Effects of elevated carbon dioxide on contraction force and proteome composition of sea urchin tube feet

Abstract

This study examined how contraction force and protein profiles of the tube feet of the sea urchin (Pseudocentrotus depressus) were affected when acclimated to 400 (control), 2000 and 10,000μatm CO for 48days. Acclimation to higher CO conditions significantly reduced contraction force of the tube feet. Two-dimensional gel electrophoresis showed that eight spots changed in protein volume: six up-regulated and two down-regulated. Using matrix-assisted laser desorption/ionization-quadrupole ion trap-time of flight mass spectrometry, three up-regulated spots (tubulin beta chain, tropomyosin fragment, and actin N-terminal fragment) and two down-regulated spots (actin C-terminal fragment and myosin light chain) were identified. One possible interpretation of the results is that elevated CO weakened contraction of the tube feet muscle through an alteration of proteome composition, mainly associated with post-translational processing/proteolysis of muscle-related proteins.

A Survey on Tubulin and Arginine Methyltransferase Families Sheds Light on P. lividus Embryo as Model System for Antiproliferative Drug Development

“…P. lividus embryo is a widely recognized model for several research programs spanning from cell proliferation assays [100] and differentiation patterns to toxicological studies [56,57,61,101,102,103,104,105,106,107,108], and also in poor-resource settings. Moreover, the sea urchin embryo has been also intensively used in order to select antimitotic compounds (and glean insights into the biological mechanism) from libraries of 1,3,4-oxadiazole derivatives [43], combretastatin derivatives [44,45] and analogues [109,110] and also 3-amino-thieno[2,3-b]pyridines [111].…”