FN Archimer Export Format
PT J
TI Evidence in oyster of a plasma extracellular superoxide dismutase which binds LPS
BT 
AF GONZALEZ, Marcelo
   ROMESTAND, Bernard
   FIEVET, Julie
   HUVET, Arnaud
   LEBART, M
   GUEGUEN, Yannick
   BACHERE, Evelyne
AS 1:1,2;2:1,2;3:2;4:2;5:3;6:2;7:2;
FF 1:;2:;3:PDG-DOP-DCM-PM-APOI;4:PDG-DOP-DCB-PFOM-PI;5:;6:PDG-DOP-DCN-AGSAE-GPIA;7:PDG-DOP-DCN-AGSAE-GPIA;
C1 Univ Montpellier 2, CNRS, UMR 5171, UMII,IFREMER, F-34095 Montpellier, France.
   IFREMER, Ctr Brest, UMR Physiol & Ecophysiol Mollusques Marins, F-29280 Plouzane, France.
   EPHE, Univ Montpellier 2, UMR 5539,Lab Motilite Cellulaire, F-34095 Montpellier, France.
C2 UNIV MONTPELLIER, FRANCE
   IFREMER, FRANCE
   EPHE, FRANCE
SI MONTPELLIER
   PALAVAS
   BREST
SE PDG-DOP-DCN-AGSAE-GPIA
   PDG-DOP-DCM-PM-APOI
   PDG-DOP-DCB-PFOM-PI
IN WOS Ifremer jusqu'en 2018
   copubli-univ-france
IF 3
TC 76
UR https://archimer.ifremer.fr/doc/2005/publication-3583.pdf
LA English
DT Article
DE ;Beta integrin;Oxidative burst;Hemocyte;Crassostrea gigas;Invertebrate;Mollusc bivalve
AB We have characterized in the oyster Crassostrea gigas an extracellular superoxide dismutase (Cg-EcSOD) which appears to bind lipopolysaccharides (LPS). The protein has been purified from the oyster plasma and identified as a Cu/ZnSOD according to its N-terminal sequencing and biological activity. Cg-EcSOD expression and synthesis are restricted to hemocytes as revealed by in situ hybridization and immunocytochemistry. Cg-EcSOD-expressing hemocytes were seen in blood circulation, in connective tissues, and closely associated to endothelium blood vessels. Cg-EcSOD presents in its amino acid sequence a LPS-binding motif found in the endotoxin receptor CD14 and we show that the protein displays an affinity to Escherichia coli bacteria and with LPS and Lipid A. Additionally, an RGD motif known to be implicated in the association to membrane integrin receptor is present in the amino acid sequence. The purified Cg-EcSOD was shown to bind to oyster hemocytes and to be immunocolocalized with a beta-integrin-like receptor. (c) 2005 Elsevier Inc. All rights reserved.
PY 2005
PD DEC
SO Biochemical and Biophysical Research Communications
SN 0006-291X
PU Elsevier
VL 338
IS 2
UT 000233451100055
BP 1089
EP 1097
DI 10.1016/j.bbrc.2005.10.075
ID 3583
ER

EF