The responses of hyperglycemic dividing mesangial cells to heparin is mediated by the non-reducing terminal trisaccharide
AuthorWang, Christina P.; Hascall, Vincent C.; Zhang, Fuming; Linhardt, Robert J.; Abbadi, Amina; Wang, Aimin
SubjectBiology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Full CitationThe responses of hyperglycemic dividing mesangial cells to heparin is mediated by the non-reducing terminal trisaccharide. C.P. Wang, V.C. Hascall, F. Zhang, R.J. Linhardt, A. Abbadi, A Wang, Journal of Biological Chemistry, 290, 29045–29050, 2015.
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AbstractOur previous studies showed: (i) that growth-arrested G0/G1 rat mesangial cells stimulated to divide in hyperglycemic medium initiate intracellular hyaluronan synthesis that induces autophagy and the cyclin D3-induced formation of a monocyte-adhesive extracellular hyaluronan matrix after completing cell division; and (ii) that heparin inhibits the intracellular hyaluronan and autophagy responses, but after completing division, induces hyaluronan synthesis at the plasma membrane with the formation of a larger monocyte-adhesive hyaluronan matrix. This study shows: (i) that the non-terminal trisaccharide of heparin is sufficient to initiate the same responses as intact heparin, (ii) that a fully sulfated tetrasaccharide isolated from bacterial heparin lyase 1 digests of heparin that contains a Δ-2S-iduronate on the non-reducing end does not initiate the same responses as intact heparin, and (iii) that removal of the Δ-2S-iduronate to expose the fully sulfated trisaccharide (GlcNS(6S)-IdoUA(2S)-GlcNS(6S)) does initiate the same responses as intact heparin. These results provide evidence that mammalian heparanase digestion of heparin and heparan sulfate exposes a cryptic motif on the non-reducing termini that is recognized by a receptor on dividing cells.;
DescriptionJournal of Biological Chemistry, 290, 29045–29050; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
DepartmentThe Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
PublisherAmerican Society for Biochemistry and Molecular Biology (ASBMB) and Elsevier
RelationshipsThe Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Journal of Biological Chemistry; https://harc.rpi.edu/;
AccessCC BY — Creative Commons Attribution; Open Access; A full text version is available in DSpace@RPI;
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