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The biochemistry of Alzheimer's disease, the most common cause of dementia, is not yet very well understood. Alzheimer's disease (AD) has been identified as a proteopathy : a protein misfolding disease due to the accumulation of abnormally folded amyloid beta (Aβ) protein in the brain . [ 1 ]
[260] [261] Alzheimer's disease is known for placing a great burden on caregivers which includes social, psychological, physical, or economic aspects. [23] [262] [263] Home care is usually preferred by both those people with Alzheimer's disease as well as their families. [264]
For the first time, researchers have identified a genetic form of late-in-life Alzheimer’s disease — in people who inherit two copies of a worrisome gene. Scientists have long known a gene ...
It is coded for by the gene APP and regulated by substrate presentation. [10] APP is best known as the precursor molecule whose proteolysis generates amyloid beta (Aβ), a polypeptide containing 37 to 49 amino acid residues, whose amyloid fibrillar form is the primary component of amyloid plaques found in the brains of Alzheimer's disease patients.
The normal function of Aβ is not yet known. [9] Though some animal studies have shown that the absence of Aβ does not lead to any obvious loss of physiological function, [10] [11] several potential activities have been discovered for Aβ, including activation of kinase enzymes, [12] [13] protection against oxidative stress, [14] [15] regulation of cholesterol transport, [16] [17] functioning ...
Alzheimer’s usually is a disease of people over age 65 and while simply getting older is the main risk, the APOE gene has long been known to play some role. It comes in three main varieties.
SORL1 (also known as SORLA, SORLA1, or LR11; SORLA or SORL1 are used, often interchangeably, for the protein product of the SORL1 gene) is a 2214 residue type I transmembrane protein receptor that binds certain peptides and integral membrane protein cargo in the endolysosomal pathway and delivers them for sorting to the retromer multi protein ...
The majority of these cases carry mutant presenilin genes. An important part of the disease process in Alzheimer's disease is the accumulation of Amyloid beta (Aβ) protein. To form Aβ, APP must be cut by two enzymes, beta secretases and gamma secretase. Presenilin is the sub-component of gamma secretase that is responsible for the cutting of APP.
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