Calmodulin- a multigene family promoting multitudes of cellular activities

To summarize the importance of calcium as second messenger may not be enough to emphasize. The Ca 2+ signal passing Ca 2+ signaling (such as calmodulin) regulates various important functions in response to intracellular stimulation. Calmodulin is a small, evolutionarily conserved EF hand superfamily Ca 2+ binding protein that is involved in many different cellular pathways by regulating a large number of target sets. Its function has been shown to be highly dependent on how it is distributed throughout the cell and the pool can allow CaM to be activated at the appropriate time and place.

The skeletal muscle fiber phenotype of adult animals is regulated by several independent signal transduction pathways. These include the Ras / mitogen activated protein kinase (MAPK) pathway, calcineurin, calcium / calmodulin dependent protein kinase IV, and peroxisome proliferator - g coactivator - 1 (PGC - 1). It is a method. The Ras / MAPK signaling pathway is associated with motor neurons and signaling systems and promotes a neurodependent induction of slow treatment in regenerating muscles in association with excitation and transcriptional regulation. Calcineurin is a Ca 2+ / calmodulin activated phosphatase involved in fibrous skeletal muscle-dependent neuronal activity, directly regulating the phosphorylation status of the transcription factor NFAT, causing its translocation to the nucleus and delaying retardation Cause it. Activation of muscle proteins complexed with muscle cell enhancer factor 2 (MEF2) protein and other regulatory proteins

Caspase-3 is activated by both endogenous and exogenous apoptotic pathways. Cellular stress induces endogenous apoptosis and results in activation of the Bcl-2 protein family. The BAK and BAX oligomers then promote pore formation in the mitochondrial outer membrane. Release of various interstitial proteins occurs. Cytochrome C binds to apoptosis protease activator 1 (APAF 1) and induces oligomerization of APAF 1 to form apoptotic bodies. Apoptotic bodies mobilize pro-caspase-9, resulting in dimerization and activation of caspase-9. Caspase-9 activation stimulates the caspase cascade and ultimately activates executor caspase-3 and -7. These caspases are involved in the cleavage of many cellular proteins leading to biochemical and morphological markers of apoptosis. Stimulation of the exogenous apoptotic pathway by the ligand binding to the corresponding death receptor and recruitment of FADD to the death receptor

Caspase 3 inhibits diethylnitrosamine-induced hepatocyte death, compensatory proliferation and liver carcinogenesis by inhibiting p38 activation