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Relative expression of sarco‐endoplasmic reticulum calcium ATPase (SERCA) protein in crayfish, Procambarus clarkii during molting and in response to cold temperature
Author(s) -
Jamal Zeenat,
Gao Yongping,
Wheatly Michele G.
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.1239.19
Subject(s) - serca , procambarus clarkii , endoplasmic reticulum , microbiology and biotechnology , biology , crayfish , cytoplasm , calcium atpase , atpase , biochemistry , enzyme , fishery
Molting is a prerequisite for development and growth in crustaceans and other arthropods. In the past we have used the natural molting cycle as a non‐mammalian model system to study calcium (Ca2+) homeostasis and the genes encoding for the Ca2+ handling proteins. Ca2+ pumps are integral membrane proteins having 1000 amino acid residues and three cytoplasmic domains (ATP‐binding site, phosphorylation site and a transduction domain). In both epithelial and non‐epithelial tissues of Procambarus clarkii, the Ca2+ pumping ATPase of sarcoplasmic reticulum (SERCA) performs the critical function of sequestering Ca2+ from the cytoplasm at the expense of ATP hydrolysis. In this study, we have specifically looked at the expression of mRNA and protein of SERCA in cardiac muscle during the molting cycle and cold acclimation at 4ºC for 3 weeks by using in‐situ hybridization and immunofluorescence. During intermolt and postmolt stages, a dynamic upregulation of SERCA expression was revealed in cardiac tissues as compared with premolt stage. Tissues of animals cold acclimated at 4ºC for 3 weeks also exhibited a significant increase in SERCA expression. These two experimental conditions will be further employed to better examine the mechanisms of regulation of expression of this important Ca2+ sequestration mechanism (Supported by Grant IBN 0445202 to MGW, YG and CMG).