources for pan-cancer analysis.

Li Y, Dou Y, Veiga Leprevost F, Geffen Y, Calinawan A, Aguet F Cancer Cell. 2023; 41(8):1397-1406.

PMID: 37582339 PMC: 10506762. DOI: 10.1016/j.ccell.2023.06.009.


References
1.
Zhou Q, Fulop A, Hopf C . Recent developments of novel matrices and on-tissue chemical derivatization reagents for MALDI-MSI. Anal Bioanal Chem. 2020; 413(10):2599-2617. PMC: 8007514. DOI: 10.1007/s00216-020-03023-7. View

2.
Kleeff J, Korc M, Apte M, La Vecchia C, Johnson C, Biankin A . Pancreatic cancer. Nat Rev Dis Primers. 2016; 2:16022. DOI: 10.1038/nrdp.2016.22. View

3.
Maynard J, Chalkley R . Methods for Enrichment and Assignment of N-Acetylglucosamine Modification Sites. Mol Cell Proteomics. 2020; 20:100031. PMC: 8724609. DOI: 10.1074/mcp.R120.002206. View

4.
Sarrats A, Saldova R, Pla E, Fort E, Harvey D, Struwe W . Glycosylation of liver acute-phase proteins in pancreatic cancer and chronic pancreatitis. Proteomics Clin Appl. 2010; 4(4):432-48. DOI: 10.1002/prca.200900150. View

5.
Raghav A, Ahmad J, Alam K . Nonenzymatic glycosylation of human serum albumin and its effect on antibodies profile in patients with diabetes mellitus. PLoS One. 2017; 12(5):e0176970. PMC: 5435419. DOI: 10.1371/journal.pone.0176970. View