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    Metabolic alteration of the N-glycan structure of a protein from patients with a heterozygous protein deficiency

    Author
    Zhang, Fuming; Bries, Andrew D.; Lang, Sybil C.; Wang, Qun; Murhammer, David W.; Weiler, John M.; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    METABOLIC ALTERATION OF THE N-GLYCAN STRUCTURE OF A PROTEIN FROM.pdf (992.8Kb)
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    Date Issued
    2004-12-24
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/;
    Full Citation
    Metabolic alteration of the N-glycan structure of a protein from patients with a heterozygous protein deficiency, F. Zhang, A. D. Bries, S. C. Lang, Q. Wang, D. W. Murhammer, J. M. Weiler, R. J. Linhardt, Biochimica Biophysica Acta, 1739, 43-49, 2004.
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    URI
    https://hdl.handle.net/20.500.13015/5154; https://doi.org/10.1016/j.bbadis.2004.08.006
    Abstract
    Glycosylation, an important post-translation modification, could alter biological activity or influence the clearance rates of glycoproteins. We report here the first example of a heterozygous protein deficiency leading to metabolic alteration of N-glycan structures in residual secreted protein. Analysis of C1 esterase inhibitor (C1INH) glycans from normal individuals and patients with hereditary deficiency of C1INH demonstrated identical O-glycan structures but the N-glycans of patients with a heterozygous genetic deficiency were small, highly charged and lacked sialidase releasable N-acetylneuraminic acid. Structural studies indicate that the charge character of these aberrant N-glycan structures may result from the presence of mannose-6-phosphate residues. These residues might facilitate secretion of C1INH through an alternate lysosomal pathway, possibly serving as a compensatory mechanism to enhance plasma levels of C1INH in these deficient patients.;
    Description
    Biochimica Biophysica Acta, 1739, 43-49; 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.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Publisher
    Elsevier
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Biochimica et Biophysica Acta - Molecular Basis of Disease; https://harc.rpi.edu/;
    Access
    Open Access; A full text version is available in DSpace@RPI;
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