![]() ![]() Potentially, small molecules that increase Hsc70 levels could be used for treating spinocerebellar ataxia, says Xiao-Jiang Li. To confirm Hsc70’s importance, the researchers showed that boosting cells’ levels of Hsc70 can bolster their ability to cope with misfolded proteins. Li’s team identified a chaperone called Hsc70 whose activity declines with age in the brain, while others’ activity does not. The misfolded proteins are toxic and interfere with the normal forms of the same protein.Ĭhaperones are proteins whose job is to prevent improper liaisons between other proteins they prevent the sticky regions of proteins from grabbing something they’re not supposed to. Scientists led by Shi-Hua Li and Xiao-Jiang Li, both professors of human genetics, devised a system in which production of a misfolding-prone protein that causes a form of spinocerebellar ataxia can be triggered artificially in mice at various ages. The results were published in January in the journal Neuron. ![]() They also identified targets for potential therapies: bolstering levels of either a particular chaperone or a growth factor in brain cells can protect against the toxic effects of misfolded proteins. The scientists were studying a model of spinocerebellar ataxia, but the findings have implications for understanding other diseases, such as Alzheimer’s, Parkinson’s, and Huntington’s. Researchers at the School of Medicine have demonstrated that as animals age, their brains are more vulnerable to misfolded proteins, partly because of a decline in chaperone activity. Chaperones, which assist protein folding, and proteases, which remove misfolded proteins, are among the cellular factors that influence protein folding in. But the word also describes a type of protein that can guard the brain against its own troublemakers: misfolded proteins that are involved in several neurodegenerative diseases. We show that desiccation induces protein misfolding/aggregation of cytoplasmic and membrane proteins using luciferase and prion reporters. Examples for this class include the Hsp70 and. Interestingly, the protein chaperone Hsp104 compensates for loss of trehalose during short-term, but not long-term, desiccation. Most of us think of a chaperone as an adult who keeps teenagers out of trouble at a dance or overnight trip. Foldases are the chaperones that actively refold unfolded proteins, generally with an ATP-dependent mechanism. ![]()
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