Aberrant glycosylation in the human trabecular meshwork

Adam E. Sienkiewicz, Brandon N. Rosenberg, Genea Edwards, Teresia A. Carreon, Sanjoy K Bhattacharya

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Purpose: To determine the difference in protein glycosylation and glycosylation enzyme levels between glaucomatous and control trabecular meshwork (TM). Experimental design: Glaucomatous and normal donor (n = 12 each) TM tissues, lectin fluorescence, fluorophore-assisted carbohydrate analyses, and quantitative MS were used to determine the glycosylation levels. Primary TM cells and glycosylation inhibitors were used to determine their effect on cell shape and motility. Results: In contrast to elevated levels of glycoproteins determined by lectin fluorescence, simultaneous hyper- and hypo-glycosylation in glaucomatous TM was revealed by fluorophore-assisted carbohydrate analyses. Analyses of enzymes showed elevation of beta-glycosidase 1 and decrease in galactosyltransferase family 6 domain containing protein 1 in the glaucomatous TM. Quantitative MS identified select protein level changes between glaucomatous and normal TM. Primary TM cells were treated with inhibitors to elicit hypo-glycosylation, which affected cell shape, motility, and fluorescent tracer transport across a layer of TM cells. Conclusions and clinical relevance: Global protein glycosylation is aberrant in glaucomatous TM compared to controls. The results presented here suggest that the alteration in global TM protein glycosylation encompassing cellular and extracellular matrix proteins contributes to glaucoma pathology likely mediated through changes in properties of TM cells.

Original languageEnglish
Pages (from-to)130-142
Number of pages13
JournalProteomics - Clinical Applications
Volume8
Issue number3-4
DOIs
StatePublished - Jan 1 2014

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Glycosylation
Trabecular Meshwork
Fluorophores
Proteins
Lectins
Cell Shape
Fluorescence
Cell Movement
Carbohydrates
Galactosyltransferases
Extracellular Matrix Proteins
Glycoside Hydrolases
Pathology
Enzymes
Design of experiments
Glycoproteins
Glaucoma
Tissue
Research Design

Keywords

  • Carbohydrate electrophoresis
  • Glaucoma
  • Glycosylation
  • Trabecular meshwork

ASJC Scopus subject areas

  • Clinical Biochemistry

Cite this

Aberrant glycosylation in the human trabecular meshwork. / Sienkiewicz, Adam E.; Rosenberg, Brandon N.; Edwards, Genea; Carreon, Teresia A.; Bhattacharya, Sanjoy K.

In: Proteomics - Clinical Applications, Vol. 8, No. 3-4, 01.01.2014, p. 130-142.

Research output: Contribution to journalArticle

Sienkiewicz, AE, Rosenberg, BN, Edwards, G, Carreon, TA & Bhattacharya, SK 2014, 'Aberrant glycosylation in the human trabecular meshwork', Proteomics - Clinical Applications, vol. 8, no. 3-4, pp. 130-142. https://doi.org/10.1002/prca.201300031
Sienkiewicz, Adam E. ; Rosenberg, Brandon N. ; Edwards, Genea ; Carreon, Teresia A. ; Bhattacharya, Sanjoy K. / Aberrant glycosylation in the human trabecular meshwork. In: Proteomics - Clinical Applications. 2014 ; Vol. 8, No. 3-4. pp. 130-142.
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