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Comparative evaluation of the aqueous humor proteome of primary angle closure and primary open angle glaucomas and senile cataract eyes

ABSTRACT: Comparative evaluation of the aqueous humor proteome of primary angle closure and primary open angle glaucomas and senile cataract eyes

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Anterior Chamber Of The Eye

SUBMITTER: Inderjeet Kaur

LAB HEAD: Ramanjit Sihota

PROVIDER: PXD004928 | Pride | 2020-05-29

REPOSITORIES: Pride

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			Action	DRS
	Cat_1_U_R.raw	Raw
	Cat_1_U_R_long.raw	Raw
	Cat_1_U_R_long2.raw	Raw
	Cat_2_long1.raw	Raw
	Cat_2_long2.raw	Raw

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Publications

Comparative evaluation of the aqueous humor proteome of primary angle closure and primary open angle glaucomas and age-related cataract eyes.

Kaur Inderjeet I Kaur Jasbir J Sooraj K K Goswami Sandeep S Saxena Rohit R Chauhan Virander Singh VS Sihota Ramanjit R

International ophthalmology 20180113 1

<h4>Purpose</h4>To analyze and compare the total proteome of aqueous humor (AH) from patients having primary angle closure glaucoma (PACG), primary open angle glaucoma (POAG) and age-related cataract.<h4>Materials and methodology</h4>Aqueous humor was collected from age-matched PACG, POAG and cataract patients who underwent surgery, and it was immediately stored at - 80 °C until analysis. From each sample, 25 µg of total protein was subjected to trypsin digestion and subsequently LC-MS/MS analys ...[more]

PMID: 29332228

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miRNA microarray of human aqueous humor and lens capsule with glaucoma

Project description:A miRNA PCR array comprising 84 miRNAs was used to analyze the AH (glaucoma, n=3; control, n=3) and LC samples (glaucoma, n=3; control, n=4). Expression levels of 19 and 3 miRNAs were significantly upregulated in the AH and LC samples of the glaucoma group, respectively (p < 0.05).

2024-02-16 | E-MTAB-13771 | biostudies-arrayexpress

Dysregulated proteins in aqueous humor from primary open angle glaucoma patients with clinical correlation

Project description:Primary open angle glaucoma (POAG) presents as an irreversible optic neuropathy with corresponding visual field deficits and no other notable symptoms. The pathophysiology of POAG remains poorly understood. Through proteomic analysis of aqueous humour (AH) from POAG patients, we aim to identify changes in protein composition of these samples compared to control samples. This enables us to better understand pathological changes in POAG from a molecular perspective, and may reveal potential diagnostic molecular biomarkers in POAG. We are also interested in correlating differences in AH protein compositions with demographics and clinical severity in POAG patients.

2024-05-23 | PXD033153 | Pride

Differentially expressed microRNAs in the aqueous humor of patients with exfoliation glaucoma or primary open-angle glaucoma

Project description:To better understand the molecular changes in the aqueous humor (AH) content with glaucoma, we analyzed the microRNA (miRNA) profiles of AH samples from patients with Primary Open Angle Glaucoma (POAG) and Exfoliation Glaucoma (XFG) compared to non-glaucoma controls.

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Expression profiling of extracellular long noncoding RNAs in aqueous humor of primary open-angle glaucoma patients

Project description:Long noncoding RNAs (lncRNAs) are emerging as important regulators in cellular processes and have been showed to be involved in the occurrence and development of various neurodegenerative diseases including glaucoma. The aim of this study is to reveal disease-related extracellular lncRNAs and message RNAs (mRNAs) in aqueous humor (AH) of individual primary open-angle glaucoma (POAG) patients, to determine the potential biomarkers for POAG diagnosis

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Compositional analysis of extracellular aggregates in the eyes of patients with exfoliation syndrome and exfoliation glaucoma.

Project description:Exfoliation syndrome (XFS) is a condition characterized by the production of insoluble fibrillar aggregates (exfoliation material; XFM) in the eye and elsewhere. Many patients with XFS progress to exfoliation glaucoma (XFG), a significant cause of global blindness. We used quantitative mass spectrometry to analyze the composition of XFM in lens capsule specimens and aqueous humor samples from XFS and XFG patients and individuals without XFS. Pieces of lens capsule and samples of aqueous humor were obtained with consent from patients undergoing cataract surgery. Tryptic digests of capsule or aqueous samples were analyzed by HPLC-mass spectrometry and relative differences between samples were quantified using the tandem mass tag technique. The distribution of XFM on the capsular surface was visualized by scanning electron microscopy and super-resolution light microscopy. A small set of proteins was consistently upregulated in XFS samples, including microfibril components fibrillin-1 (FBN1), latent TGFBeta-binding protein-2 (LTBP-2), and LTBP-3. Lysyl oxidase-like 1 (LOXL1), a protein linked strongly to XFS in genetic studies, was an abundant XFM protein. Ligands of the TGFBeta superfamily were prominent, including LEFTY2, a protein known for its role in establishing the embryonic body axis. Elevated levels of LEFTY2 were also detected in aqueous humor from XFG patients and confirmed by ELISA. This analysis verified the presence of several suspected XFM proteins and identified novel components. Quantitative comparisons between patient samples revealed a consistent XFM proteome. The expression of FBN1, LOXL1, and LEFTY2 was particularly strong in XFG patients in comparison to XFS patients.

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microRNA profiling in the aqueous humor of highly myopic eyes by next generation sequencing

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Proteomic Alterations in Aqueous Humor From Patients With Primary Open Angle Glaucoma.

Project description:Purpose:Primary open angle glaucoma (POAG) is the most prevalent form of glaucoma, accounting for approximately 90% of all cases. The aqueous humor (AH), a biological fluid in the anterior and posterior chambers of the eye, is involved in a multitude of functions including the maintenance of IOP and ocular homeostasis. This fluid is very close to the pathologic site and is also known to have a significant role in glaucoma pathogenesis. The purpose of this study was to identify proteomic alterations in AH from patients with POAG. Methods:AH samples were extracted from 47 patients undergoing cataract surgery (controls: n = 32; POAG: n = 15). Proteomic analysis of the digested samples was accomplished by liquid-chromatography-mass spectrometry. The identified proteins were evaluated using a variety of statistical and bioinformatics methods. Results:A total of 33 proteins were significantly altered in POAG subjects compared with the controls. The most abundant proteins in POAG subjects are IGKC (13.56-fold), ITIH4 (4.1-fold), APOC3 (3.36-fold), IDH3A (3.11-fold), LOC105369216 (2.98-fold). SERPINF2 (2.94-fold), NPC2 (2.88-fold), SUCLG2 (2.70-fold), KIAA0100 (2.29-fold), CNOT4 (2.23-fold), AQP4 (2.11-fold), COL18A1 (2.08-fold), NWD1 (2.07-fold), and TMEM120B (2.06-fold). A significant increasing trend in the odds ratios of having POAG was observed with increased levels of these proteins. Conclusion:Proteins identified in this study are implicated in signaling, glycosylation, immune response, molecular transport, and lipid metabolism. The identified candidate proteins may be potential biomarkers associated with POAG development and may lead to more insight in understanding the mechanisms underlying the pathogenesis of this disease.

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