Dataset Information

Human tear (Diabetic macular edema), LC-MSMS

ABSTRACT: Tear proteome changes in diabetic macular edema with treatment. The constitution of tear protein change was assessed for difference in treatment response

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Tear

SUBMITTER: I-Hsin Ma

LAB HEAD: I-Hsin Ma

PROVIDER: PXD061821 | Pride | 2025-10-13

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	20221105_3314_NTUSWPan_TMT10x_F1-01.raw	Raw
	20221105_3318_NTUSWPan_TMT10x_F2-01.raw	Raw
	20221105_3322_NTUSWPan_TMT10x_F3-01.raw	Raw
	20230209_0132_NTUSWPan_TMT10plex_F1-01.raw	Raw
	20230209_0136_NTUSWPan_TMT10plex_F2-01.raw	Raw

Items per page:

1 - 5 of 12

Publications

Comparative Tear Fluid Proteomics to Explore Treatment Responsiveness in Diabetic Macular Edema: A Pilot Study.

Ma I-Hsin IH Hsu Yuan-Ling YL Wu Hsin-Yi HY Hsieh Yi-Ting YT Pan Szu-Hua SH

Journal of proteome research 20250829 10

Diabetic macular edema (DME) is a leading cause of vision loss in patients with diabetes, with variable responses to intravitreal antivascular endothelial growth factor (VEGF) therapy. This study aimed to identify tear fluid proteins linked to treatment responsiveness. Tear fluid samples were collected from 13 patients with diabetes (21 eyes with DME), among which 9 samples were analyzed using tandem mass tag-labeled liquid chromatography-mass spectrometry, and all 21 samples were validated with ...[more]

PMID: 40882144

Similar Datasets

Project description:Glycosylation of proteins is one of the most common post-translational modification (PTM) and plays important regulatory functions in diverse biological processes such as protein stability or cell signaling. Accordingly, glycoproteins are also a consistent part of the human tear film proteome maintaining the proper function of the ocular surface and forming the first defense barrier of the ocular immune system. Irregularities in the glycoproteomic composition of the tear film might promote development of chronic eye diseases indicating glycoproteins as valuable source for biomarker discovery or drug target identification. The present study aimed to develop a lectin-based affinity method for the enrichment and concentration of tear glycoproteins/glycopeptides and the characterization of their specific N-glycosylation sites by high-resolution mass spectrometry (MS). For method development and evaluation, we accumulated first native glycoproteins from human tear sample pools and assessed the enrichment efficiency of different lectin column systems by 1D gel electrophoresis and specific protein stainings (Coomassie and glycoproteins). The best-performing multi-lectin column system (comprising the four lectins ConA, JAC, WGA and UEA I, termed as 4L) was applied for glycopeptide enrichment from human tear sample digests followed by MS-based detection and localization of their specific N-glycosylation sites. As main result, the present study identified in total 26 N glycosylation sites of 11 N-glycoproteins in tear sample pools of healthy individuals (n=3 biological sample pools). Amongst others, we identified tear film proteins lactotransferrin (N497 and N642, LTF), Ig heavy chain constant α-1 (N144 and 340, IGHA1), prolactin-inducible protein (N105, PIP) as well as extracellular lacritin (N105, LACRT) as highly reliable and significant N glycoproteins, which were already associated with the pathogenesis of various chronic eye diseases such as the dry eye syndrome (DES). In conclusion, the results of the present study will serve as important tear film N-glycoprotein catalogue for future studies focusing the human tear film and ocular surface-related inflammatory diseases.