Glycation changes molecular organization and charge distribution in type I collagen fibrils.

Autor: Bansode S; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK., Bashtanova U; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK., Li R; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK., Clark J; Babraham Institute, Cambridge, CB22 3AT, UK., Müller KH; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.; Cambridge Advanced Imaging Centre, Department of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge, CB2 3DY, UK., Puszkarska A; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK., Goldberga I; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK., Chetwood HH; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK., Reid DG; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK., Colwell LJ; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK., Skepper JN; Cambridge Advanced Imaging Centre, Department of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge, CB2 3DY, UK., Shanahan CM; BHF Centre of Research Excellence, Cardiovascular Division, James Black Centre King's College London, 125 Coldharbour Lane, London, SE5 9NU, UK., Schitter G; Automation and Control Institute (ACIN), TU Wien, Gusshausstrasse 27-29, A-1040, Vienna, Austria., Mesquida P; Automation and Control Institute (ACIN), TU Wien, Gusshausstrasse 27-29, A-1040, Vienna, Austria. patrick.mesquida@kcl.ac.uk.; Department of Physics, King's College London, Strand, London, WC2R 2LS, UK. patrick.mesquida@kcl.ac.uk., Duer MJ; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK. mjd13@cam.ac.uk.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2020 Feb 25; Vol. 10 (1), pp. 3397. Date of Electronic Publication: 2020 Feb 25.
DOI: 10.1038/s41598-020-60250-9
Abstrakt: Collagen fibrils are central to the molecular organization of the extracellular matrix (ECM) and to defining the cellular microenvironment. Glycation of collagen fibrils is known to impact on cell adhesion and migration in the context of cancer and in model studies, glycation of collagen molecules has been shown to affect the binding of other ECM components to collagen. Here we use TEM to show that ribose-5-phosphate (R5P) glycation of collagen fibrils - potentially important in the microenvironment of actively dividing cells, such as cancer cells - disrupts the longitudinal ordering of the molecules in collagen fibrils and, using KFM and FLiM, that R5P-glycated collagen fibrils have a more negative surface charge than unglycated fibrils. Altered molecular arrangement can be expected to impact on the accessibility of cell adhesion sites and altered fibril surface charge on the integrity of the extracellular matrix structure surrounding glycated collagen fibrils. Both effects are highly relevant for cell adhesion and migration within the tumour microenvironment.
Databáze: MEDLINE
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