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      Toxicity of organotin compounds: shared and unshared biochemical targets and mechanisms in animal cells.

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          Abstract

          Most biochemical effects of organotin compounds leading to toxicity are astonishingly similar in different animal species. In vitro tests, designed to explore organotin action modes at cell level by minimizing interfering factors, point out akin responses to these man-made environmental pollutants from prokaryotes to mammals. On the other hand, a broad susceptibility range to organotin toxicants of animal cells and variegated action mechanisms of these compounds have been reported both in vitro and in vivo studies. Endocrine and lipid homeostasis perturbations span from mollusks to mammals, in which organotins mainly favor fat accumulation. Lipid changes were also found in Bacteria. Organotin are immunotoxic both in invertebrates and humans. Mitochondria and membrane functions seem to be a preferred target of these lipophilic pollutants. The inhibition of key membrane-bound enzyme complexes such as Na,K-and F0F1-ATPases, accompanied by perturbation of hydromineral balance, membrane potential and bioenergetics, has been widely reported. Highly conserved mechanisms could be involved in organotin binding to nuclear receptors, membrane components and intracellular proteins as well as in promoting DNA damage, all widely shared action modes of these toxicants. Accordingly, the different responsiveness/refractoriness to organotins, here overviewed, may mirror the biochemical-physiological selectivity of biomembranes, signalling pathways and intracellular protein components.

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          Author and article information

          Journal
          Toxicol In Vitro
          Toxicology in vitro : an international journal published in association with BIBRA
          1879-3177
          0887-2333
          Mar 2013
          : 27
          : 2
          Affiliations
          [1 ] Department of Veterinary Medical Sciences, University of Bologna, Italy. alessandra.pagliarani@unibo.it
          Article
          S0887-2333(12)00340-2
          10.1016/j.tiv.2012.12.002
          23232461
          a3d94a39-9d59-46b4-a86d-ca99d8c559f9
          Copyright © 2012 Elsevier Ltd. All rights reserved.
          History

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