Transferrin: structure, function and potential therapeutic actions

Gomme, Peter T.; McCann, Karl B.; Bertolini, Joseph

doi:10.1016/s1359-6446(04)03333-1

Cited by 384 publications

(293 citation statements)

References 72 publications

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“…It is a powerful chelator, capable of binding iron tightly but reversibly. A molecule of transferrin can bind two atoms of ferric iron (Fe 3+ ) with high affinity, which is higher in the extracellular pH of 7.4 and decreases in acidified endosomes, allowing the dissociation of Fe 3+ (Gomme and McCann 2005). The primary role of transferrin is to transport iron safely around the body to supply growing cells (Huebers and Finch 1987).…”

Section: Transferrinmentioning

confidence: 99%

Acute phase proteins and their use in the diagnosis of diseases in ruminants: a review

Tóthová¹,

Nagy²,

Kováč³

2014

Vet. Med. - Czech

152

159

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ABSTRACT:The acute phase response is a complex systemic early-defence system of reactions activated by trauma, infection, tissue damage, inflammation, stress or neoplasia. One of the most important elements of this response is the increased hepatic synthesis of some plasma proteins, collectively known as acute phase proteins. The discovery of these new biomarkers has allowed the clinical monitoring of different diseases; therefore, their clinical application has been studied widely in human medicine in order to improve the diagnosis, evaluation, treatment, prognosis and therapeutics of many diseases. Although a wide range of studies have been carried out to determine the usefulness of acute phase proteins in several diseases also in animals, they are still relatively under-utilised in veterinary medicine, predominantly in farm animals. The acute phase response and clinical application of acute phase proteins in ruminants are reviewed in this article, including their diagnostic use in clinical practice and application in the monitoring of treatment, which is one of the most promising practical uses of these proteins.

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Section: Transferrinmentioning

confidence: 99%

Acute phase proteins and their use in the diagnosis of diseases in ruminants: a review

Tóthová¹,

Nagy²,

Kováč³

2014

Vet. Med. - Czech

152

159

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“…-create binding pocket [73]. Gly65, Glu83, Tyr85, Arg124, Lys206, Ser248, Lys296 -they stabilize metal binding site and play crucial role in iron release [73].…”

Section: Methodsmentioning

confidence: 99%

“…All identified sites were situated on the protein surface, with site 3 forming a kind of shallow nest. Transferrin The most plausible binding pocket observed for transferrin is placed in a functionally important area of this protein including Asn413 and Asn611 [73] and it was identified as site 1. The second binding site was the target of 20% of the ligand population.…”

Section: Binding Sites Analysismentioning

confidence: 99%

Rapid insight into C60 influence on biological functions of proteins

et al. 2017

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Experimental methods of investigations of nanoparticle (NP)-protein interactions are limited, because they require a high amount of samples and the NPs tend to interfere with spectral results. Therefore, molecular modeling is a commonly accepted tool in such kind of investigations. Examining the molecule toxicity on the molecular level, we usually want to know, mainly, the location of the ligand on the protein surface and what is an influence of such a contact on the biological functions of the protein. In the presented work, we demonstrate that multiple-docking of the ligand from a random start and with large grid volume, to let the ligand search the whole protein surface, allows to find the best binding sites and gives reliable results considering ligand-protein interactions. In the present work, we have constructed six models of bronchoalveolar lavage fluids proteins: α1-antitripsin, albumin, ceruloplasmin, lactoferrin, lysozyme, and transferrin with fullerene, C 60 utilizing molecular docking methods. The most probable results were examined with steered molecular dynamics (SMD) to see, if the simple docking method is able to predict the fullerene binding affinity. Albumin and lysozyme were already widely investigated and literature data is available for their complexes with fullerene C 60 and/or its derivatives. Thus, we used these two models as a reference set to validate the used molecular modeling methods. With our best knowledge, interactions of the remaining four proteins with NPs have never been investigated in detail before. Our results indicate that fullerene C 60 readily interacts with all studied proteins and may have a large impact on their biological functions.

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“…For these studies we utilised an siRNA sequence for knockdown of luciferase in bioluminescent xenograft models, and transferrin as the ligand for cancer cell targeting. The receptor for transferrin is expressed on proliferating cells 22 and has been used for delivery of a range of therapeutic agents 23 to cancer cells, including siRNA. 24 Incorporation of transferrin-conjugated PEI into complexes has also been shown to improve DNA delivery to tumour cells; 25,26 the mechanism may involve shielding the positive charge on PEI-DNA complexes in vivo, reducing accumulation in 'first pass' organs and enabling them to reach the target tissues including tumours.…”

Section: -21mentioning

confidence: 99%