1989
DOI: 10.1016/0003-9861(89)90331-7
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Rat aglycotransferrin and human monoglycotransferrin: Production and metabolic properties

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Cited by 11 publications
(4 citation statements)
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“…The presence or absence of carbohydrate has no impact on the binding of iron to Tf or the binding of Tf to the TfR [345]. Removal of one or more of the four terminal sialic acids from the two biantenary glycans of Tf may target them for removal from the circulation by liver asialoreceptors [346]. …”
Section: A Brief History Of Human Serum Transferrinmentioning
confidence: 99%
“…The presence or absence of carbohydrate has no impact on the binding of iron to Tf or the binding of Tf to the TfR [345]. Removal of one or more of the four terminal sialic acids from the two biantenary glycans of Tf may target them for removal from the circulation by liver asialoreceptors [346]. …”
Section: A Brief History Of Human Serum Transferrinmentioning
confidence: 99%
“…Native hTF is a glycoprotein with two N-linked biantennary glycans in the C-lobe (at residues Asn413 and Asn611). While glycosylation appears to have no effect on TFR binding or iron uptake or release by hTF (Mason et al, 1993), it has been suggested that loss of the terminal sialic acids over time may play a role in clearance of hTF from the blood by asialo receptors in the liver (Regoeczi, Bolyos, & Chindemi, 1989). …”
Section: Transferrinmentioning
confidence: 99%
“…Glycosylation can regulate the lifespan of proteins. In vivo experiments in rats have shown that the half-life of Tf proteins without sugar chains is significantly lower than that of Tf proteins containing complex glycans [ 65 ], that is, less glycosylated proteins are degraded from the cell relatively quickly. This means that the TfC2 protein in AD cells can be removed more quickly, which is beneficial to the cells.…”
Section: Introductionmentioning
confidence: 99%