Alzheimer's pathology explored

Article Abstract:

Researchers who study Alzheimer's disease, a progressive condition leading to complete cognitive loss, have recently become interested in the role of a protein called beta-amyloid. The presence of beta-amyloid in the plaques (abnormal structures in the affected brain regions) that are characteristic of the disorder, has long been known. What remains to be determined is whether beta-amyloid is a cause or an effect of Alzheimer's disease. A report is provided of a recent conference on neurological diseases at which the issue was discussed. Interest in beta-amyloid intensified among Alzheimer's disease researchers in 1987, when the gene suspected of causing early-onset Alzheimer's (as distinct from the kind that begins in the seventh or eighth decade of life) seemed likely to be the beta-amyloid gene. However, the amyloid gene was found to lie far away from the Alzheimer's locus (although both are on chromosome 21). The amyloid protein is part of a larger molecule, amyloid precursor protein (APP). Two forms of APP are made by cells, including nerve cells (neurons): a short form, and a longer form containing an inserted segment of amino acids. The insert has a structure that suggests it could inhibit proteases (enzymes that cut proteins), and additional research showed that APP is located in cell membranes in such a manner that it can secrete molecules that contain the insert. The molecule containing the protease inhibitor is identical to a known protease inhibitor, protein nexin II. APP appears to play roles in wound healing and in the activity of growth factors. But what about Alzheimer's disease? It seems that the secreted form of APP does not produce beta-amyloid in the plaques, and skeptics can point to a host of other factors that could cause the pathophysiology of Alzheimer's. On the other hand, APP may play a role in the formation of neuronal connections in the nervous system, a role that is disrupted in the disease. Two lines of thought about how abnormal APP processing might occur are described. To better explore the role of APP in Alzheimer's patients, new ideas and better animal models are needed. The latter topic is discussed in a related article in the August 31, 1990 issue of Science magazine. (Consumer Summary produced by Reliance Medical Information, Inc.)

Health aspects, Protein metabolism disorders

---

Alzheimer's pathology begins to yield its secrets

Article Abstract:

Two research teams have uncovered evidence that suggests that some Alzheimer's patients develop the disease because a mutation in the gene for beta-amyloid causes them to make much larger quantities of the protein than they need.

Research, Genetic aspects, Nerve proteins, Nerve tissue proteins

---

Medicine: a signal contribution to cell biology

Article Abstract:

Edmond Fischer and Edwin Krebs won the 1992 Nobel Prize for their work demonstrating how phosphate addition and removal control enzyme activity. Work on glycogen metabolism has won a series of Nobel Prizes since the 1940s.

Achievements and awards, Nobel prizes, Biochemists, 1992 AD, Fischer, Edmond, Krebs, Edwin

Similar abstracts:

• Abstracts: NGF and Alzheimer's: hopes and fears. The T cell receptor begins to reveal its many facets. Searching for drugs that combat Alzheimer's
• Abstracts: Medicine from plants. Pathological growth of regulations. Pharmaceuticals based on biotechnology
• Abstracts: Does a retrovirus explain fatigue syndrome puzzle? Dallas AIDS survey raises expectations
• Abstracts: The calcium channel blocker nifedipine attenuates slow excitatory amino acid neurotoxicity. HIV-1 coat protein neurotoxicity prevented by calcium channel antagonists

This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.