The human Descemet's membrane and lens capsule : protein composition and biomechanical properties
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Halfter, Willi
Department of Ophthalmology, University of Basel, Switzerland
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Moes, Suzette
Proteomics Core Facility, Biozentrum, University of Basel, Switzerland
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Halfter, Kathrin
Munich Cancer Registry, Institute of Medical Informatics, Biometry and Epidemiology, Maximilian University Munich, Germany
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Schoenenberger, Monica S.
Swiss Nanoscience Institute, Nano Imaging Lab, University Basel, Switzerland
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Monnier, Christophe A.
Department of Ophthalmology, University of Basel, Switzerland
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Kalita, Joanna
Biozentrum and the Swiss Nanoscience Institute, University of Basel, Switzerland
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Asgeirsson, Daphne
Biozentrum and the Swiss Nanoscience Institute, University of Basel, Switzerland
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Binggeli, Tatjana
Department of Ophthalmology, University of Basel, Switzerland
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Jenoe, Paul
Proteomics Core Facility, Biozentrum, University of Basel, Switzerland
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Scholl, Hendrik P.N.
Department of Ophthalmology, University of Basel, Switzerland - Institute of Molecular and Clinical Ophthalmology Basel (IOB), Switzerland - Wilmer Eye Institute, Johns Hopkins University, Baltimore, MA, USA
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Henrich, Paul Bernhard
Department of Ophthalmology, University of Basel, Switzerland - Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
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Published in:
- Experimental eye research. - 2020, vol. 201, no. December, p. 13 p
English
The Descemet's membrane (DM) and the lens capsule (LC) are two ocular basement membranes (BMs) that are essential in maintaining stability and structure of the cornea and lens. In this study, we investigated the proteomes and biomechanical properties of these two materials to uncover common and unique properties. We also screened for possible protein changes during diabetes. LC-MS/MS was used to determine the proteomes of both BMs. Biomechanical measurements were conducted by atomic force microscopy (AFM) in force spectroscopy mode, and complemented with immunofluorescence microscopy. Proteome analysis showed that all six existing collagen IV chains represent 70% of all LC-protein, and are thus the dominant components of the LC. The DM on the other hand is predominantly composed of a single protein, TGF-induced protein, which accounted for around 50% of all DM-protein. Four collagen IV-family members in DM accounted for only 10% of the DM protein. Unlike the retinal vascular BMs, the LC and DM do not undergo significant changes in their protein compositions during diabetes. Nanomechanical measurements showed that the endothelial/epithelial sides of both BMs are stiffer than their respective stromal/anterior-chamber sides, and both endothelial and stromal sides of the DM were stiffer than the epithelial and anterior-chamber sides of the LC. Long-term diabetes did not change the stiffness of the DM and LC. In summary, our analyses show that the protein composition and biomechanical properties of the DM and LC are different, i.e., the LC is softer than DM despite a significantly higher concentration of collagen IV family members. This finding is unexpected, as collagen IV members are presumed to be responsible for BM stiffness. Diabetes had no significant effect on the protein composition and the biomechanical properties of both the DM and LC.
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Language
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Classification
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Pathology, clinical medicine
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License
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CC BY-NC-ND
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Open access status
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hybrid
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Identifiers
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Persistent URL
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https://n2t.net/ark:/12658/srd1319295
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