Vitronectin and proliferative intraocular disorders. I. A colocalisation study of the serum spreading factor, vitronectin, and fibronectin in traction membranes from patients with proliferative vitreoretinopathy

Weller, Michael; Wiedemann, Peter; Bresgen, M; Heimann, Klaus

doi:10.1007/bf01046428

Cited by 6 publications

(5 citation statements)

References 20 publications

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“…In the current study, CK remodeling in PVR process revealed that normal CK proteins were down-regulated or disappeared while secreted proteins significantly increased in PVR vitreous. Previous reports documented that the extracellular matrix components, fibronectin, laminin, and vitronectin (VN) were the major components of the epiretinal and subretinal membranes of PVR, which were detected in vitreous [27,28]. However, in our study, only VN could be detected in both moderate and severe PVR vitreous.…”

Section: Discussioncontrasting

confidence: 72%

Vitreous proteomic analysis of proliferative vitreoretinopathy

Liu

Cui

et al. 2008

Proteomics

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Proliferative vitreoretinopathy (PVR) is the most common cause of anatomic failure in retinal detachment surgery. To understand the molecular mechanisms, vitreous proteomes of patients with PVR were investigated by two-dimensional-nano-liquid chromatography coupled with tandem mass spectrometry. Vitreous samples of moderate PVR (grade B), and severe PVR (grade C or D) were aspirated during pars plana vitrectomy before infusion. In the current study, 129, 97 and 137 proteins were identified in vitreous of normal control, moderate and severe PVR, respectively. In PVR vitreous samples, complement components, serine proteinase inhibitors, and extracellular proteins were up-regulated or appeared, while normal cytoskeleton and metabolism proteins were down-regulated or disappeared. It was noteworthy that the proteins involved in transcription and translation regulation increased in vitreous with PVR. Among 102 PVR-specific proteins, kininogen 1 was specifically detected in both vitreous and the corresponding serum. Therefore, it can be concluded that PVR is a complicated pathology process with great amount of proteins involved in metabolism dysfunction, immune reactions, and cytoskeleton remolding. Kininogen 1 may be a candidate biomarker of PVR. Further investigations of these special proteins will provide additional targets for treatment or prevention of ocular proliferative diseases.

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Section: Discussioncontrasting

confidence: 72%

Vitreous proteomic analysis of proliferative vitreoretinopathy

Liu

Cui

et al. 2008

Proteomics

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“…A limited number of reports exist regarding details of cellular metabolism in macular pucker, RD and PVR. Also the glycoprotein vitronectin has been identified in epiretinal membranes 40 . This glycoprotein stabilizes PAI‐1 41 and mediates its binding to extracellular matrix 42 .…”

Section: Discussionmentioning

confidence: 99%

Components of the fibrinolytic system in the vitreous body in patients with vitreoretinal disorders

Ulrich

Spannagl

Gandorfer

2008

Clinical Exper Ophthalmology

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Purpose: To assess components of the fibrinolytic system in the vitreous humour and serum of patients with vitreoretinal disorders. Methods: Forty‐three samples of vitreous humour and plasma of 43 patients undergoing pars plana vitrectomy for macular hole, macular pucker, retinal detachment or proliferative vitreoretinopathy were evaluated for their content of plasminogen, a2‐antiplasmin, plasminogen‐activator‐inhibitor 1, plasmin‐a2‐antiplasmin‐complex, tissue plasminogen activator, total protein, albumin, d‐dimer. Patient groups were compared with each other using the U‐test (Mann and Whitney) for non‐parametric testing of two independent samples. Results: The groups of retinal detachment and proliferative vitreoretinopathy had elevated vitreal levels of plasminogen‐activator‐inhibitor 1 (352.5 and 370.7 ng/mL vs. 1.86 and 56.6 ng/mL, P = non‐significant), plasmin‐a2‐antiplasmin‐complex (2416.5 and 1836.2 µg/L vs. 124.2 and 133.4 µg/L, P < 0.001), albumin (0.08 and 0.15 g/dL vs. 0.03 and 0.07 g/dL, P < 0.05) and d‐dimer (4.76 and 1.64 µg/mL vs. 0.40 and 0.48 µg/mL, P = non‐significant) when compared with patients with macular hole and macular pucker. Conclusions: There are significant differences in the vitreal concentration of components of the fibrinolytic system in patients with vitreoretinal disorders. Breakdown of the blood–retinal barrier and complex disease‐specific mechanisms are thought to be responsible for an increase of components of the fibrinolytic system in the vitreous.

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“…Retinal membranes are composed of retinal pigment epithelial cells, glial cells, astrocytes and fibroblasts (Gilbert et al, 1988 ;Jerdan et al, 1989), in addition to infiltrating macrophages and lymphocytes (Limb et al, 1993 ;Weller, Heimann and Wiedemann, 1988). All these cells are bound into a framework of extracellular matrix proteins composed of collagen, fibronectin, vitronectin and laminin (Rodriguez, Newsome and Machemer, 1981 ;Weller et al, 1991 ;Scheiffarth et al, 1988), which confers contractibility to retinal membranes.…”

Section: Introductionmentioning

confidence: 99%