Physiological Functions of APP Family Proteins
Biochemical and genetic evidence establishes a central role of the amyloid precursor protein (APP) in Alzheimer disease (AD) pathogenesis. Biochemically, deposition of the β-amyloid (Aβ) peptides produced from proteolytic processing of APP forms the defining pathological hallmark of AD; genetically,...
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| Published in | Cold Spring Harbor perspectives in medicine Vol. 2; no. 2; p. a006288 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Cold Spring Harbor Laboratory Press
01.02.2012
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| Online Access | Get full text |
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| Abstract | Biochemical and genetic evidence establishes a central role of the amyloid precursor protein (APP) in Alzheimer disease (AD) pathogenesis. Biochemically, deposition of the β-amyloid (Aβ) peptides produced from proteolytic processing of APP forms the defining pathological hallmark of AD; genetically, both point mutations and duplications of wild-type APP are linked to a subset of early onset of familial AD (FAD) and cerebral amyloid angiopathy. As such, the biological functions of APP and its processing products have been the subject of intense investigation, and the past 20+ years of research have met with both excitement and challenges. This article will review the current understanding of the physiological functions of APP in the context of APP family members. |
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| AbstractList | Biochemical and genetic evidence establishes a central role of the amyloid precursor protein (APP) in Alzheimer disease (AD) pathogenesis. Biochemically, deposition of the β-amyloid (Aβ) peptides produced from proteolytic processing of APP forms the defining pathological hallmark of AD; genetically, both point mutations and duplications of wild-type APP are linked to a subset of early onset of familial AD (FAD) and cerebral amyloid angiopathy. As such, the biological functions of APP and its processing products have been the subject of intense investigation, and the past 20+ years of research have met with both excitement and challenges. This article will review the current understanding of the physiological functions of APP in the context of APP family members.Biochemical and genetic evidence establishes a central role of the amyloid precursor protein (APP) in Alzheimer disease (AD) pathogenesis. Biochemically, deposition of the β-amyloid (Aβ) peptides produced from proteolytic processing of APP forms the defining pathological hallmark of AD; genetically, both point mutations and duplications of wild-type APP are linked to a subset of early onset of familial AD (FAD) and cerebral amyloid angiopathy. As such, the biological functions of APP and its processing products have been the subject of intense investigation, and the past 20+ years of research have met with both excitement and challenges. This article will review the current understanding of the physiological functions of APP in the context of APP family members. Biochemical and genetic evidence establishes a central role of the amyloid precursor protein (APP) in Alzheimer disease (AD) pathogenesis. Biochemically, deposition of the β-amyloid (Aβ) peptides produced from proteolytic processing of APP forms the defining pathological hallmark of AD; genetically, both point mutations and duplications of wild-type APP are linked to a subset of early onset of familial AD (FAD) and cerebral amyloid angiopathy. As such, the biological functions of APP and its processing products have been the subject of intense investigation, and the past 20+ years of research have met with both excitement and challenges. This article will review the current understanding of the physiological functions of APP in the context of APP family members. A pathological hallmark of Alzheimer disease is the deposition of β-amyloid (Aβ) peptides from amyloid precursor protein (APP). APP undergoes complex proteolytic processing and is part of a gene family whose members have partially overlapping functions. Biochemical and genetic evidence establishes a central role of the amyloid precursor protein (APP) in Alzheimer disease (AD) pathogenesis. Biochemically, deposition of the β-amyloid (Aβ) peptides produced from proteolytic processing of APP forms the defining pathological hallmark of AD; genetically, both point mutations and duplications of wild-type APP are linked to a subset of early onset of familial AD (FAD) and cerebral amyloid angiopathy. As such, the biological functions of APP and its processing products have been the subject of intense investigation, and the past 20+ years of research have met with both excitement and challenges. This article will review the current understanding of the physiological functions of APP in the context of APP family members. |
| Author | Zheng, H. Muller, U. C. |
| AuthorAffiliation | 2 Huffington Center on Aging and Departments of Molecular & Human Genetics, Molecular & Cellular Biology and Neuroscience, Baylor College of Medicine, Houston, Texas 77030 1 Institute for Pharmacy and Molecular Biotechnology, University of Heidelberg, D-69120 Heidelberg, Germany |
| AuthorAffiliation_xml | – name: 2 Huffington Center on Aging and Departments of Molecular & Human Genetics, Molecular & Cellular Biology and Neuroscience, Baylor College of Medicine, Houston, Texas 77030 – name: 1 Institute for Pharmacy and Molecular Biotechnology, University of Heidelberg, D-69120 Heidelberg, Germany |
| Author_xml | – sequence: 1 givenname: U. C. surname: Muller fullname: Muller, U. C. – sequence: 2 givenname: H. surname: Zheng fullname: Zheng, H. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22355794$$D View this record in MEDLINE/PubMed |
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| Snippet | Biochemical and genetic evidence establishes a central role of the amyloid precursor protein (APP) in Alzheimer disease (AD) pathogenesis. Biochemically,... |
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| SubjectTerms | Alzheimer Disease - etiology Amyloid beta-Protein Precursor - genetics Amyloid beta-Protein Precursor - metabolism Amyloid beta-Protein Precursor - physiology Animals Apoptosis - physiology Axonal Transport - physiology Cell Adhesion - physiology Disease Models, Animal Germ-Line Mutation - physiology Humans Mice Mice, Knockout Nerve Degeneration - physiopathology Neurons - physiology Signal Transduction - physiology Synapses - physiology |
| Title | Physiological Functions of APP Family Proteins |
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