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Metal cation symporter ZIP8

Definition:

Electroneutral divalent metal cation:bicarbonate symporter of the plasma membrane mediating the cellular uptake of zinc and manganese, two divalent metal cations important for development, tissue homeostasis and immunity. Transports an electroneutral complex composed of a divalent metal cation and two bicarbonate anions or alternatively a bicarbonate and a selenite anion. Thereby, it also contributes to the cellular uptake of selenium, an essential trace metal and micronutrient. Also imports cadmium a non-essential metal which is cytotoxic and carcinogenic. May also transport iron and cobalt through membranes. Through zinc import, indirectly regulates the metal-dependent transcription factor MTF1 and the expression of some metalloproteases involved in cartilage catabolism and also probably heart development. Also indirectly regulates the expression of proteins involved in cell morphology and cytoskeleton organization. Indirectly controls innate immune function and inflammatory response by regulating zinc cellular uptake which in turn modulates the expression of genes specific of these processes. Protects, for instance, cells from injury and death at the onset of inflammation. By regulating zinc influx into monocytes also directly modulates their adhesion to endothelial cells and arteries (By similarity). Reclaims manganese from the bile at the apical membrane of hepatocytes, thereby regulating the activity of the manganese-dependent enzymes through the systemic levels of the nutrient. Also participates in manganese reabsorption in the proximal tubule of the kidney. By mediating the extracellular uptake of manganese by cells of the blood-brain barrier, may also play a role in the transport of the micronutrient to the brain. With manganese cellular uptake also participates in mitochondrial proper function. Finally, also probably functions intracellularly, translocating zinc from lysosome to cytosol to indirectly enhance the expression of specific genes during TCR-mediated T cell activation.

References:

[1]. Nasim A Begum, et al. Mycobacterium bovis BCG cell wall and lipopolysaccharide induce a novel gene, BIGM103, encoding a 7-TM protein: identification of a new protein family having Zn-transporter and Zn-metalloprotease signatures. Genomics. 2002 Dec;80(6):630-45. [Content Brief]

[2]. Ming-Jie Liu, et al. ZIP8 regulates host defense through zinc-mediated inhibition of NF-κB. Cell Rep. 2013 Feb 21;3(2):386-400. [Content Brief]

[3]. Wen Lin, et al. Zinc transporter Slc39a8 is essential for cardiac ventricular compaction. J Clin Invest. 2018 Feb 1;128(2):826-833. [Content Brief]

[4]. Xiangrong Geng, et al. Role of ZIP8 in regulating cell morphology and NF-κB/Snail2 signaling. Metallomics. 2018 Jul 18;10(7):953-964. [Content Brief]

[5]. Joseph R McDermott, et al. Zinc- and bicarbonate-dependent ZIP8 transporter mediates selenite uptake. Oncotarget. 2016 Jun 7;7(23):35327-40. [Content Brief]

[6]. Tolunay B Aydemir, et al. Zinc transporter ZIP8 (SLC39A8) and zinc influence IFN-gamma expression in activated human T cells. J Leukoc Biol. 2009 Aug;86(2):337-48. [Content Brief]

[7]. Wen Lin, et al. Hepatic metal ion transporter ZIP8 regulates manganese homeostasis and manganese-dependent enzyme activity. J Clin Invest. 2017 Jun 1;127(6):2407-2417. [Content Brief]

[8]. Charlie J Pyle, et al. Zinc Modulates Endotoxin-Induced Human Macrophage Inflammation through ZIP8 Induction and C/EBPβ Inhibition. PLoS One. 2017 Jan 5;12(1):e0169531. [Content Brief]

[9]. Chia-Yu Wang, et al. ZIP8 is an iron and zinc transporter whose cell-surface expression is up-regulated by cellular iron loading. J Biol Chem. 2012 Oct 5;287(41):34032-43. [Content Brief]

[10]. Eun-Kyung Choi, et al. Functional analysis of SLC39A8 mutations and their implications for manganese deficiency and mitochondrial disorders. Sci Rep. 2018 Feb 16;8(1):3163. [Content Brief]

[11]. Ruoxin Zhang, et al. A blood pressure-associated variant of the SLC39A8 gene influences cellular cadmium accumulation and toxicity. Hum Mol Genet. 2016 Sep 15;25(18):4117-4126. [Content Brief]

[12]. Beth Besecker, et al. The human zinc transporter SLC39A8 (Zip8) is critical in zinc-mediated cytoprotection in lung epithelia. Am J Physiol Lung Cell Mol Physiol. 2008 Jun;294(6):L1127-36. [Content Brief]

[13]. Kym M Boycott, et al. Autosomal-Recessive Intellectual Disability with Cerebellar Atrophy Syndrome Caused by Mutation of the Manganese and Zinc Transporter Gene SLC39A8. Am J Hum Genet. 2015 Dec 3;97(6):886-93. [Content Brief]

[14]. Brittany L Steimle, et al. The solute carriers ZIP8 and ZIP14 regulate manganese accumulation in brain microvascular endothelial cells and control brain manganese levels. J Biol Chem. 2019 Dec 13;294(50):19197-19208. [Content Brief]

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