CIDEC Human

CIDEC was initially identified due to its upregulation during adipogenesis, the process by which preadipocytes differentiate into adipocytes . The protein is characterized by an N-terminal domain and a C-terminal domain, both essential for its functionality . CIDEC is localized to lipid droplets, where it is required for the formation of unilocular lipid droplets and optimal energy storage .

CIDEC plays a significant role in lipid metabolism. It promotes lipid droplet formation in adipocytes and hepatocytes, thereby controlling lipid storage and metabolism . The protein is also involved in mediating adipocyte apoptosis, a form of programmed cell death . CIDEC’s function is inversely regulated by tumor necrosis factor-alpha (TNF-α) and insulin, aligning with its antilipolytic function .

Research has shown that CIDEC is implicated in various metabolic disorders. For instance, its elevated expression is associated with metabolic disturbances and insulin resistance, which are critical factors in the development of diabetic cardiomyopathy . Gene silencing of CIDEC has been shown to alleviate these conditions by upregulating AMP-activated protein kinase (AMPK) phosphorylation .

Human recombinant CIDEC is produced using recombinant DNA technology, which involves inserting the CIDEC gene into an expression vector and introducing it into a host cell to produce the protein. This recombinant protein is used in various research applications to study its function and role in metabolic processes and diseases.