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posted by martyb on Tuesday December 01 2020, @10:31AM   Printer-friendly
from the all-you-need-is-love dept.

'Love hormone' oxytocin could be used to treat cognitive disorders like Alzheimer's:

Alzheimer's disease is a progressive disorder in which the nerve cells (neurons) in a person's brain and the connections among them degenerate slowly, causing severe memory loss, intellectual deficiencies, and deterioration in motor skills and communication. One of the main causes of Alzheimer's is the accumulation of a protein called amyloid β (Aβ) in clusters around neurons in the brain, which hampers their activity and triggers their degeneration.

[...] a team of scientists from Japan, led by Professor Akiyoshi Saitoh from the Tokyo University of Science, has looked at oxytocin, a hormone conventionally known for its role in the female reproductive system and in inducing the feelings of love and well-being. "Oxytocin was recently found to be involved in regulating learning and memory performance, but so far, no previous study deals with the effect of oxytocin on Aβ-induced cognitive impairment," Prof Saitoh says.

[...] Prof Saitoh and team first perfused slices of the mouse hippocampus with Aβ to confirm that Aβ causes the signaling abilities of neurons in the slices to decline or—in other words—impairs their synaptic plasticity. Upon additional perfusion with oxytocin, however, the signaling abilities increased, suggesting that oxytocin can reverse the impairment of synaptic plasticity that Aβ causes.

To find out how oxytocin achieves this, they conducted a further series of experiments. In a normal brain, oxytocin acts by binding with special structures in the membranes of brain cells, called oxytocin receptors. The scientists artificially 'blocked' these receptors in the mouse hippocampus slices to see if oxytocin could reverse Aβ-induced impairment of synaptic plasticity without binding to these receptors. Expectedly, when the receptors were blocked, oxytocin could not reverse the effect of Aβ, which shows that these receptors are essential for oxytocin to act.

Alzheimer's disease.

Journal Reference:
Junpei Takahashi, et al. Oxytocin reverses Aβ-induced impairment of hippocampal synaptic plasticity in mice, Biochemical and Biophysical Research Communications (2020). DOI: 10.1016/j.bbrc.2020.04.046


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  • (Score: 2, Interesting) by Anonymous Coward on Tuesday December 01 2020, @12:32PM (3 children)

    by Anonymous Coward on Tuesday December 01 2020, @12:32PM (#1082792)

    > One of the main causes of Alzheimer's is the accumulation of a protein called amyloid β (Aβ)

    This has been debunked years ago. If a crackhead lives in squalor because they are too high to care about cleaning their place do you blame the trash everywhere for the problem?

    Same thing, unless everything is working perfectly you'll get accumulation of amyloids which are simply the lowest energy structure polypeptides can form. That is why there is no disease shown to not be associated with accumulation of amyloids. Either they have been found in the diseased tissue or no one has looked yet. Zero cases of looking and failing to find them elevated for any disease.

    • (Score: 1, Insightful) by Anonymous Coward on Tuesday December 01 2020, @02:02PM (2 children)

      by Anonymous Coward on Tuesday December 01 2020, @02:02PM (#1082809)

      [citation needed]

      • (Score: 0) by Anonymous Coward on Tuesday December 01 2020, @05:22PM

        by Anonymous Coward on Tuesday December 01 2020, @05:22PM (#1082870)

        I could but usually a waste of time to post that here. "Links and quotes are not evidence I was told"

      • (Score: 0) by Anonymous Coward on Wednesday December 02 2020, @04:12AM

        by Anonymous Coward on Wednesday December 02 2020, @04:12AM (#1083087)

        "From a wide range of in vitro experiments on peptides and proteins we now know that the formation of amyloid structures is not a rare phenomenon associated with a small number of diseases but rather that it reflects a well-defined structural form of the protein that is an alternative to the native state — a form that may in principle be adopted by many, if not all, polypeptide sequences

        [...]

        These observations, therefore, have led to the remarkable conclusion that, at the concentrations present in living systems, the native states may not always represent the absolute free energy minima of the corresponding polypeptide chains — the native form of a protein could in some cases simply be a metastable monomeric (or functionally oligomeric) state that is separated from its polymeric amyloid form by high kinetic barriers"

        http://www.ncbi.nlm.nih.gov/pubmed/24854788 [nih.gov]

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