(Los Angeles) Ivory Weatherall of Hancock Park has been missing since Thursday morning. Kent Shocknek reports.
(Miami) If someone you love is suffering from Alzheimer`s you might think differently when you see a fish. Researchers racing to find a treatment think a compound in fish may hold some promise.
(Baltimore) Another study finds a diet rich in fish, fruits and vegetables reduces the risk of dementia and Alzheimer`s. Kellye Lynn reports.
Biochemistry of Alzheimer's disease
From Wikipedia, the free encyclopedia
The biochemistry of Alzheimer's disease (AD), one of the most common causes of adult dementia, is as yet not well understood at the molecular level. It has been identified as a protein misfolding disease due to the accumulation of abnormally folded amyloid beta protein in the brains of AD patients.[1] Amyloid beta, also written A², is a short peptide that is an abnormal proteolytic byproduct of the transmembrane protein amyloid precursor protein (APP), whose function is unclear but thought to be involved in neuronal development.[2] The presenilins are components of proteolytic complex involved in APP processing and degradation.[3]
Amyloid beta monomers are soluble and contain short regions of beta sheet and polyproline II helix secondary structures in solution,[4] though they are largely alpha helical in membranes;[5] however, at sufficiently high concentration, they undergo a dramatic conformational change to form a beta sheet-rich tertiary structure that aggregates to form amyloid fibrils.[6] These fibrils deposit outside neurons in dense formations known as senile plaques or neuritic plaques, in less dense aggregates as diffuse plaques, and sometimes in the walls of small blood vessels in the brain in a process called amyloid angiopathy or congophilic angiopathy.
AD is also considered a tauopathy due to abnormal aggregation of the tau protein, a microtubule-associated protein expressed in neurons that normally acts to stabilize microtubules in the cell cytoskeleton. Like most microtubule-associated proteins, tau is normally regulated by phosphorylation; however, in AD patients, hyperphosphorylated tau accumulates as paired helical filaments[7] that in turn aggregate into masses inside nerve cell bodies known as neurofibrillary tangles and as dystrophic neurites associated with amyloid plaques. Although little is known about the process of filament assembly, it has recently been shown that a depletion of a prolyl isomerase protein in the parvulin family accelerates the accumulation of abnormal tau. [8][9]
