Proteomic analysis of vitreous humor in retinal vein occlusion

• Verfasst von: Reich, Michael [VerfasserIn]
• Verfasst von: Steliyanova Dacheva, Ivanka [VerfasserIn]
• Verfasst von: Nobl, Matthias Johannes [VerfasserIn]
• Verfasst von: Kopitz, Jürgen [VerfasserIn]
• Verfasst von: Kretz, Florian Tobias Alwin [VerfasserIn]
• Verfasst von: Auffarth, Gerd U. [VerfasserIn]
• Verfasst von: Koss, Michael Janusz [VerfasserIn]
• Titel: Proteomic analysis of vitreous humor in retinal vein occlusion
• Verf.angabe: Michael Reich, Ivanka Dacheva, Matthias Nobl, Justyna Siwy, Joost P. Schanstra, William Mullen, Frank H.J. Koch, Jürgen Kopitz, Florian T.A. Kretz, Gerd U. Auffarth, Michael J. Koss
• E-Jahr: 2016
• Jahr: June 30, 2016
• Teil: volume:11
• Teil: year:2016
• Teil: number:6
• Fussnoten: Gesehen am 25.10.2021
• Titel Quelle: Enthalten in: PLOS ONE
• Ort Quelle: San Francisco, California, US : PLOS, 2006
• Jahr Quelle: 2016
• Band/Heft Quelle: 11(2016,6) Artikel-Nummer e0158001, 19 Seiten
• ISSN Quelle: 1932-6203
• DOI: doi:10.1371/journal.pone.0158001
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Biomarkers
• Sach-SW: Collagens
• Sach-SW: Complement system
• Sach-SW: Extracellular matrix proteins
• Sach-SW: Proteomes
• Sach-SW: Retinal vessels
• Sach-SW: Serum proteins
• Sach-SW: Signal peptides
• K10plus-PPN: 1745536132

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.