High nickel release from 1- and 2-euro coins

Nestle, Frank O.; Speidel, Hannes J. C.; Speidel, Markus O.

doi:10.1038/419132a

Cited by 101 publications

(79 citation statements)

References 3 publications

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“…Thus, the nickel is widely present in soil, meteorities and emitted from volcanoes. [112][113][114] The range in surface water and groundwater of nickel levels was about 3 and 10 mg/L. Based on this average nickel concentration, a person took 2 L/day water would intake 4 to 8.6 mg/L nickel.…”

Section: Nickelmentioning

confidence: 99%

Heavy metals, islet function and diabetes development

Lin¹,

Yang²,

Huang³

et al. 2009

Islets

199

131

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Section: Nickelmentioning

confidence: 99%

Heavy metals, islet function and diabetes development

Lin¹,

Yang²,

Huang³

et al. 2009

Islets

199

131

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“…11 Locally this concentration can probably easily reach a micromolar level in the stratum corneum, especially because some kinds of jewelry and coins release 100 times more nickel than allowed by the 10 Directive. 29,30 Taking the protonation constants and stability constants of Ni(II) complexes from the literature 26,31,32 and from this paper we calculated the distribution of Ni(II) species for above concentrations of ligands and of 1 µM nickel ions (Fig. 7).…”

mentioning

confidence: 99%

cis-Urocanic acid as a potential nickel(ii) binding molecule in the human skin

et al. 2014

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5cis-Urocanic acid, a derivative of histidine, is one of essential components of human skin. We found that it can bind nickel(II) ions in a pH-dependent manner, with the dissociation constant in the low millimolar range, as revealed by potentiometry, and confirmed by isothermal titration calorimetry and UV-vis spectroscopy. The binding occurs within the physiological skin pH range. Considering the fact that cisurocanic acid is present in the human skin in concentrations as high as millimolar, this molecule may be a 10 physiologically important player in nickel trafficking in the human organism.

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“…Ni-specific, IFN-␥-producing CD4 ϩ and CD8 ϩ effector T cells are believed to be responsible for sensitization as well as for skin reactions (4,5), whereas IL-10-and TGF-␤-secreting CD4 ϩ regulatory T cells are thought to down-modulate the response (2). Ag-specific activation of these cells upon skin contact with Ni-containing alloys such as the new one-and two-euro coins requires translocation of Ni 2ϩ from the surface to Langerhans cells (LC) 5 in deeper layers of the skin (6,7). According to current models, LC will thereby be stimulated to mature and migrate to local lymph nodes where they supposedly present Ni-HLA epitopes to T cells (7,8).…”

mentioning

confidence: 99%

Metal-Protein Complex-Mediated Transport and Delivery of Ni2+ to TCR/MHC Contact Sites in Nickel-Specific Human T Cell Activation

Thierse

Moulon

Allespach

et al. 2004

The Journal of Immunology

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Nickel allergy clearly involves the activation of HLA-restricted, skin-homing, Ni-specific T cells by professional APCs. Nevertheless, knowledge concerning the molecular details of metal-protein interactions underlying the transport and delivery of metal ions to APC during the early sensitization phase and their interactions with HLA and TCRs is still fragmentary. This study investigates the role of human serum albumin (HSA), a known shuttling molecule for Ni2+ and an often-disregarded, major component of skin, in these processes. We show that Ni-saturated HSA complexes (HSA-Ni) induce and activate Ni-specific human T cells as potently as Ni salt solutions when present at equimolar concentrations classically used for in vitro T cell stimulation. However, neither HSA itself nor its Ni-binding N-terminal peptide are involved in determining the specificity of antigenic determinants. In fact, HSA could be replaced by xenogeneic albumins exhibiting sufficient affinity for Ni2+ as determined by surface plasmon resonance (Biacore technology) or atomic absorption spectroscopy. Moreover, despite rapid internalization of HSA-Ni by APC, it was not processed into HLA-associated epitopes recognizable by Ni-specific T cells. In contrast, the presence of HSA-Ni in the vicinity of transient contacts between TCR and APC-exposed HLA molecules appeared to facilitate a specific transfer of Ni2+ from HSA to high-affinity coordination sites created at the TCR/HLA-interface.

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High nickel release from 1- and 2-euro coins

Cited by 101 publications

References 3 publications

Heavy metals, islet function and diabetes development

Heavy metals, islet function and diabetes development

cis-Urocanic acid as a potential nickel(ii) binding molecule in the human skin

Metal-Protein Complex-Mediated Transport and Delivery of Ni2+ to TCR/MHC Contact Sites in Nickel-Specific Human T Cell Activation

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