FN Archimer Export Format
PT J
TI Penaeidins, antimicrobial peptides with chitin-binding activity, are produced and stored in shrimp granulocytes and released after microbial challenge
BT 
AF DESTOUMIEUX-GARZON, Delphine
   MUNOZ, Marcello
   COSSEAU, Céline
   RODRIGUEZ, Jenny
   BULET, Philippe
   COMPS, Marie-Annick
   BACHERE, Evelyne
AS 1:;2:;3:;4:;5:;6:;7:;
FF 1:;2:PDG-DRV-RA-DRIM;3:;4:;5:;6:PDG-DEL-ST;7:PDG-DRV-RA-DRIM;
C1 Univ Montpellier 2, IFREMER, JCSCNRS, UMR 219, F-34095 Montpellier, France.
   CNRS, UPR 9022, Inst Biol Mol & Cellulaire, F-67084 Strasbourg, France.
   Escuela Super Politecn Litoral, Ctr Nacl Acuicultura & Invest Marinas, Guayaquil, Ecuador.
   IFREMER, F-34230 Palavas Les Flots, France.
C2 UNIV MONTPELLIER 2, FRANCE
   CNRS, FRANCE
   ESCUELA SUPER POLITECN LITORAL, ECUADOR
   IFREMER, FRANCE
SI MONTPELLIER
   SETE
SE PDG-DRV-RA-DRIM
   PDG-DEL-ST
IN WOS Ifremer jusqu'en 2018
   copubli-univ-france
IF 5.996
TC 202
UR https://archimer.ifremer.fr/doc/2000/publication-412.pdf
LA English
DT Article
DE ;Crustacean immunity;Penaeid shrimp;Haemocyte;Chitin binding;Antimicrobial peptide
AB Penaeidins are members of a new family of antimicrobial peptides isolated from a crustacean, which present both Gram-positive antibacterial and antifungal activities. We have studied the localization of synthesis and storage of penaeidins in the shrimp Penaeus vannamei. The distribution of penaeidin transcripts and peptides in various tissues reveals that penaeidins are constitutively synthesized and stored in the shrimp haemocytes. It was shown by immunocytochemistry, at both optical and ultrastructural levels, that the peptides are localized in granulocyte cytoplasmic granules, The expression and localization of penaeidins were further analysed in shrimp subjected to microbial challenge. We found that (1) penaeidin mRNA levels decrease in circulating haemocytes in the first 3 hours following stimulation and (2) an increase in plasma penaeidin concentration occurs after microbial challenge, together with (3) a penaeidin immunoreactivity in cuticular tissue, which can be related to the chitin-binding activity we demonstrate here for penaeidins.
PY 2000
PD FEB
SO Journal of Cell Science
SN 0021-9533
PU Company of Biologists
VL 113
IS 3
UT 000085540600015
BP 461
EP 469
ID 412
ER

EF