Over het archief
Het OWA, het open archief van het Waterbouwkundig Laboratorium heeft tot doel alle vrij toegankelijke onderzoeksresultaten van dit instituut in digitale vorm aan te bieden. Op die manier wil het de zichtbaarheid, verspreiding en gebruik van deze onderzoeksresultaten, alsook de wetenschappelijke communicatie maximaal bevorderen.
Dit archief wordt uitgebouwd en beheerd volgens de principes van de Open Access Movement, en het daaruit ontstane Open Archives Initiative.
Basisinformatie over ‘Open Access to scholarly information'.
| one publication added to basket [221272] |
Cloning and characterization of Arenicola marina peroxiredoxin 6, an annelid two-cysteine peroxiredoxin highly homologous to mammalian one-cysteine peroxiredoxins
Loumaye, E.; Andersen, A.C.; Clippe, A.; Degand, H.; Dubuisson, M.; Zal, F.; Morsomme, P.; Rees, J.F.; Knoops, B. (2008). Cloning and characterization of Arenicola marina peroxiredoxin 6, an annelid two-cysteine peroxiredoxin highly homologous to mammalian one-cysteine peroxiredoxins. Free Radic. Biol. Med. 45(4): 482-493. http://dx.doi.org/10.1016/j.freeradbiomed.2008.04.033
In: Free Radical Biology and Medicine. Elsevier: New York; Oxford. ISSN 0891-5849; e-ISSN 1873-4596, meer
|  |
| Trefwoorden |
Annelida [WoRMS]; Arenicola marina (Linnaeus, 1758) [WoRMS]
Marien/Kust |
| Author keywords |
Annelid; Arenicola marina; Peroxidase; Peroxiredoxin; Antioxidant |
| Auteurs | | Top |
- Loumaye, E., meer
- Andersen, A.C.
- Clippe, A., meer
|
- Degand, H.
- Dubuisson, M., meer
- Zal, F.
|
- Morsomme, P.
- Rees, J.F., meer
- Knoops, B., meer
|
| Abstract |
Peroxiredoxins (PRDXs) are a superfamily of thiol-dependent peroxidases found in all phyla. PRDXs are mechanistically divided into three subfamilies, namely typical 2-Cys, atypical 2-Cys, and 1-Cys PRDXs. To reduce peroxides, the N-terminal peroxidatic Cys of PRDXs is first oxidized into sulfenic acid. This intermediate is reduced by forming a disulfide bond either with a resolving Cys of another monomeric entity (typical 2-Cys) or of the same molecule (atypical 2-Cys). In 1-Cys PRDXs, the resolving Cys is missing and the sulfenic acid of the peroxidatic Cys is reduced by a heterologous thiol-containing reductant. In search of a homolog of human 1-Cys PRDX6 in Arenicola marina, an annelid worm living in intertidal sediments, we have cloned and characterized a PRDX exhibiting high sequence homology with its mammalian counterpart. However, A. marina PRDX6 possesses five Cys among which two Cys function as peroxidatic and resolving Cys of typical 2-Cys PRDXs. Thus, A. marina PRDX6 belongs to a transient group exhibiting sequence homologies with mammalian 1-Cys PRDX6 but must be mechanistically classified into typical 2-Cys PRDXs. Moreover, PRDX6 is highly expressed in tissues directly exposed to the external environment, suggesting that this PRDX may be of particular importance for protection against exogenous oxidative attacks. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.
