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dc.rights.licenseOpen Access
dc.contributor.authorZhang, Fuming
dc.contributor.authorBries, Andrew D.
dc.contributor.authorLang, Sybil C.
dc.contributor.authorWang, Qun
dc.contributor.authorMurhammer, David W.
dc.contributor.authorWeiler, John M.
dc.contributor.authorLinhardt, Robert J.
dc.date2004
dc.date.accessioned2022-06-23T03:52:47Z
dc.date.available2022-06-23T03:52:47Z
dc.date.issued2004-12-24
dc.identifier.citationMetabolic 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.
dc.identifier.issn9254439
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5154
dc.identifier.urihttps://doi.org/10.1016/j.bbadis.2004.08.006
dc.descriptionBiochimica Biophysica Acta, 1739, 43-49
dc.descriptionNote : 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.
dc.description.abstractGlycosylation, 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.
dc.description.sponsorshipNational Science Foundation
dc.languageen_US
dc.language.isoENG
dc.publisherElsevier
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofBiochimica et Biophysica Acta - Molecular Basis of Disease
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleMetabolic alteration of the N-glycan structure of a protein from patients with a heterozygous protein deficiency
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1016/j.bbadis.2004.08.006
dc.rights.holderIn 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/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages43-49
rpi.description.volume1739


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