.gif "IP Gear")
- Joined
- Jul 16, 2018
- Messages
- 312
Recently a research shows that revealing Viagra's mechanism of treating heart disease by inhibiting protein kinase G
When normal cells grow, split, or perform any other task in the body, they respond to a large number of internal sensors that measure nutrients and energy supplies and tell what is happening outside the cell based on environmental clues. A protein called mTOR receives information from these signals and then instructs the cells to take action. Now, in a new study, researchers from the Johns Hopkins University School of Medicine have discovered a long-held built-in molecular switch that behaves much like a car brake, based on data from cells and mice. --- Slow down the role of mTOR -- and prevent the overworked heart from expanding.
Their findings have had a potential impact on the manipulation of this molecular switch to treat heart disease -- a focus of the study -- diabetes, kidney disease, lung disease, cancer and autoimmune diseases. The results of the study were published online January 30, 2019 in the journal Nature, entitled "PKG1-modified TSC2 regulates mTORC1 activity to counter adverse cardiac stress"
The researchers found that opening protein kinase G blocked mTORC1, and they figured out how this happened. The answer lies in a key regulator of mTORC1 called tuberin (which they call TCS2), which acts like an "antenna" that receives biochemical signals that trigger or prevent cell growth and regulate metabolism.
By using genetic engineering tools in the myocardium and connective tissue cells, these researchers mutated the TCS2 protein, where the mutation occurs where protein kinase G phosphorylates TCS2. These mutations allow cells to behave in one of two ways: one type of mutation has been "increasing" the effect of TCS2, That is to say, raising the mutation, while another type of mutation has essentially "down" it. The effect of lowering the mutation.
In cells with a down-regulated mutation in TCS2, these cells did not change at rest. However, when these researchers treated them with hormones that promote the growth of these cells, mTORC1 was hyperactivated and these cells increased more than cells with normal TCS2. When they studied cells with elevated mutations in TCS2, they found that these cells did not change when the same hormone was added.
Through the research we can know keeping TCS2 "down" is like lifting the foot on the brake pedal, triggering mTORC1 hyperactivation, while in TCS2 "up" cells, The brakes were stepped harder and mTORC1 remained unactive under the action of stimulating hormones.
When normal cells grow, split, or perform any other task in the body, they respond to a large number of internal sensors that measure nutrients and energy supplies and tell what is happening outside the cell based on environmental clues. A protein called mTOR receives information from these signals and then instructs the cells to take action. Now, in a new study, researchers from the Johns Hopkins University School of Medicine have discovered a long-held built-in molecular switch that behaves much like a car brake, based on data from cells and mice. --- Slow down the role of mTOR -- and prevent the overworked heart from expanding.
Their findings have had a potential impact on the manipulation of this molecular switch to treat heart disease -- a focus of the study -- diabetes, kidney disease, lung disease, cancer and autoimmune diseases. The results of the study were published online January 30, 2019 in the journal Nature, entitled "PKG1-modified TSC2 regulates mTORC1 activity to counter adverse cardiac stress"
The researchers found that opening protein kinase G blocked mTORC1, and they figured out how this happened. The answer lies in a key regulator of mTORC1 called tuberin (which they call TCS2), which acts like an "antenna" that receives biochemical signals that trigger or prevent cell growth and regulate metabolism.
By using genetic engineering tools in the myocardium and connective tissue cells, these researchers mutated the TCS2 protein, where the mutation occurs where protein kinase G phosphorylates TCS2. These mutations allow cells to behave in one of two ways: one type of mutation has been "increasing" the effect of TCS2, That is to say, raising the mutation, while another type of mutation has essentially "down" it. The effect of lowering the mutation.
In cells with a down-regulated mutation in TCS2, these cells did not change at rest. However, when these researchers treated them with hormones that promote the growth of these cells, mTORC1 was hyperactivated and these cells increased more than cells with normal TCS2. When they studied cells with elevated mutations in TCS2, they found that these cells did not change when the same hormone was added.
Through the research we can know keeping TCS2 "down" is like lifting the foot on the brake pedal, triggering mTORC1 hyperactivation, while in TCS2 "up" cells, The brakes were stepped harder and mTORC1 remained unactive under the action of stimulating hormones.
