Priglinger S., Neubauer A. S., Schönfeld C. L., Kampik A., Welge-Lüßen U.

Department of Ophthalmology, Ludwig-Maximilian-University, München

Introduction: The content of extracellular matrix proteins (ECM) in proliferative vitreoretinopathy membranes is reasonable high. Such an accumulation of ECM may either result from increased protein synthesis or from a slower rate of protein degradation. Transglutaminases are enzymes capable to cross-link ECM proteins to form stable ECM, resistant to proteolytic and mechanical damage and may thus contribute to reduce protein degradation.
Material and Methods: 34 subretinal and epiretinal membranes were studied for expression of transglutaminase isoforms by RT-PCR. In situ transglutaminase activity was assessed by Cadaverin incorporation. In addition PVR membranes were stained with antibodies to various transglutaminase isoforms by immunohistochemistry.
Results: Expression of tissue transglutaminase and keratinocyte-specific transglutaminase was observed in all PVR membranes. A few membranes also expressed the erythroleukemic isoform. In situ activity could be demonstrated for all membranes. Immunohistochemistry revealed extracellular and intracellular expression of transglutaminase.
Conclusion: Expression of transglutaminases suggests that qualitative as well as quantitative changes in ECM may take place during developement of PVR membranes. These findings may help to elucidate the pathomechanisms leading to the development of PVR membranes. Blocking the irreversible cross-linking of ECM proteins may offer a therapeutic target to prevent the formation of PVR membranes. Supported by DFG (WE 2577/2-1)

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