Epithelial Transport Physiology 2009
DOI: 10.1007/978-1-60327-229-2_3
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Heavy Metal Transport and Detoxification by Crustacean Epithelial Lysosomes

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Cited by 4 publications
(6 citation statements)
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“…Toxic metals interact with binding sites of membrane transport proteins and by this way are able to gain access to the intracellular compartments where they are a danger to normal biochemical and physiological functions (Ahearn et al, 2010; Wood, 2012). …”
Section: Branchial Transport and Bioaccumulation Of Toxic Metalsmentioning
confidence: 99%
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“…Toxic metals interact with binding sites of membrane transport proteins and by this way are able to gain access to the intracellular compartments where they are a danger to normal biochemical and physiological functions (Ahearn et al, 2010; Wood, 2012). …”
Section: Branchial Transport and Bioaccumulation Of Toxic Metalsmentioning
confidence: 99%
“…Hypothetical entry of toxic metals across the gill epithelium of marine and estuarine crustaceans is presented by a model based on ionic mimicry (Figures 10 and 11 ). Toxic metals interact with binding sites of membrane transport proteins and by this way are able to gain access to the intracellular compartments where they are a danger to normal biochemical and physiological functions (Ahearn et al, 2010 ; Wood, 2012 ).…”
Section: Branchial Transport and Bioaccumulation Of Toxic Metalsmentioning
confidence: 99%
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“…Among these candidates, we found amiloride‐sensitive sodium channels, membrane ATPases and ABC and dicarboxylate transporters. These proteins are either antiporters for metal cations or are involved in cellular mechanisms for heavy metal vacuolar sequestration (Ahearn, Sterling, Mandal, & Roggenbeck, ) or in cellular metal homeostasis and detoxification (e.g., Lee, Yang, Zhitnitsky, Lewinson, & Rees, ; Sooksa‐Nguan et al, ). Another set of interesting candidates are the proteins annotated as syntaxin‐5‐like proteins with a SNARE domain, which are involved in vesicle tethering and fusion associated with copper ion homeostasis (Norgate et al, ) and, in addition to being significantly overexpressed in both specialists, also show signals of positive selection in D. tilosensis .…”
Section: Discussionmentioning
confidence: 99%
“…Among these candidates, we found amiloride-sensitive sodium channels, membrane ATPases and ABC and dicarboxylate transporters. These proteins are either antiporters for metal cations or are involved in cellular mechanisms for heavy metal vacuolar sequestration (Ahearn, Sterling, Mandal, & Roggenbeck, 2010) (Norgate et al, 2010) and, in addition to being significantly overexpressed in both specialists, also show signals of positive selection in D. tilosensis.…”
Section: Genetic Changes Matching Phenotypic Convergence: Metal-indmentioning
confidence: 99%