Cloning and characterization of a calmodulin gene (CaM) in crayfish Procambarus clarkii and expression during molting.

Calmodulin (CaM) is a highly conserved calcium (Ca(2+)) binding protein that transduces Ca(2+) signals into downstream effects influencing a range of cellular processes, including Ca(2+) homeostasis. The present study explores CaM expression when Ca(2+) homeostasis is challenged during the mineralization cycle of the freshwater crayfish (Procambarus clarkii). In this paper we report the cloning of a CaM gene from axial abdominal crayfish muscle (referred to as pcCaM). The pcCaM mRNA is ubiquitously expressed but is far more abundant in excitable tissue (muscle, nerve) than in any epithelia (gill, antennal gland, digestive) suggesting that it plays a greater role in the biology of excitation than in epithelial ion transport. In muscle cells the pcCaM was colocalized on the plasma membrane with the Ca(2+) ATPase (PMCA) known to regulate intracellular Ca(2+) through basolateral efflux. While PMCA exhibits a greater upregulation in epithelia (than in non-epithelial tissues) during molting stages requiring transcellular Ca(2+) flux (pre- and postmolt compared with intermolt), expression of pcCaM exhibited a uniform increase in epithelial and non-epithelial tissues alike. The common increase in expression of CaM in all tissues during pre- and postmolt stages (compared with intermolt) suggests that the upregulation is systemically (hormonally) mediated. Colocalization of CaM with PMCA confirms physiological findings that their regulation is linked.