This new study reports findings that support the evaluation of a potential new antidepressant agent.
According to the lead author on this study, Kamilla Miskowiak, MSc: “Although depression is often related to problems in the chemistry of the brain, recent evidence also suggests that there may be structural problems as well with nerve cells not being regenerated as fast as normal or suffering from toxic effects of stress and stress hormones.”
This led the researchers to evaluate the effects of erythropoietin (Epo), a hormone naturally produced by the kidneys that stimulates the formation of red blood cells and is known as a treatment for anemia. The authors explain that new evidence shows that Epo also “has neuroprotective and neurotrophic effects in animal models and affects cognitive and associated neural responses in humans,” suggesting that it may be a candidate in the treatment of depression.
In this study, Miskowiak and colleagues evaluated the effects of Epo on the neural and cognitive processing of emotional information in healthy volunteers using functional magnetic resonance imaging (fMRI). They found that Epo regulated the emotional responses of those volunteers that received it, similar to the effects of current antidepressants. Ms. Miskowiak explains that “this finding provides support to the idea that Epo affects neural function and may be a candidate agent for future treatment strategies for depression.”
John H. Krystal, M.D., Editor of Biological Psychiatry and affiliated with both Yale University School of Medicine and the VA Connecticut Healthcare System, confirms its potential: “Epo appears to have neurotrophic effects in the brain in animals. The current data suggest that Epo may modulate human brain activity associated with the processing of emotion.
Together, there may now be sufficient evidence to justify evaluating the antidepressant effects of Epo and related compounds in humans.”
Jayne Dawkins | alfa
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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