One puzzle in Alzheimers disease (AD) research is why mice engineered to have the abnormal protein underlying the disease in humans show little pathology of the disease. Specifically, such mice are genetically altered to overproduce mutant human amyloid precursor protein (APP). It is this protein that, when clipped by enzymes, produces the amyloid beta (Ab) peptide that clusters into the amyloid plaque that clogs the brain and kills brain cells.
The clipping of APP produces two types of amyloid beta peptide--one 40 amino acid units long (Ab40) and one 42 units long (Ab42). Circumstantial evidence has suggested that Ab42 is the "stickier" of the two forms, and underlies the pathology of the disease.
Now, researchers led by Eileen McGowan and Todd Golde of the Mayo Clinic College of Medicine report in the July 21, 2005, issue of Neuron definitive proof that Ab42 is, indeed, the culprit molecule. In their experiments, they created transgenic mice that overproduced either Ab40 or Ab42 in the absence of overproduction of APP. Thus, they could precisely study the role of each of these molecules in AD pathology.
BigH1 -- The key histone for male fertility
14.12.2017 | Institute for Research in Biomedicine (IRB Barcelona)
Guardians of the Gate
14.12.2017 | Max-Planck-Institut für Biochemie
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