5- and 6-glycosylation of transferrin in patients with Alzheimer's disease

Simple item page
dc.contributor.authorVan Rensburg S.J.
dc.contributor.authorBerman P.
dc.contributor.authorPotocnik F.
dc.contributor.authorMacGregor P.
dc.contributor.authorHon D.
dc.contributor.authorDe Villiers N.
dc.date.accessioned2011-05-15T16:17:23Z
dc.date.available2011-05-15T16:17:23Z
dc.date.issued2004
dc.description.abstractTransferrin 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.
dc.description.versionConference Paper
dc.identifier.citationMetabolic Brain Disease
dc.identifier.citation19
dc.identifier.citation1-2
dc.identifier.issn08857490
dc.identifier.other10.1023/B:MEBR.0000027420.50736.62
dc.identifier.urihttp://hdl.handle.net/10019.1/14193
dc.subjectalcohol
dc.subjectprotein antibody
dc.subjecttransferrin
dc.subjectfree radical
dc.subjectn acetylneuraminic acid
dc.subjectAlzheimer disease
dc.subjectblotting
dc.subjectclinical article
dc.subjectconference paper
dc.subjectcontrolled study
dc.subjectglycosylation
dc.subjectheterozygote
dc.subjecthomozygote
dc.subjecthuman
dc.subjectisoelectric focusing
dc.subjectmolecule
dc.subjectsialylation
dc.subjectalcoholism
dc.subjectarticle
dc.subjectgenetics
dc.subjectmetabolism
dc.subjectoxidation reduction reaction
dc.subjectAlcoholism
dc.subjectAlzheimer Disease
dc.subjectFree Radicals
dc.subjectGlycosylation
dc.subjectHeterozygote
dc.subjectHomozygote
dc.subjectHumans
dc.subjectIsoelectric Focusing
dc.subjectN-Acetylneuraminic Acid
dc.subjectOxidation-Reduction
dc.subjectTransferrin
dc.title5- and 6-glycosylation of transferrin in patients with Alzheimer's disease
dc.typeConference Paper
Files
Collections
Stellenbosch University - Scopus Tygerberg Hospital Publications