Transport routes of metalloids into and out of the cell: A review of the current knowledge

Except for their extra- and intra-cellular interfaces, cell membranes are hydrophobic and inhibit the transport of hydrophilic molecules. Metalloids in aqueous solutions form chemical species with oxygen and hydroxyl groups and, therefore, exist as hydrophilic neutral polar solutes or as hydrophilic...

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Published in:Chemico-biological interactions Vol. 197; no. 1; pp. 47 - 57
Main Authors: Zangi, Ronen, Filella, Montserrat
Format: Journal Article
Language:English
Published: Ireland Elsevier Ireland Ltd 15-04-2012
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Abstract Except for their extra- and intra-cellular interfaces, cell membranes are hydrophobic and inhibit the transport of hydrophilic molecules. Metalloids in aqueous solutions form chemical species with oxygen and hydroxyl groups and, therefore, exist as hydrophilic neutral polar solutes or as hydrophilic anions. This characteristic of metalloids introduces a large barrier for their passage through the cell membrane via unaided diffusion. The necessity for an uptake mechanism for metalloids arises from the requirement of these species for the maintenance of life, such as the need of boron for plant cells. Conversely, the transport of these species out of the cell is necessary because some metalloids are toxic, such as arsenic and antimony, and their entrance into the cell is undesirable. The undesired uptake of these toxic species is possible via pathways designed for the uptake of other structurally and chemically similar essential compounds. Therefore, the extrusion of arsenic and antimony out of the cell is an example of a detoxification mechanism. As a consequence of the hydrophobic character of the cell membrane in all living systems, the main route for the uptake and efflux of metalloids is facilitated by transmembrane proteins, driven either by concentration gradients or by energy-fueled pumps. However, metalloids forming or embedded in nano-sized particles escape the need to cross the cell membrane because these particles can be taken into the cell by endocytosis. Here, we review the uptake and efflux pathways of boron, silicon, arsenic, and antimony through the cell membranes of different organisms and the protein channels involved in these processes. In particular, passive diffusion via aquaglyceroporins, active transport via primary and secondary ion pumps, extrusion into vacuoles of metalloid-thiol conjugates via ATP-binding cassette, the efflux of methylated metalloids, and endocytosis are summarized.
AbstractList Except for their extra- and intra-cellular interfaces, cell membranes are hydrophobic and inhibit the transport of hydrophilic molecules. Metalloids in aqueous solutions form chemical species with oxygen and hydroxyl groups and, therefore, exist as hydrophilic neutral polar solutes or as hydrophilic anions. This characteristic of metalloids introduces a large barrier for their passage through the cell membrane via unaided diffusion. The necessity for an uptake mechanism for metalloids arises from the requirement of these species for the maintenance of life, such as the need of boron for plant cells. Conversely, the transport of these species out of the cell is necessary because some metalloids are toxic, such as arsenic and antimony, and their entrance into the cell is undesirable. The undesired uptake of these toxic species is possible via pathways designed for the uptake of other structurally and chemically similar essential compounds. Therefore, the extrusion of arsenic and antimony out of the cell is an example of a detoxification mechanism. As a consequence of the hydrophobic character of the cell membrane in all living systems, the main route for the uptake and efflux of metalloids is facilitated by transmembrane proteins, driven either by concentration gradients or by energy-fueled pumps. However, metalloids forming or embedded in nano-sized particles escape the need to cross the cell membrane because these particles can be taken into the cell by endocytosis. Here, we review the uptake and efflux pathways of boron, silicon, arsenic, and antimony through the cell membranes of different organisms and the protein channels involved in these processes. In particular, passive diffusion via aquaglyceroporins, active transport via primary and secondary ion pumps, extrusion into vacuoles of metalloid-thiol conjugates via ATP-binding cassette, the efflux of methylated metalloids, and endocytosis are summarized.
Author Filella, Montserrat
Zangi, Ronen
Author_xml – sequence: 1
  givenname: Ronen
  surname: Zangi
  fullname: Zangi, Ronen
  email: r.zangi@ikerbasque.org
  organization: Department of Organic Chemistry I, University of the Basque Country UPV/EHU, Avenida de Tolosa 72, 20018 San Sebastian, Spain
– sequence: 2
  givenname: Montserrat
  surname: Filella
  fullname: Filella, Montserrat
  organization: Institute F.-A. Forel, University of Geneva, Route de Suisse 10, CH-1290 Versoix, Switzerland
BackLink https://www.ncbi.nlm.nih.gov/pubmed/22370390$$D View this record in MEDLINE/PubMed
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Keywords Channel proteins
Passive and active transport
Endocytosis
Nano-particles
Influx and efflux
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Snippet Except for their extra- and intra-cellular interfaces, cell membranes are hydrophobic and inhibit the transport of hydrophilic molecules. Metalloids in aqueous...
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SubjectTerms active transport
Animals
anions
antimony
aqueous solutions
arsenic
Biological Transport
Biological Transport, Active
boron
Cell Membrane - metabolism
cell membranes
cells
Channel proteins
chemical speciation
Endocytosis
extrusion
Humans
hydrophobicity
Influx and efflux
Membrane Transport Proteins - metabolism
Metalloids - metabolism
Nano-particles
nanoparticles
oxygen
Passive and active transport
silicon
solutes
toxicity
transmembrane proteins
transporters
vacuoles
Title Transport routes of metalloids into and out of the cell: A review of the current knowledge
URI https://dx.doi.org/10.1016/j.cbi.2012.02.001
https://www.ncbi.nlm.nih.gov/pubmed/22370390
https://search.proquest.com/docview/1009127960
https://search.proquest.com/docview/1492615665
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