FN Archimer Export Format
PT J
TI HSP70 from the Antarctic sea urchin Sterechinus neumayeri: molecular characterization and expression in response to heat stress
BT 
AF GONZALEZ-ARAVENA, Marcelo
   CALFIO, Camila
   MERCADO, Luis
   MORALES-LANGE, Byron
   BETHKE, Jorn
   DE LORGERIL, Julien
   CARDENAS, Cesar A.
AS 1:1;2:1;3:2;4:2;5:2;6:3;7:1;
FF 1:;2:;3:;4:;5:;6:PDG-RBE-IHPE;7:;
C1 Inst Antartico Chileno, Dept Cient, Lab Biorrecursos Antarticos, Plaza Munoz Gamero 1055, Punta Arenas, Chile.
   Pontificia Univ Catolica Valparaiso, Lab Genet & Inmunol Mol, Grp Marcadores Inmunol, Inst Biol, Ave Univ 330, Valparaiso, Chile.
   Univ Perpignan, IFREMER, Univ Montpellier 2, CNRS,UMR IHPE 5244, Via Domitia,Pl Eugene Bataillon CC80, F-34095 Montpellier, France.
C2 INACH, CHILE
   UNIV PONTIFICIA CATOLICA VALPARAISO, CHILE
   IFREMER, FRANCE
SI MONTPELLIER
SE PDG-RBE-IHPE
UM IHPE
IN WOS Ifremer jusqu'en 2018
   DOAJ
   copubli-int-hors-europe
IF 2.482
TC 19
UR https://archimer.ifremer.fr/doc/00435/54619/56019.pdf
LA English
DT Article
DE ;Hsp70;Coelomocytes;Antarctica;Echinoderms;Climate change
AB Background Heat stress proteins are implicated in stabilizing and refolding denatured proteins in vertebrates and invertebrates. Members of the Hsp70 gene family comprise the cognate heat shock protein (Hsc70) and inducible heat shock protein (Hsp70). However, the cDNA sequence and the expression of Hsp70 in the Antarctic sea urchin are unknown. Methods We amplified and cloned a transcript sequence of 1991 bp from the Antarctic sea urchin Sterechinus neumayeri, experimentally exposed to heat stress (5  and 10 °C for 1, 24 and 48 h). RACE-PCR and qPCR were employed to determine Hsp70 gene expression, while western blot and ELISA methods were used to determine protein expression. Results The sequence obtained from S. neumayeri showed high identity with Hsp70 members. Several Hsp70 family features were identified in the deduced amino acid sequence and they indicate that the isolated Hsp70 is related to the cognate heat shock protein type. The corresponding 70 kDa protein, called Sn-Hsp70, was immune detected in the coelomocytes and the digestive tract of S. neumayeri using a monospecific polyclonal antibody. We showed that S. neumayeri do not respond to acute heat stress by up-regulation of Sn-Hsp70 at transcript and protein level. Furthermore, the Sn-Hsp70 protein expression was not induced in the digestive tract. Conclusions Our results provide the first molecular evidence that Sn-Hsp70 is expressed constitutively and is non-induced by heat stress in S. neumayeri. 
PY 2018
PD MAR
SO Biological Research
SN 0716-9760
PU Soc Biolgia Chile
VL 51
UT 000430746500001
DI 10.1186/s40659-018-0156-9
ID 54619
ER

EF