Glycoprotein Research Group (gPRG) 2013 Interlaboratory Study: Quantitative N-glycan Profiling of Prostate Specific Antigen
Year: 2013
Type: article
Abstract: The fact that most proteins are glycosylated underlies the key roles played by glycosylation during evolution. The functions of glycoproteins are tremendously broad and include cell attachment recognition, homeostasis, transport of molecules, and enzymatic and immunology recognition domains. One of the principal axes of glycoprotein research is to understand better the correlation between glycan structure and function. Mass spectrometry has emerged as a powerful analytical technique in the field of glycoprotein characterization. Its sensitivity, high dynamic range, and mass accuracy provide both quantitative and sequence/structural information. The goal of the gPRG 2013 study was to determine the ability of the international glycoproteomics community to compare N-glycosylation between two different sources of prostate specific antigen (PSA) by mass spectrometry. PSA was selected to conduct this study for several reasons: PSA is a relatively small glycoprotein (MW ∼30,000Da) characterized by a single site of N-glycosylation and is of significant biological interest as a biomarker for prostate cancer. Which sample preparation, separation and analysis methods produced the most consistent results? What is the consensus for the glycosylation patterns of the two sources of PSA? For which glycoforms from the two PSA sources are abundances significantly different?
Source: Europe PMC (PubMed Central)
Institution: Macquarie University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W258672388