Protein kinases are enzymes that modify other proteins by adding phosphate groups to them (phosphorylation), changing their function radically. About thirty percent of proteins can be modified by kinases.
Disregulated kinase activity is the root cause of many disease, especially cancers, as kinases regulate many aspects of cell growth, movement, and apoptosis. Kinase-inhibiting drugs are being developed to treat several diseases.
Kinases are stress-activated when specific events such as DNA damage or an overload of Ca2+ ions is detected. There are also kinases that are activated only by stress, referred to as c-Jun N-terminal kinases, or JNKs. These stress activated protein kinases respond to stress stimuli like cytokines, ultrafiolet radiation, heat schock, and osmotic shock. They're also involved in cell differentiation and apoptosis.
Because of this dual role in stress and cell death and differentiation, repeated stress activation of JNKs may be one of the triggers of certain types of cancer. In particular, they've been implicated in breast cancer and in some melanomas. But in addition to contributing to pre-tumorous conditions, due to their role in apoptosis they also may be the answer to eliminating cancer as well.
Web Resources On Stress-Activated Kinases
Effects of exercise on mitogen- and stress-activated kinase signal transduction in human skeletal muscle.
ROS, stress-activated kinases and stress signaling in cancer
Book Resources On Stress-Activated Kinases
Protein kinase C epsilon negatively regulates stress fiber formation in transformed cells by Yingxin Li
Stress Testing : Principles and Practice by Myrvin H. Ellestad