Abstract
Prostate-specific antigen (PSA) is an extensively studied glycoprotein with critical biological functions in reproduction and is an important biomarker for detection of prostate cancer. The central role of PSA in both areas has made it one of the most studied human glycoproteins. Structurally, it has a single site of N-glycosylation, making it an attractive target for characterization of the glycans attached to it in relation to disease and function. The methods used and results from the most extensive glycan structural studies are summarized. Cumulatively, these studies have identified a large number of structurally diverse glycans attached to the single glycosylation site of PSA, which has hindered assignment of specific glycan structures to be associated with only prostate cancer or other condition. The primary analytical tools used for these types of studies are high-resolution mass spectrometers. As this technology continues to evolve, and as more samples of PSA from individual patients are analyzed, it is expected that the functions of the numerous N-linked glycan structures present on the single glycosylation site of PSA will emerge.
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Drake, R.R. (2015). Enigma of Multiple N-Linked Glycoforms of Prostate Specific Antigen. In: Taniguchi, N., Endo, T., Hart, G., Seeberger, P., Wong, CH. (eds) Glycoscience: Biology and Medicine. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54841-6_187
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DOI: https://doi.org/10.1007/978-4-431-54841-6_187
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