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Glycomic characterization of basal tears and changes with diabetes and diabetic retinopathy.
Nguyen-Khuong, Terry; Everest-Dass, Arun V; Kautto, Liisa; Zhao, Zhenjun; Willcox, Mark D P; Packer, Nicolle H.
Afiliação
  • Nguyen-Khuong T; Biomolecular Frontiers Research Centre, Department of Chemistry and Biomolecular Sciences, Faculty of Science, Macquarie University, Building E8C Room 307, Sydney, NSW 2109, Australia.
  • Everest-Dass AV; Biomolecular Frontiers Research Centre, Department of Chemistry and Biomolecular Sciences, Faculty of Science, Macquarie University, Building E8C Room 307, Sydney, NSW 2109, Australia.
  • Kautto L; Biomolecular Frontiers Research Centre, Department of Chemistry and Biomolecular Sciences, Faculty of Science, Macquarie University, Building E8C Room 307, Sydney, NSW 2109, Australia.
  • Zhao Z; School of Optometry and Vision Science, University of New South Wales, Sydney, NSW, Australia.
  • Willcox MD; School of Optometry and Vision Science, University of New South Wales, Sydney, NSW, Australia.
  • Packer NH; Biomolecular Frontiers Research Centre, Department of Chemistry and Biomolecular Sciences, Faculty of Science, Macquarie University, Building E8C Room 307, Sydney, NSW 2109, Australia nicki.packer@mq.edu.au.
Glycobiology ; 25(3): 269-83, 2015 Mar.
Article em En | MEDLINE | ID: mdl-25303961
ABSTRACT
As a secreted fluid, the state of tear glycosylation is particularly important in the role of immunity of the ocular surface. Tears are a valuable source of non-invasive biomarkers for disease and there are continued efforts to characterize their components thoroughly. In this study, a small volume of basal tears (5 µL) was collected from healthy controls, patients with diabetes without retinopathy and patients with diabetes and retinopathy. The detailed N- and O-linked tear protein glycome was characterized and the relative abundance of each structure determined. Of the 50 N-linked glycans found, 89% were complex with 50% containing a bisecting N-acetylglucosamine, 65% containing a core fucose whilst 33% were sialylated. Of the 8 O-linked glycans detected, 3 were of cores 1 and 5 of core 2 type, with a majority of them being sialylated (90%). Additionally, these glycan structures were profiled across the three diabetic disease groups. Whilst the higher abundant structures did not alter across the three groups, only five low abundance N-linked glycans and 1 O-linked glycan did alter with the onset of diabetes mellitus and diabetic retinopathy (DR). These results suggest the conservation of glycan types on basal tear proteins between individuals and point to only small changes in glycan expression on the proteins in tears with the development of diabetes and DR.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polissacarídeos / Lágrimas / Retinopatia Diabética Tipo de estudo: Observational_studies Limite: Humans Idioma: En Revista: Glycobiology Assunto da revista: BIOQUIMICA Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Austrália

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polissacarídeos / Lágrimas / Retinopatia Diabética Tipo de estudo: Observational_studies Limite: Humans Idioma: En Revista: Glycobiology Assunto da revista: BIOQUIMICA Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Austrália