PKC

PKC or Protein Kinase C is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins, or the members of AGC kinase family related to the second messengers, diacylglycerol and inositol trisphosphate.

Function

Protein Kinase C (PKC) enzymes are vital for several signal transduction cascades. They are known to be activated by signals such as increases in the concentration of diacylglycerol (DAG) or calcium ions (Ca2+). Once activated, PKC enzymes phosphorylate a wide range of protein targets, thereby altering their function.

Isoforms

There are several isoforms of PKC which include:

• PKC alpha
• PKC beta
• PKC gamma
• PKC delta
• PKC epsilon
• PKC zeta
• PKC eta
• PKC theta
• PKC iota
• PKC mu
• PKC nu

Each isoform has a unique structure, tissue distribution, and function.

Role in Disease

PKC has been implicated in a number of diseases including cancer, diabetic complications, and bipolar disorder. In cancer, PKC enzymes have been shown to be involved in growth, survival, and metastasis of tumor cells. In diabetic complications, PKC enzymes have been shown to be activated, leading to vascular complications. In bipolar disorder, some studies have suggested that PKC is overactive, and that its downregulation could help manage this condition.

See Also

• Protein Kinase
• Signal Transduction
• Phosphorylation
• Diacylglycerol
• Inositol Trisphosphate

References

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