{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T03:56:29Z","timestamp":1791518189457,"version":"4.3.4"},"reference-count":33,"publisher":"Public Library of Science (PLoS)","issue":"2","license":[{"start":{"date-parts":[[2021,2,26]],"date-time":"2021-02-26T00:00:00Z","timestamp":1614297600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Faculty of Medicine and Health Sciences"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"abstract":"<jats:p>Prolactin is a peptide hormone produced in the anterior pituitary, which increase in several physiological and pathological situations. It is unclear if hyperprolactinaemia may affect glycosylation of immunoglobulin G (IgG). Twenty-five patients with hyperprolactinemia and 22 healthy control subjects were included in the study. The groups had similar age and gender distribution. A panel of hormonal and haematological analyses, creatinine, glucose, liver enzymes and immunoglobulins were measured by routine clinical methods. IgG was purified from serum by Protein G Sepharose. Sialic acid was released from IgG by use of neuraminidase followed by quantification on high performance anion-exchange chromatography with pulsed amperometric detection. Tryptic glycopeptides of IgG was analysed by matrix-assisted laser desorption\/ionization-time of flight mass spectrometry. Hormone and immunoglobulin levels were similar in the two groups, except for IgA and prolactin. Significantly higher IgG1 and IgG2\/3 galactosylation was found in the patient group with hyperprolactinaemia compared to controls. (A significant correlation between prolactin and IgG2\/3 galactosylation (Rs 0.61, p&lt;0.001) was found for samples with prolactin values below 2000 mIU\/L. The relative amount of sialylated and bisecting glycans on IgG did not differ between patients and controls. The four macroprolactinaemic patients showed decreased relative amount of bisecting IgG2\/3 glycans. Hyperprolactinaemia was found to be associated with increased galactosylation of IgG1and IgG2\/3. This may have impact on IgG interactions with Fc-receptors, complement and lectins, and consequently lead to an altered immune response.<\/jats:p>","DOI":"10.1371\/journal.pone.0247805","type":"journal-article","created":{"date-parts":[[2021,2,26]],"date-time":"2021-02-26T18:31:23Z","timestamp":1614364283000},"page":"e0247805","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":2,"title":["Altered immunoglobulin G glycosylation in patients with isolated hyperprolactinaemia"],"prefix":"10.1371","volume":"16","author":[{"given":"Daniel","family":"Hirschberg","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bertil","family":"Ekman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeanette","family":"Wahlberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0541-7345","authenticated-orcid":true,"given":"Eva","family":"Landberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2021,2,26]]},"reference":[{"issue":"4","key":"pone.0247805.ref001","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1074\/mcp.R112.026005","article-title":"Glycoproteomic analysis of antibodies","volume":"12","author":"G Zauner","year":"2013","journal-title":"Mol Cell Proteomics"},{"issue":"8","key":"pone.0247805.ref002","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1111\/exd.12171","article-title":"The carbohydrate switch between pathogenic and immunosuppressive antigen-specific antibodies","volume":"22","author":"M Collin","year":"2013","journal-title":"Exp Dermatol"},{"issue":"8","key":"pone.0247805.ref003","doi-asserted-by":"crossref","first-page":"934","DOI":"10.1177\/0961203316640368","article-title":"Sweet but dangerous\u2014the role of immunoglobulin G glycosylation in autoimmunity and inflammation","volume":"25","author":"MH Biermann","year":"2016","journal-title":"Lupus"},{"issue":"3","key":"pone.0247805.ref004","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1016\/j.bbagen.2007.06.012","article-title":"The N-linked sugar chains of human immunoglobulin G: their unique pattern, and their functional roles","volume":"1780","author":"A. 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