CIAPIN1 Human

CIAPIN1 was originally identified as a molecule that conferred resistance to apoptosis induced by growth factor starvation . It is mainly expressed in the cytoplasm of liver, pancreas, and heart tissue cells . The protein is involved in the cytosolic iron-sulfur cluster assembly pathway, which is essential for various cellular processes .

CIAPIN1 functions by inhibiting caspase activity, which is a family of protease enzymes playing essential roles in programmed cell death . This inhibition helps cells to survive under conditions that would normally induce apoptosis. The protein’s expression is reliant on growth factor stimulation, indicating its role in cellular growth and survival .

Mutations or dysregulation of the CIAPIN1 gene have been associated with several diseases, including Amelogenesis Imperfecta, Hypomaturation Type, and Sideroblastic Anemia . The protein’s ability to inhibit apoptosis makes it a potential target for therapeutic interventions in diseases where cell survival is compromised.

Research on CIAPIN1 has shown its potential in regulating apoptosis in both human cell lines and parasitic organisms like Schistosoma japonicum . This makes it a promising candidate for developing treatments for parasitic infections and other conditions involving excessive apoptosis.