High glucose treatment promotes extracellular matrix proteome remodeling in Müller glial cells
Autor: | Agnese Petrera, Stefanie M. Hauck, Juliane Merl-Pham, Cornelia A. Deeg, Sandra Sagmeister |
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Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
Veterinary Medicine
Integrin Neuroprotection General Biochemistry Genetics and Molecular Biology Extracellular matrix 03 medical and health sciences Glycolysis Inhibition 0302 clinical medicine Diabetic retinopathy medicine Osteopontin Neurodegeneration Molecular Biology 030304 developmental biology Pig 0303 health sciences Retina biology Chemistry General Neuroscience Translational large animal model Cell Biology General Medicine medicine.disease Cell biology Organotypic explant cultures medicine.anatomical_structure Proteome biology.protein Medicine General Agricultural and Biological Sciences Secreted phosphoprotein 1 (SPP1) 030217 neurology & neurosurgery Neuroscience |
Zdroj: | PeerJ, Vol 9, p e11316 (2021) PeerJ |
ISSN: | 2167-8359 |
Popis: | Background The underlying pathomechanisms in diabetic retinopathy (DR) remain incompletely understood. The aim of this study was to add to the current knowledge about the particular role of retinal Müller glial cells (RMG) in the initial processes of DR. Methods Applying a quantitative proteomic workflow, we investigated changes of primary porcine RMG under short term high glucose treatment as well as glycolysis inhibition treatment. Results We revealed significant changes in RMG proteome primarily in proteins building the extracellular matrix (ECM) indicating fundamental remodeling processes of ECM as novel rapid response to high glucose treatment. Among others, Osteopontin (SPP1) as well as its interacting integrins were significantly downregulated and organotypic retinal explant culture confirmed the selective loss of SPP1 in RMG upon treatment. Since SPP1 in the retina has been described neuroprotective for photoreceptors and functions against experimentally induced cell swelling, it’s rapid loss under diabetic conditions may point to a direct involvement of RMG to the early neurodegenerative processes driving DR. Data are available via ProteomeXchange with identifier PXD015879. |
Databáze: | OpenAIRE |
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