Ultrastructure of connective tissue of eye drainage system in ophthalmic hypertension associated with primary juvenile glaucoma

Kuleshova, O. N.; Nepomnyashchikh, G. I.; Айдагулова, С. В.

doi:10.1007/s10517-008-0095-5

Cited by 1 publication

(1 citation statement)

References 5 publications

(6 reference statements)

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“…How PTMs, and in particular, global TM glycosylation affect the aqueous outflow dynamics is not fully understood. Alterations in global TM glycosylation levels were found in POAG as well as juvenile glaucoma . Unlike angle closure glaucoma, the iridocorneal angle remains open in the POAG but yet the aqueous outflow is decreased which is thought to be due to increased resistance at the TM.…”

Section: Discussionmentioning

confidence: 99%

Aberrant glycosylation in the human trabecular meshwork

Sienkiewicz

Rosenberg

Edwards

et al. 2014

Proteomics Clinical Apps

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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 mass spectrometry 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 trabecular meshwork 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 trabecular meshwork. Quantitative mass spectrometry identified select protein level changes between glaucomatous and normal trabecular meshwork. Primary trabecular meshwork cells were treated with inhibitors to elicit hypo-glycosylation, which affected cell shape, motility, and fluorescent tracer transport across a layer of trabecular meshwork cells. Conclusions and clinical relevance Global protein glycosylation is aberrant in glaucomatous trabecular meshwork 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.

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Section: Discussionmentioning

confidence: 99%