caa a22 4500 467911819 CHVBK 20180406152851.0 cr unu---uuuuu 170328e20060801xx s 000 0 eng 10.1007/s11157-006-0013-0 doi (NATIONALLICENCE)springer-10.1007/s11157-006-0013-0 Metal detoxification and homeostasis in Antarctic Notothenioids. A comparative survey on evolution, expression and functional properties of fish and mammal metallothioneins [Elektronische Daten] [Clemente Capasso, Vincenzo Carginale, Marilisa Riggio, Rosaria Scudiero, Piero Temussi, Francesca Trinchella, Elio Parisi] Organisms from yeast to mammals contain cysteine-rich, heavy metal binding proteins termed metallothioneins. The putative roles of these proteins are trace metal homeostasis and detoxification of poisonous heavy metals. The highly conserved chemical composition and the structural constraints led to the conclusion that metallothioneins of different origin must display remarkably similar features. The present review aims at surveying the studies carried out on the metallothioneins of Antarctic Notothenioidei, a dominating fish group endowed of a number of striking adaptive characters, including reduced (or absent) hematocrit and presence of antifreeze glycoproteins. Given the unique peculiarities of the Antarctic environment, a comparative study of the features of notothenioid metallothioneins could provide new insights into the role of these proteins in physiology and toxicology. The results summarized here show that the metallothioneins of this fish group display a number of features at the level of evolution, expression pattern, structure and function remarkably different from those of mammal metallothioneins. Springer Science+Business Media B.V., 2006 Antarctic fish nationallicence Evolution nationallicence Function nationallicence Mammals nationallicence Metallothionein nationallicence Structure nationallicence Capasso Clemente CNR Institute of Protein Biochemistry, Via Pietro Castellino 111, 80131, Napoli, Italy aut Carginale Vincenzo CNR Institute of Protein Biochemistry, Via Pietro Castellino 111, 80131, Napoli, Italy aut Riggio Marilisa Department of Biological Sciences, University Federico II, Napoli, Italy aut Scudiero Rosaria Department of Biological Sciences, University Federico II, Napoli, Italy aut Temussi Piero National Institue for Medical Research, London, UK aut Trinchella Francesca Department of Biological Sciences, University Federico II, Napoli, Italy aut Parisi Elio CNR Institute of Protein Biochemistry, Via Pietro Castellino 111, 80131, Napoli, Italy aut Reviews in Environmental Science and Bio/Technology Kluwer Academic Publishers 5/2-3(2006-08-01), 253-267 1569-1705 5:2-3<253 2006 5 11157 https://doi.org/10.1007/s11157-006-0013-0 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11157-006-0013-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Capasso Clemente CNR Institute of Protein Biochemistry, Via Pietro Castellino 111, 80131, Napoli, Italy aut NATIONALLICENCE 700 1- Carginale Vincenzo CNR Institute of Protein Biochemistry, Via Pietro Castellino 111, 80131, Napoli, Italy aut NATIONALLICENCE 700 1- Riggio Marilisa Department of Biological Sciences, University Federico II, Napoli, Italy aut NATIONALLICENCE 700 1- Scudiero Rosaria Department of Biological Sciences, University Federico II, Napoli, Italy aut NATIONALLICENCE 700 1- Temussi Piero National Institue for Medical Research, London, UK aut NATIONALLICENCE 700 1- Trinchella Francesca Department of Biological Sciences, University Federico II, Napoli, Italy aut NATIONALLICENCE 700 1- Parisi Elio CNR Institute of Protein Biochemistry, Via Pietro Castellino 111, 80131, Napoli, Italy aut NATIONALLICENCE 773 0- Reviews in Environmental Science and Bio/Technology Kluwer Academic Publishers 5/2-3(2006-08-01), 253-267 1569-1705 5:2-3<253 2006 5 11157 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer