In a cell with defective chaperones, what would happen?

What are the possible consequences in a cell with defective chaperones?

Explanation:

Chaperone proteins are essential for the correct protein folding of proteins. These proteins were originally discovered in bacteria. The chaperones play a crucial role in guiding newly synthesized proteins to fold into their proper three-dimensional structures.

When a cell has defective chaperones, it means that these chaperone proteins are unable to properly assist in protein folding. As a result, misfolded proteins would accumulate within the cell. This is because without functional chaperones, misfolded proteins are not refolded into their correct shapes and thus remain in a non-functional state.

One of the key roles of chaperones is to prevent the aggregation of misfolded proteins, which can be harmful to the cell. Without functional chaperones, the concentration of misfolded proteins would be higher than normal, leading to cellular stress and potential dysfunction.

In humans, Hsp70 is a chaperone protein that is constitutively expressed under stress conditions. It is involved in the folding of protein precursors and the refolding of misfolded proteins. The increased expression level of Hsp70 is associated with various health problems, including neurodegenerative diseases, cerebral ischemia, and epilepsy.