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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids

Article Abstract:

Beta-amyloid peptide (A-beta), which forms deposits in the brains of people with Alzheimer's disease, has been detected in cerebrospinal fluid and in conditioned medium of mixed-brain cell cultures. This detection was made with antibodies unique for an epitope within A-beta that covers the site of normal constitutive cleavage. The isolation of A-beta in these two fluids may lead to new methods of diagnosing Alzheimer's disease and to new treatments based on removing cerebral deposits of A-beta.

Author: Schenk, Dale, Davis, Dave, Seubert, Peter, Lee, Michael, Vigo-Pelfrey, Carmen, Esch, Fred, Dovey, Harry, Sinha, Sukanto, Schlossmacher, Michael, Whaley, Justine, Swindlehurst, Cathy, McCormack, Robert, Wolfert, Robert, Selkoe, Dennis, Liederburg, Ivan
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
Health aspects, Care and treatment, Abnormalities, Peptides, Cerebrospinal fluid proteins

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Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production

Article Abstract:

A study was conducted to establish genetic determinants of familial Alzheimer's disease (FAD). Cells cultured from a FAD family were found to express DNA which encode the beta-amyloid precursor protein (beta-APP) having mutations at two points. These cells produced six to eight times more of the protein found in cerebral depositions of Alzheimer's patients than in cells expressing normal beta-APP. This is one link between a FAD genotype and its well-known phenotype.

Author: Selkoe, Dennis J., Haass, Christian, Lieberburg, Ivan, McConlogue, Lisa, Seubert, Peter, Oltersdorf, Tilman, Hung, Albert Y., Vigo-Pelfrey, Carmen, Citron, Martin
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
Causes of

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Purification and cloning of amyloid precursor protein Beta-secretase from human brain

Article Abstract:

A membrane-bound enzyme activity cleaving full-length amyloid precursor protein (APP) at the Beta-secretase cleavage site, is described. It is found to be the dominant Beta-cleavage activity in human brain. The enzyme activity was purified using a new substrate analogue inhibitor of the enzyme activity, showing that the purified enzyme has the properties predicted by Beta-secretase.

Author: Barbour, Robin, Lieberburg, Ivan, McConlogue, Lisa, Seubert, Peter, Davis, David, Power, Michael, Sinha, Sukanto, Anderson, John P., Basi, Guriqbal S., Caccavello, Russell, Doan, Minhtam, Dovey, Harry F., Frigon, Normand, Hong, Jin, Jacobson-Croak, Kirsten, Jewett, Nancy, Keim, Pamela, Knops, Jeroen, Tan, Hua, Tatsuno, Gwen, Tung, Jay, Schenk,Dale, Suomensaari, Susanna M., Wang, Shuwen, Walker, Donald, Zhao, Jun, John, Varghese
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
Research, Proteins

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Subjects list: Alzheimer's disease, Brain diseases
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