Manganese+2 exhibits dynamic binding to multiple ligands in human plasma

Critchfield, James W.; Keen, Carl L.

doi:10.1016/0026-0495(92)90290-q

Cited by 37 publications

(15 citation statements)

References 18 publications

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“…In blood, Mn +2 is predominantly (>99%) in the 2+ oxidation state and mainly bound to β-globulin and albumin. A small fraction of Mn +3 is complexed with transferrin [34,35]. Mn (in the 2+ oxidation state) transport across the blood–brain barrier (BBB) and cell membranes is facilitated by the divalent metal ion transporter 1 (DMT1), N -methyl-d-aspartate (NMDA) receptor channel and Zip8 [36-38], to name a few.…”

Section: Reviewmentioning

confidence: 99%

Manganese Neurotoxicity: a Focus on Glutamate Transporters

Karki

Lee

Aschner

2013

Ann of Occup and Environ Med

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Manganese (Mn) is an essential element that is required in trace amount for normal growth, development as well maintenance of proper function and regulation of numerous cellular and biochemical reactions. Yet, excessive Mn brain accumulation upon chronic exposure to occupational or environmental sources of this metal may lead to a neurodegenerative disorder known as manganism, which shares similar symptoms with idiopathic Parkinson’s disease (PD). In recent years, Mn exposure has gained public health interest for two primary reasons: continuous increased usage of Mn in various industries, and experimental findings on its toxicity, linking it to a number of neurological disorders. Since the first report on manganism nearly two centuries ago, there have been substantial advances in the understanding of mechanisms associated with Mn-induced neurotoxicity. This review will briefly highlight various aspects of Mn neurotoxicity with a focus on the role of astrocytic glutamate transporters in triggering its pathophysiology.

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Section: Reviewmentioning

confidence: 99%

Manganese Neurotoxicity: a Focus on Glutamate Transporters

Karki

Lee

Aschner

2013

Ann of Occup and Environ Med

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“…The expression of DMT1 has been identified in other cell types including brain, erythrocytes, renal epithelial cells, cardiomyocytes and human placenta epithelia, but not in thyroid gland [60]. In our study, it appears that the bioavailability of Mn is reduced due to altered transferrin (Tf) / Tf receptor (TfR) transport system, because several studies suggesting that Tf/TfR is the major transport ligand of manganese and iron in plasma [61,62,63,64]. Thereby, the Mn bound with Tf is in the Mn(III) state, which forms a stable and much stronger complex with Tf than Mn(II) [65].…”

Section: Discussionmentioning

confidence: 39%

Trace elements profile is associated with insulin resistance syndrome and oxidative damage in thyroid disorders: Manganese and selenium interest in Algerian participants with dysthyroidism

Maouche

Meskine

Alamir

et al. 2015

Journal of Trace Elements in Medicine and Biology

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“…For example, transferrins (Tf )-a major class of plasma iron-binding proteins-can accommodate a variety of other metal ions in the two available iron-binding sites of the Tf molecule (5). In particular, Tf has been shown to be one of the major manganese plasma transport proteins in both rodents and humans (6,7). Another potential pathway for manganese transport across biologic membranes is via the divalent metal ion transporter 1 (DMT-1), which can facilitate the influx/efflux of a number of divalent metal cations, including Mn 2þ (8,9).…”

Section: Introductionmentioning

confidence: 99%

Manganese cell labeling of murine hepatocytes using manganese(III)‐transferrin

Sotak

Sharer

Koretsky

2008

Contrast Media & Molecular

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Manganese(III)-transferrin [Mn(III)-Tf] was investigated as a way to accomplish manganese-labeling of murine hepatocytes for MRI contrast. It is postulated that Mn(III)-Tf can exploit the same transferrin-receptor-dependent and -independent metabolic pathways used by hepatocytes to transport the iron analog Fe(III)-Tf. More specifically, it was investigated whether manganese delivered by transferrin could give MRI contrast in hepatocytes. Comparison of the T1 and T2 relaxation times of Mn(III)-Tf and Fe(III)-Tf over the same concentration range showed that the r1 relaxivities of the two metalloproteins are the same in vitro, with little contribution from paramagnetic enhancement. The degree of manganese cell labeling following incubation for 2-7 h in 31.5 microm Mn(III)-Tf was comparable to that of hepatocytes incubated in 500 microm Mn2+ for 1 h. The intrinsic manganese tissue relaxivity between Mn(III)-Tf-labeled and Mn2+-labeled cells was found to be the same, consistent with Mn(III) being released from transferrin and reduced to Mn2+. For both treatment regimens, manganese uptake by hepatocytes appeared to saturate in the first 1-2 h of the incubation period and may explain why the efficiency of hepatocyte cell labeling by the two methods appeared to be comparable in spite of the approximately 16-fold difference in effective manganese concentration. Hepatocytes continuously released manganese, as detected by MRI, and this was the same for both Mn2+- and Mn(III)-Tf-labeled cells. Manganese release may be the result of normal hepatocyte function, much in the same way that hepatocytes excrete manganese into the bile in vivo. This approach exploits a biological process-namely receptor binding, endocytosis and endosomal acidification-to initiate the release of an MRI contrast agent, potentially conferring more specificity to the labeling process. The ubiquitous expression of transferrin receptors by eukaryotic cells should make Mn(III)-Tf particularly useful for manganese labeling of a wide variety of cells both in culture and in vivo.

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Manganese+2 exhibits dynamic binding to multiple ligands in human plasma

Cited by 37 publications

References 18 publications

Manganese Neurotoxicity: a Focus on Glutamate Transporters

Manganese Neurotoxicity: a Focus on Glutamate Transporters

Trace elements profile is associated with insulin resistance syndrome and oxidative damage in thyroid disorders: Manganese and selenium interest in Algerian participants with dysthyroidism

Manganese cell labeling of murine hepatocytes using manganese(III)‐transferrin

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