Scientists have found that a molecular chaperone works to collect and detoxify high levels of Abeta found in Alzheimer's disease.
HspB1, it is known, is a molecular chaperone which is present in Alzheimer’s disease patients, but until a recent study, the role of HspB1 was a mystery.
“What we have found is HspB1 is a protective mechanism that tries to get rid of the toxic oligomers or aggregates of amyloid beta that occur in Alzheimer’s,” reported study author Anil G. Cashikar, M.D., biochemist at Georgia Health Sciences University’s Center for Molecular Chaperones and Radiobiology.
Amyloid beta peptide, or Abeta, is thought to begin the surge of events which leads to brain cell damage and death in Alzheimer’s disease. As levels of Abeta swell, the peptide begins to accumulate in the brain; elevated levels of the peptide in the spinal fluid are a diagnostic marker for Alzheimer’s.
Molecular chaperones such as HspB1 are known to react to the disease-producing misfolded proteins such as Abeta.
Cashikar stated that, even though plaques which are a consequence of the buildup inhabit important areas of the brain, it is still better than toxic Abeta killing neurons. “We think maybe the system gets overwhelmed,” said Cashikar.
According to this study, neurons from HspB1-deficient mice were found to be more responsive to the toxic ravages of Abeta.
“HspB1 is present because its function is to protect cells. The implication is if we can elevate the levels of this molecular chaperone, we may be able to handle the situation a little better,” said Cashikar.
Cashikar reported that his goal is to exploit this natural system by creating a miniature version of the molecular chaperone that could be inserted into the bloodstream in order to consume surplus Abeta from the brain.
“We want to come up with smaller versions of HspB1 that can be put into the bloodstream so you can sop up the material from the brain into the blood where it can be cleared more efficiently,” continued Cashikar. He also expressed his desire to discover a method of increasing the natural production of the protective HspB1.
The study is published in Molecular and Cellular Biology.