Journal article
Integrated glycoproteomics identifies a role of N-glycosylation and galectin-1 on myogenesis and muscle development
R Blazev, C Ashwood, JL Abrahams, LH Chung, D Francis, P Yang, KI Watt, H Qian, GA Quaife-Ryan, JE Hudson, P Gregorevic, M Thaysen-Andersen, BL Parker
Molecular and Cellular Proteomics | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2021
Abstract
Many cell surface and secreted proteins are modified by the covalent addition of glycans that play an important role in the development of multicellular organisms. These glycan modifications enable communication between cells and the extracellular matrix via interactions with specific glycan-binding lectins and the regulation of receptor-mediated signaling. Aberrant protein glycosylation has been associated with the development of several muscular diseases, suggesting essential glycan- and lectin-mediated functions in myogenesis and muscle development, but our molecular understanding of the precise glycans, catalytic enzymes, and lectins involved remains only partially understood. Here, we q..
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Awarded by National Health and Medical Research Council
Funding Acknowledgements
This work was funded by an National Health and Medical Research Council (NHMRC) Early Career Fellowship and the University of Melbourne Driving Research Momentum program (to B. L. P.). J. E. H. is supported by grants and fellowships from the NHMRC and National Heart Foundation of Australia. The contents of the published material are solely the responsibility of the individual authors and do not reflect the view of NHMRC.