High glucose treatment promotes extracellular matrix proteome remodeling in Mller glial cells.

PeerJ

Research Unit Protein Science and Metabolomics and Proteomics Core Facility, Helmholtz Center Munich, German Research Center for Environmental Health GmbH, Munich, Germany.

Published: May 2021

AI Article Synopsis

  • * Researchers used a quantitative proteomic approach to analyze changes in the protein composition of porcine RMG after exposure to high glucose and glycolysis inhibition.
  • * Results showed significant alterations, particularly in extracellular matrix proteins, with the loss of Osteopontin (SPP1) suggesting that RMG might contribute to neurodegenerative changes in the early stages of DR.

Article Abstract

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 Mller 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, its 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8139267PMC
http://dx.doi.org/10.7717/peerj.11316DOI Listing

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