 |
|
Researchers get closer to preventing Alzheimer's disease
July 06, 2006A recent study directed by Mount Sinai School of Medicine identifies a faulty molecule in the brain found in cases of mild cognitive impairment (MCI). Researchers say this faulty molecule may be responsible for the progression of MCI to mild Alzheimer's disease (AD) dementia. The study, which appeared June 10th online in the journal Neurobiology of Aging, may lead to preventative treatments for AD.
An estimated 4.5 million Americans have Alzheimer's disease and presently there are no known cures or effective preventive strategies.
"Alzheimer's Disease is a growing health concern that affects millions of people, "says Giulio Maria Pasinetti, M.D., Ph.D., Professor of Psychiatry and Neuroscience, Director of the Neuroinflammation Research Center at Mount Sinai School of Medicine and lead author of the study. "We hope our research provides direction for preventative treatments to delay the onset of AD dementia by eliminating amyloid plaque-causing peptides in the brain."
People with AD exhibit elevated levels of beta-amyloid peptides that cause plaque buildup in the brain (the main characteristic of AD). In the earliest stages of Alzheimer's, beta-amyloid peptides are on the rise, especially in the two connected brain regions critical for memory functions— the hippocampus and entorhinal cortex.
In this study, Dr. Pasinetti and colleagues at Mount Sinai School of Medicine in New York suggests one reason for that early increase of beta-amyloid peptides: an enzyme that breaks down beta-amyloid peptides, also referred to as an insulin-degrading enzyme (IDE), is not active in the brain in the cases at high-risk for developing AD. To assess possible changes in IDE during MCI, the investigators measured protein levels and enzymatic activity in postmortem brain tissue from 46 elderly subjects.
Implications
A loss of IDE activity has been previously shown to occur in severe AD dementia, and the current results raise the possibility that a deficit in degradation of amyloid peptides from IDE could raise levels of toxic beta-amyloid peptides even before AD dementia is diagnosed. If these results are confirmed, Mount Sinai researchers suggest that boosting IDE activity pharmacologically may reverse beta-amyloid peptide accumulation. This new finding may provide a pharmacological therapeutic angle to preventing AD dementia.
Dr. Pasinetti and colleagues also measured levels of beta-amyloid peptides in the entorhinal cortex and found that the amount of beta-amyloid was inversely correlated with IDE activity they measured in the hippocampus. These results support the idea that alterations in IDE might be causally related to beta-amyloid peptides accumulation, starting in the earliest stages of AD.
The Mount Sinai Hospital / Mount Sinai School of Medicine
People with AD exhibit elevated levels of beta-amyloid peptides that cause plaque buildup in the brain (the main characteristic of AD). In the earliest stages of Alzheimer's, beta-amyloid peptides are on the rise, especially in the two connected brain regions critical for memory functions— the hippocampus and entorhinal cortex.
In this study, Dr. Pasinetti and colleagues at Mount Sinai School of Medicine in New York suggests one reason for that early increase of beta-amyloid peptides: an enzyme that breaks down beta-amyloid peptides, also referred to as an insulin-degrading enzyme (IDE), is not active in the brain in the cases at high-risk for developing AD. To assess possible changes in IDE during MCI, the investigators measured protein levels and enzymatic activity in postmortem brain tissue from 46 elderly subjects.
Implications
A loss of IDE activity has been previously shown to occur in severe AD dementia, and the current results raise the possibility that a deficit in degradation of amyloid peptides from IDE could raise levels of toxic beta-amyloid peptides even before AD dementia is diagnosed. If these results are confirmed, Mount Sinai researchers suggest that boosting IDE activity pharmacologically may reverse beta-amyloid peptide accumulation. This new finding may provide a pharmacological therapeutic angle to preventing AD dementia.
Dr. Pasinetti and colleagues also measured levels of beta-amyloid peptides in the entorhinal cortex and found that the amount of beta-amyloid was inversely correlated with IDE activity they measured in the hippocampus. These results support the idea that alterations in IDE might be causally related to beta-amyloid peptides accumulation, starting in the earliest stages of AD.
The Mount Sinai Hospital / Mount Sinai School of Medicine
A 'grape' future for Alzheimer's disease research
With National Alzheimer's Awareness Month upon us, attention continues to focus on new approaches to cognitive health in an aging population.
U.Va. Scientists Identify 'Missing Link' in Process Leading to Alzheimer's Disease
Scientists at the University of Virginia have identified what appears to be a major missing link in the process that destroys nerve cells in Alzheimer's disease, an incurable disease that slowly destroys memory and cognitive abilities.
Cabernet sauvignon red wine reduces the risk of Alzheimer's disease
A new study directed by Mount Sinai School of Medicine has found that moderate red wine consumption in a form of Cabernet Sauvignon may help reduce the incidence of Alzheimer's Disease (AD).
Calorie restriction may prevent Alzheimer's through promotion of longevity program in the brain
A recent study directed by Mount Sinai School of Medicine suggests that experimental dietary regimens might calm or even reverse symptoms of Alzheimer's Disease (AD).
More Beta-amyloid Peptides Current Events and Beta-amyloid Peptides News Articles
|
Beta amyloid: the peptide that kills from both the outside and inside to produce Alzheimer's disease. (Collegiate Communications--Undergraduate).(Brief ... of the North Dakota Academy of Science by Jason Spah (Author), Katherine Splichal (Author), Kali Wilson (Author), Garl K. Rieke (Author) This digital document is an article from Proceedings of the North Dakota Academy of Science, published by North Dakota Academy of Science on April 1, 2000. The length of the article is 897 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available in your Amazon.com Digital Locker immediately after purchase. You can view it with any web browser. Citation Details Title: Beta amyloid: the peptide that kills from both the outside and inside to produce Alzheimer's disease. (Collegiate Communications--Undergraduate).(Brief Article) Author: Jason Spah Publication: Proceedings of the North Dakota Academy of Science (Refereed) Date: April 1, 2000 Publisher: North Dakota Academy of Science Page:... | |
![[beta]-amyloid Peptide (1-42), Human, Oncogene - Size 250 Ug - Model Pp69--25mg - Each (.25 Mg)](http://ecx.images-amazon.com/images/I/31Y1NF0J0EL._SL160_.gif) |
[beta]-amyloid Peptide (1-42), Human, Oncogene - Size 250 Ug - Model Pp69--25mg - Each (.25 Mg) by Oncogene [beta]-Amyloid Peptide (1-42), Human, Oncogene - Size 250 ug - Model PP69--25MG - Each (.25 MG) : Lyophilized.Synthetic peptide corresponding to amino acids 1-42 of the processed human amyloid peptide. Supplied in a form that is not neurotoxic prior to preincubation. The level of toxicity has recently been shown to correlate to the extent of beta sheet structure. Reconstitute with degassed HPLC grade deionized water. Purity: >95% by HPLC. FW: 4 kDa. |
|
Protective effects of Angelica sinensis extract on amyloid [beta]-peptide-induced neurotoxicity.: An article from: Phytomedicine: International Journal of Phytotherapy & Phytopharmacology by Shih-Hao Huang (Author), Chun-Mao Lin (Author), Been-Huang Chiang (Author) This digital document is an article from Phytomedicine: International Journal of Phytotherapy & Phytopharmacology, published by Urban & Fischer Verlag on September 1, 2008. The length of the article is 6283 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available immediately after purchase. You can view it with any web browser. Citation Details Title: Protective effects of Angelica sinensis extract on amyloid [beta]-peptide-induced neurotoxicity. Author: Shih-Hao Huang Publication: Phytomedicine: International Journal of Phytotherapy & Phytopharmacology (Magazine/Journal) Date: September 1, 2008 Publisher: Urban & Fischer Verlag Volume: 15 Issue: 9 Page: 710(12) Distributed by Gale, a... | |
 |
Peroxisome Proliferator-Activated Receptor: A Transcription Factor Relgulating Amyloid Beta Peptide Clearance (Acta Biomedica Lovaniensia) by Ira Espuny Camacho (Author) |
 |
Abeta Peptide and Alzheimer's Disease: Celebrating a Century of Research by Colin J. Barrow (Editor), David H. Small (Editor) Recent advances in genetics and brain biochemistry point to the Abeta peptide as the major culprit in causing neurodegeneration in Alzheimer’s Disease (AD). Abeta Peptide and Alzheimer’s Disease is specifically targeted at summarizing current knowledge of the Abeta peptide and its role in AD. Written by leaders in the industrial and academic world specializing in this rapidly moving area, the book covers fundamental biochemical studies on this peptide, the genetic impact on Abeta expression and processing, and various AD therapeutic strategies that target Abeta. Although specifically focusing on the Abeta peptide and AD, there is also some discussion on the similarity and differences of this peptide and AD with other amyloidogenic diseases, such as prion disease, Parkinsons and... |
|
|
[beta]-amyloid Peptide (1-40, Gln22), Human, Oncogene - Size 500 Ug - Model Pp68--5mg - Each (1 Mg) by Oncogene [beta]-Amyloid Peptide (1-40, Gln22), Human, Oncogene - Size 500 ug - Model PP68--5MG - Each (1 MG) : Lyophilized.Synthetic peptide corresponding to amino acids 1-40 of the processed human amyloid peptide with a substitution of Gln22. Supplied in a form that is not neurotoxic prior to preincubation. The level of toxicity has recently been shown to correlate to the extent of beta sheet structure. Reconstitute with degassed HPLC grade deionized water. Purity: >99% by HPLC. FW: 4 kDa. |
| © 2009 BrightSurf.com |