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PLoS One. 2016 Jun 30;11(6):e0158001. doi: 10.1371/journal.pone.0158001. eCollection 2016.

Proteomic Analysis of Vitreous Humor in Retinal Vein Occlusion.

Author information

1
Eye Center, Albert-Ludwigs-University Freiburg, Freiburg, Germany.
2
Department of Ophthalmology, University of Heidelberg, Heidelberg, Germany.
3
Mosaiques Diagnostics GmbH, Hannover, Germany.
4
Institut National de la Santé et de la Recherche Médicale (INSERM), U1048, Institut of Cardiovascular and Metabolic Disease, Toulouse, France.
5
Université Toulouse III Paul-Sabatier, Toulouse, France.
6
BHF Glasgow Cardiovascular Research Centre, University of Glasgow, Glasgow, United Kingdom.
7
Department of Ophthalmology, University of Frankfurt, Frankfurt am Main, Germany.
8
Department of Pathology, University of Heidelberg, Heidelberg, Germany.
9
Department of Ophthalmology, University of Southern California, Los Angeles, California, United States of America.

Abstract

PURPOSE:

To analyze the protein profile of human vitreous of untreated patients with retinal vein occlusion (RVO).

METHODS:

Sixty-eight vitreous humor (VH) samples (44 from patients with treatment naïve RVO, 24 controls with idiopathic floaters) were analyzed in this clinical-experimental study using capillary electrophoresis coupled to mass spectrometer and tandem mass spectrometry. To define potential candidate protein markers of RVO, proteomic analysis was performed on RVO patients (n = 30) and compared with controls (n = 16). To determine validity of potential biomarker candidates in RVO, receiver operating characteristic (ROC) was performed by using proteome data of independent RVO (n = 14) and control samples (n = 8).

RESULTS:

Ninety-four different proteins (736 tryptic peptides) could be identified. Sixteen proteins were found to be significant when comparing RVO and control samples (P = 1.43E-05 to 4.48E-02). Five proteins (Clusterin, Complement C3, Ig lambda-like polypeptide 5 (IGLL5), Opticin and Vitronectin), remained significant after using correction for multiple testing. These five proteins were also detected significant when comparing subgroups of RVO (central RVO, hemi-central RVO, branch RVO) to controls. Using independent samples ROC-Area under the curve was determined proving the validity of the results: Clusterin 0.884, Complement C3 0.955, IGLL5 1.000, Opticin 0.741, Vitronectin 0.786. In addition, validation through ELISA measurements was performed.

CONCLUSION:

The results of the study reveal that the proteomic composition of VH differed significantly between the patients with RVO and the controls. The proteins identified may serve as potential biomarkers for pathogenesis induced by RVO.

PMID:
27362861
PMCID:
PMC4928959
DOI:
10.1371/journal.pone.0158001
[Indexed for MEDLINE]
Free PMC Article

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