Albumin Facilitates Zinc Acquisition by Endothelial Cells

Rowe, David J.; Bobilya, Dennis J.

doi:10.1111/j.1525-1373.2000.22418.x

Cited by 9 publications

(5 citation statements)

References 59 publications

(97 reference statements)

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“…Albumin plays important role in blood plasma zinc(II) "buffering" [122]. It participates in the transport of newly absorbed zinc(II) from intestine to liver, it assist the transfer of zinc(II) to target sites [123], it promotes zinc(II) uptake by endothelial cells [124]. However, mechanisms of zinc(II) transfer from albumin are not completely understood.…”

Section: Blood Plasma Levelmentioning

confidence: 99%

Insight to Physiology and Pathology of Zinc(II) Ions and Their Actions in Breast and Prostate Carcinoma

Gumulec¹,

Masařík²,

Křížková³

et al. 2011

CMC

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Zinc(II) ions contribute to a number of biological processes e.g. DNA synthesis, gene expression, enzymatic catalysis, neurotransmission, and apoptosis. Zinc(II) dysregulation, deficiency and over-supply are connected with various diseases, particularly cancer. 98 % of human body zinc(II) is localized in the intracellular compartment, where zinc(II) is bound with low affinity to metallothionein (MT). Zinc transporters ZIP and ZnT maintain transmembrane transport from/to cells or organelles. Imbalance of their regulation is described in cancers, particularly prostate (down-regulated zinc transporters ZIP1, 2, 3 and ZnT-2) and breast, notably its high-risk variant (up-regulated ZIP6, 7, 10). As a result, intracellular and even blood plasma zinc(II) levels are altered. MT protects cells against oxidative stress, because it cooperates with reduced glutathione (GSH). Recent studies indicate elevated serum level of MT in a number of malignancies, among others in breast, and prostate. MT together with zinc(II) affect apoptosis and proliferation, thus together with its antioxidative effects it may affect cancer. To date, only little is known about the influence of zinc(II) and MT on cancer, while these compounds may play an important role in pathogenesis. This review concludes current data regarding the impact of zinc(II) on the pathogenesis of breast and prostate cancers with potential outlines of new, targeted therapy and prevention. Moreover, blood plasma zinc(II) and MT levels and dietary zinc(II) intake are discussed in relation to breast and prostate cancer risk.

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Section: Blood Plasma Levelmentioning

confidence: 99%

Insight to Physiology and Pathology of Zinc(II) Ions and Their Actions in Breast and Prostate Carcinoma

Gumulec¹,

Masařík²,

Křížková³

et al. 2011

CMC

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“…80% of all plasma zinc [4]. Numerous studies have also demonstrated that albumin modulates zinc uptake into cells [5,6], and some suggest that, at least in some cell types, such as endothelial cells, there is a receptor-mediated endocytosis pathway for albumin-bound zinc uptake [7], and that zinc transport across endothelia involves co-transport with albumin [8]. Furthermore, certain cases of familial hyperzincaemia appear to be due to increased zinc binding to albumin [9].…”

Section: Introductionmentioning

confidence: 98%

Albumin as a zinc carrier: properties of its high-affinity zinc-binding site

Jin

Stewart

Sadler

et al. 2008

Biochemical Society Transactions

214

162

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Although details of the molecular mechanisms for the uptake of the essential nutrient zinc into the bloodstream and its subsequent delivery to zinc-requiring organs and cells are poorly understood, it is clear that in vertebrates the majority of plasma zinc (9-14 microM; approx. 75-85%) is bound to serum albumin, constituting part of the so-called exchangeable pool. The binding of metal ions to serum albumins has been the subject of decades of studies, employing a multitude of techniques, but only recently has the identity and putative structure of the major zinc site on albumin been reported. Intriguingly, this site is located at the interface between two domains, and involves two residues from each of domains I and II. Comparisons of X-ray crystal structures of free and fatty-acid bound human serum albumin suggest that zinc binding to this site and fatty acid binding to one of the five major sites may be interdependent. Interactive binding of zinc and long-chain fatty acids to albumin may therefore have physiological implications.

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“…We therefore investigated the results of adding gadolinium ions in the form of gadolinium chloride, and found that this resulted in binding of, on average, 1.7 gadolinium ions per albumin molecule (these albumin molecules bearing no DTPA). This result is readily explained by the presence of two metal-binding sites in each HSA molecule, and which in physiological conditions bind zinc (Stewart et al 2003;André and Guillaume 2004;Rowe and Bobilya 2000). This gadolinium binding would be of potential toxicological significance, because these gadolinium ions could escape into the tissues and exert significant toxic effects.…”

Section: Gadolinium Content Of Hsa-dtpa-gd Conjugatesmentioning

confidence: 80%

Albumin-based nanoparticles as magnetic resonance contrast agents: II. Physicochemical characterisation of purified and standardised nanoparticles

Abdelmoez

Thurner

Wallnöfer

et al. 2010

Histochem Cell Biol

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We are developing a nanoparticulate histochemical reagent designed for histochemistry in living animals (molecular imaging), which should finally be useful in clinical imaging applications. The iterative development procedure employed involves conceptual design of the reagent, synthesis and testing of the reagent, then redesign based on data from the testing; each cycle of testing and development generates a new generation of nanoparticles, and this report describes the synthesis and testing of the third generation. The nanoparticles are based on human serum albumin and the imaging modality selected is magnetic resonance imaging (MRI). Testing the second particle generation with newly introduced techniques revealed the presence of impurities in the final product, therefore we replaced dialysis with diafiltration. We introduced further testing methods including thin layer chromatography, arsenazo III as chromogenic assay for gadolinium, and several versions of polyacrylamide gel electrophoresis, for physicochemical characterisation of the nanoparticles and intermediate synthesis compounds. The high grade of chemical purity achieved by combined application of these methodologies allowed standardised particle sizes to be achieved (low dispersities), and accurate measurement of critical physicochemical parameters influencing particle size and imaging properties. Regression plots confirmed the high purity and standardisation. The good degree of quantitative physicochemical characterisation aided our understanding of the nanoparticles and allowed a conceptual model of them to be prepared. Toxicological screening demonstrated the extremely low toxicity of the particles. The high magnetic resonance relaxivities and enhanced mechanical stability of the particles make them an excellent platform for the further development of MRI molecular imaging.

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Albumin Facilitates Zinc Acquisition by Endothelial Cells

Cited by 9 publications

References 59 publications

Insight to Physiology and Pathology of Zinc(II) Ions and Their Actions in Breast and Prostate Carcinoma

Insight to Physiology and Pathology of Zinc(II) Ions and Their Actions in Breast and Prostate Carcinoma

Albumin as a zinc carrier: properties of its high-affinity zinc-binding site

Albumin-based nanoparticles as magnetic resonance contrast agents: II. Physicochemical characterisation of purified and standardised nanoparticles

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