5- and 6-glycosylation of transferrin in patients with Alzheimer's disease
Date
2004
Authors
Van Rensburg S.J.
Berman P.
Potocnik F.
MacGregor P.
Hon D.
De Villiers N.
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
Transferrin is a glycosylated metal-carrying serum protein. One of the biological functions of glycosylation is to regulate the life span of proteins, less glycosylation leading to a faster clearance of a protein from the circulation. In the case of transferrin, this would indirectly also influence iron homeostasis. Higher glycosylation has been demonstrated in patients with Parkinson's disease and rheumatoid arthritis. A genetic variant of transferrin, TfC2, occurs with increased frequency in patients with Alzheimer's disease (AD), rheumatoid arthritis, and other diseases associated with a free radical etiology. Investigations have so far not revealed the reason for the pro-oxidative qualities of TfC2. In this study the glycosylation of Tf in AD (TfC1 homozygotes and TfC1C2 heterozygotes) was compared with alcohol-induced dementia (AID) patients and nondemented, age-matched controls, using isoelectric focusing followed by blotting with anti-Tf antibodies. In TfC1 homozygotes a shift was found toward higher sialylation, but in TfC1C2 heterozygotes the 5- and 6-sialylated bands were less concentrated. The decreased sialalytion found for TfC1C2 heterozygotes, may indicate that the pro-oxidative TfC2 molecules are removed from the circulation at a faster rate than TfC1. This may be of benefit to AD patients having TfC2, but still does not explain why this Tf variant is pro-oxidative.
Description
Keywords
alcohol, protein antibody, transferrin, free radical, n acetylneuraminic acid, Alzheimer disease, blotting, clinical article, conference paper, controlled study, glycosylation, heterozygote, homozygote, human, isoelectric focusing, molecule, sialylation, alcoholism, article, genetics, metabolism, oxidation reduction reaction, Alcoholism, Alzheimer Disease, Free Radicals, Glycosylation, Heterozygote, Homozygote, Humans, Isoelectric Focusing, N-Acetylneuraminic Acid, Oxidation-Reduction, Transferrin
Citation
Metabolic Brain Disease
19
1-2
19
1-2