Metabolic alteration of the N-glycan structure of a protein from patients with a heterozygous protein deficiency
Authors
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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Other Contributors
Issue Date
2004-12-24
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
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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.
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.
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)
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/
Rensselaer Polytechnic Institute, Troy, NY
Biochimica et Biophysica Acta - Molecular Basis of Disease
https://harc.rpi.edu/
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A full text version is available in DSpace@RPI
Open Access
Open Access