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Calcium absorption in the fluted giant clam, Tridacna squamosa, may involve a homolog of voltage-gated calcium channel subunit α1 (CACNA1) that has an apical localization and displays light-enhanced protein expression in the ctenidium.

J Comp Physiol B. 2019; 
Cao-Pham AH, Hiong KC, Boo MV, Choo CYL, Wong WP, Chew SF, Ip YK,.
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Peptide Synthesis … Separately, a peptide competition assay was performed to determine the specificity of the custom-made anti-CACNA1 antibody The anti-CACNA1 antibody was incubated with the immunizing peptide (GenScript) for 1 h prior to immunoblotting Immunofluorescence microscopy … Get A Quote

摘要

In light, giant clams can increase rates of shell formation and growth due to their symbiotic relationship with phototrophic zooxanthellae residing extracellularly in a tubular system. Light-enhanced shell formation necessitates increase in the uptake of Ca2+ from the ambient seawater and the supply of Ca2+ through the hemolymph to the extrapallial fluid, where calcification occurs. In this study, the complete coding cDNA sequence of a homolog of voltage-gated calcium channel subunit α1 (CACNA1), which is the pore-forming subunit of L-type voltage-gated calcium channels (VGCCs), was obtained from the ctenidium (gill) of the giant clam, Tridacna squamosa. It consisted of 6081 bp and encoded a 223 kDa polypept... More

关键词

Bicarbonate; Calcification; Shell formation; Symbiodinium; Zooxanthellae