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dc.contributor.authorBousfield, George R.
dc.contributor.authorHarvey, David J.
dc.date.accessioned2019-07-18T10:56:41Z
dc.date.available2019-07-18T10:56:41Z
dc.date.issued2019-06-01
dc.identifier.citationGeorge R Bousfield, David J Harvey, Follicle-Stimulating Hormone Glycobiology, Endocrinology, Volume 160, Issue 6, June 2019, Pages 1515–1535en_US
dc.identifier.issn1945-7170
dc.identifier.urihttps://doi.org/10.1210/en.2019-00001
dc.identifier.urihttp://hdl.handle.net/10057/16434
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractFSH glycosylation varies in two functionally important aspects: microheterogeneity, resulting from oligosaccharide structure variation, and macroheterogeneity, arising from partial FSHβ subunit glycosylation. Although advances in mass spectrometry permit extensive characterization of FSH glycan populations, microheterogeneity remains difficult to illustrate, and comparisons between different studies are challenging because no standard format exists for rendering oligosaccharide structures. FSH microheterogeneity is illustrated using a consistent glycan diagram format to illustrate the large array of structures associated with one hormone. This is extended to commercially available recombinant FSH preparations, which exhibit greatly reduced microheterogeneity at three of four glycosylation sites. Macroheterogeneity is demonstrated by electrophoretic mobility shifts due to the absence of FSHβ glycans that can be assessed by Western blotting of immunopurified FSH. Initially, macroheterogeneity was hoped to matter more than microheterogeneity. However, it now appears that both forms of carbohydrate heterogeneity have to be taken into consideration. FSH glycosylation can reduce its apparent affinity for its cognate receptor by delaying initial interaction with the receptor and limiting access to all of the available binding sites. This is followed by impaired cellular signaling responses that may be related to reduced receptor occupancy or biased signaling. To resolve these alternatives, well-characterized FSH glycoform preparations are necessary.en_US
dc.language.isoen_USen_US
dc.publisherNLM (Medline)en_US
dc.relation.ispartofseriesEndocrinology;v.160:no.6
dc.titleFollicle-stimulating hormone glycobiologyen_US
dc.typeArticleen_US
dc.rights.holder© 2019 Endocrine Societyen_US


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