FN Archimer Export Format
PT J
TI Differential protein expression during sperm maturation and capacitation in an hermaphroditic bivalve,     Pecten maximus     (Linnaeus, 1758)
BT 
AF BOONMEE, A.
   BERTHELIN, C. Heude
   KINGTONG, S.
   PAULETTO, M.
   BERNAY, B.
   ADELINE, B.
   SUQUET, Marc
   SOURDAINE, P.
   KELLNER, K.
AS 1:1;2:2,3,4;3:5;4:6;5:2,7;6:2,3,4;7:8;8:2,3,4;9:2,3,4;
FF 1:;2:;3:;4:;5:;6:;7:PDG-RBE-PFOM-PI;8:;9:;
C1 Rambhai Barni Rajabhat Univ, Fac Sci & Technol, Dept Chem, Chanthaburi 22000, Thailand.
   Normandie Univ, F-14032 Caen, France.
   Univ Caen Normandie, IBFA, F-14032 Caen, France.
   Univ Caen Normandie, UMR BOREA Biol Organismes & Ecosyst Aquat, CNRS 7208, MNHN,UPMC,UCN,UA,IRD 207, F-14032 Caen, France.
   Burapha Univ, Dept Biol, Fac Sci, Chon Buri 20131, Thailand.
   Univ Padua, Dept Comparat Biomed & Food Sci, Viale Univ 16, I-35020 Legnaro, PD, Italy.
   Univ Caen Normandie, Proteogen Platform SFR ICORE, F-14032 Caen, France.
   Ifremer, UMR 6539, PFOM Dept, Stn Expt Argenton, F-29840 Argenton, France.
C2 UNIV RAMBHAI BARNI RAJABHAT, THAILAND
   UNIV CAEN NORMANDIE, FRANCE
   UNIV CAEN NORMANDIE, FRANCE
   UNIV CAEN NORMANDIE, FRANCE
   UNIV BURAPHA, THAILAND
   UNIV PADUA, ITALY
   UNIV CAEN NORMANDIE, FRANCE
   IFREMER, FRANCE
SI ARGENTON
SE PDG-RBE-PFOM-PI
UM LEMAR
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-europe
   copubli-univ-france
   copubli-int-hors-europe
   copubli-sud
IF 1.25
TC 4
UR https://archimer.ifremer.fr/doc/00353/46386/47178.pdf
LA English
DT Article
AB In order to investigate the mechanisms of final maturation and capacitation of spermatozoa in Pecten maximus, we used a 2D proteomic approach coupled with MALDI-TOF/TOF mass spectrometry (MS) and bioinformatics search against the Pecten database, to set up a reference map of the proteome of spawned spermatozoa, and identified 133 proteins on the basis of the EST database. These proteins are mainly involved in energy production, ion and electron transport (44%), cell movement (22%) and developmental processes (10%). Comparison between proteomes of spermatozoa collected before and after transit through the genital ducts of P. maximus led to the identification of differentially expressed proteins. Most of them are associated with energy metabolism (aconitate hydratase, malate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase), indicating important modifications of energy production during transit in gonoducts, potentially linked with acquisition of sperm motility. Three proteins involved in cell movement (Tektin-2, tubulin and microtubule-associated protein RP/EB family member 3) were down-regulated in spermatozoa stripped from the gonad. 40S ribosomal protein SA, involved in maturation of 40S ribosomal subunits, was also found to be down-regulated in spermatozoa obtained by induced spawning, suggesting reduction of the efficiency of RNA translation, a characteristic of late spermatozoon differentiation. These results confirm that maturation processes of P. maximus spermatozoa during transit through the gonoduct involve RNA translation, energy metabolism and structural proteins implicated in cell movement. Spermatozoa maturation processes clearly differ between P. maximus and gonochoric or alternately hermaphroditic bivalves, potentially in relation to reproductive strategies: the final maturation of the spermatozoon along the genital tract probably contributes to reduction of autofertilization in this simultaneously hermaphroditic species.
PY 2016
PD NOV
SO Journal Of Molluscan Studies
SN 0260-1230
PU Oxford Univ Press
VL 82
IS 4
UT 000386901500011
BP 575
EP 584
DI 10.1093/mollus/eyw028
ID 46386
ER

EF