The biology of transferrin

Jong, Gerard de; Dijk, J.P. van; Eijk, H.G. Van

doi:10.1016/0009-8981(90)90278-z

Cited by 350 publications

(206 citation statements)

References 179 publications

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“…To the authors' knowledge, the first candidate gene association study of R. equi pneumonia compared the frequencies of single nucleotide polymorphisms (SNPs) in the transferrin gene ( Tf) among Thoroughbred foals from Kentucky that died of R. equi pneumonia with those of control Thoroughbred mares 19. In one study, the Tf gene was selected on the basis of its product's ability to bind iron because iron sequestration is a known host defense mechanism against bacterial replication 20, 21. The authors postulated that polymorphisms in the Tf gene might result in enhanced (or decreased) iron binding, which then could confer a selective advantage (or disadvantage) to survive infections with bacteria such as R. equi 19.…”

Section: Candidate Genesmentioning

confidence: 99%

Genetic Susceptibility to Rhodococcus equi

McQueen

Dindot

2015

Veterinary Internal Medicne

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Rhodococcus equi pneumonia is a major cause of morbidity and mortality in neonatal foals. Much effort has been made to identify preventative measures and new treatments for R. equi with limited success. With a growing focus in the medical community on understanding the genetic basis of disease susceptibility, investigators have begun to evaluate the interaction of the genetics of the foal with R. equi. This review describes past efforts to understand the genetic basis underlying R. equi susceptibility and tolerance. It also highlights the genetic technology available to study horses and describes the use of this technology in investigating R. equi. This review provides readers with a foundational understanding of candidate gene approaches, single nucleotide polymorphism‐based, and copy number variant‐based genome‐wide association studies, and next generation sequencing (both DNA and RNA).

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Section: Candidate Genesmentioning

confidence: 99%

Genetic Susceptibility to Rhodococcus equi

McQueen

Dindot

2015

Veterinary Internal Medicne

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“…The sample was applied to a miniaturized column containing a mixed ion exchange resin (AG50W X4, NH 4 + -form and AG2-X, Cl --form, Bio-Rad). Oligosaccharides were eluted with water and lyophilized.…”

Section: Mass Spectrometrymentioning

confidence: 99%

“…It has two main glycosylation sites at Asn-413 and Asn-611 [1]. The oligosaccharides found on these sites are mainly bi-and triantennary complex type glycans with terminal sialic acid [2][3][4]. Normal human serum typically contains a major transferrin glycoform containing two biantennary N-glycans with a total number of four sialic acid residues (tetrasialotransferrin), and minor isoforms with two (disialotransferrin), three (trisialotransferrin), and five (pentasialotransferrin) sialic acid residues.…”

Section: Introductionmentioning

confidence: 99%

Disialo–trisialo bridging of transferrin is due to increased branching and fucosylation of the carbohydrate moiety

Landberg

Åström

Kågedal

et al. 2012

Clinica Chimica Acta

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Methods: Nineteen serum samples showing di-tri bridging when analyzed by HPLC were collected. Transferrin was purified by affinity chromatography, and N-linked oligosaccharides were released enzymatically. The N-glycans were further analyzed by high performance anion-exchange chromatography with pulsed amperometric detection and MALDI-TOF mass spectrometry. Results:The HPLC-analysis showed three different types of glycoform patterns. The Nglycans from fifteen samples showed patterns with increased number of triantennary structures containing one or two fucose residues. One sample contained an increased amount of triantennary glycans without fucose. Three samples showed a glycosylation pattern similar to normal transferrin. Conclusions:The di-tri bridging phenomenon was associated with alterations in transferrin glycosylation in the majority of cases. Transferrin contained a higher extent of triantennary and often fucosylated N-linked oligosaccharides. These results may be important in future diagnostic approaches to liver diseases.3

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“…The transferrin receptor has greater affinity at physiologic pH for diferric transferrin than the apo form of the protein. Transferrin binding is followed by internalization of the receptor-transferrin-Fe complex via endocytosis (9,10). The Fe is released, in part, by acidification of the endosome and reduction of Fe 3ϩ to Fe 2ϩ (9,10).…”

mentioning

confidence: 99%

“…Transferrin binding is followed by internalization of the receptor-transferrin-Fe complex via endocytosis (9,10). The Fe is released, in part, by acidification of the endosome and reduction of Fe 3ϩ to Fe 2ϩ (9,10). The Fe 2ϩ is then transported to the cytoplasm through the action of the divalent metals transporter 1 (DMT-1), 3 also known as Nramp2 and DCT-1 (12).…”

mentioning

confidence: 99%

Multivalent Metal-Induced Iron Acquisition from Transferrin and Lactoferrin by Myeloid Cells

Olakanmi

Rasmussen

Lewis

et al. 2002

The Journal of Immunology

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We previously described a unique, high-capacity, ATP-independent mechanism through which myeloid cells acquire Fe from low-m.w. chelates. The rate of this Fe acquisition is markedly increased by cellular exposure to multivalent metal cations. Because most Fe in vivo is bound to transferrin or lactoferrin, we examined whether this mechanism also contributes to myeloid cell acquisition of Fe from transferrin and/or lactoferrin. Using HL-60 cells as a model system, we show cellular acquisition of 59Fe from both lactoferrin and transferrin that was unaffected by conditions that depleted the cells of ATP or disrupted their cytoskeleton. Fe acquisition was dramatically increased by cell exposure to various metals including Ga3+, Gd3+, Al3+, Fe3+, La3+, Zr4+, Sn4+, Cu2+, and Zn2+ by a process that was reversible. Exposure to these same metals also increased binding of both transferrin and lactoferrin to the cell surface by a process that does not appear to involve the well-described plasma membrane receptor for transferrin. Approximately 60% of the Fe acquired by the cells from transferrin and lactoferrin remained cell associated 18 h later. HL-60 cells possess a high-capacity multivalent metal-inducible mechanism for Fe acquisition from transferrin and lactoferrin that bears many similarities to the process previously described that allows these and other cell types to acquire Fe from low-m.w. Fe chelates. The biologic importance of this mechanism may relate to its high Fe acquisition capacity and the speed with which it is able to rapidly adapt to the level of extracellular Fe.

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The biology of transferrin

Cited by 350 publications

References 179 publications

Genetic Susceptibility to Rhodococcus equi

Genetic Susceptibility to Rhodococcus equi

Disialo–trisialo bridging of transferrin is due to increased branching and fucosylation of the carbohydrate moiety

Multivalent Metal-Induced Iron Acquisition from Transferrin and Lactoferrin by Myeloid Cells

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