Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
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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.
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.;
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.
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Biochimica et Biophysica Acta - Molecular Basis of Disease; https://harc.rpi.edu/;
Open Access; A full text version is available in DSpace@RPI;