Meeting Abstract
We analyzed the proteomic responses of gill tissue of the spider crab (Hyas araneus) and the intertidal porcelain crab (Petrolisthes cinctipes) to simultaneous emersion, pH and temperature stress. Both species showed a decrease in tyrosine metabolism, while simultaneously changing the abundance of lectins and serine proteases, which are thought to lead to the conversion of pro-phenoloxidases (including hemocyanin) to phenoloxidases. These catalyze the synthesis of quinones and melanin from tyrosine. Quinones are involved in the sclerotization of the arthropod cuticle and both species showed abundance changes in a number of cuticle proteins. The porcelain crab also showed changes in the abundance of proteins that are involved in the excretion of ammonium, and thus the excretion of proton equivalents, across the gill tissue. This response to low pH was dependent on the immersion/emersion and temperature conditions animals experienced. Changes in the abundance of proteins involved in the urea cycle might indicate that it too is involved in the excretion of bicarbonate ions and thus protons. Low pH also decreased the abundance of chaperones of the endoplasmic reticulum. In general, crustacean gill tissue changed a number of proteins involved in cuticle structure which may affect the passive ion transport properties of the apical side of the gill epithelium. These changes were accompanied by changes in the active transport of ammonium and the urea cycle (funded by NSF EF-1041227).
