Amyloid precursor protein (APP) and amyloid β (Aβ) interact with cell adhesion molecules: Implications in Alzheimer’s disease and normal physiology
Alzheimer’s disease (AD) is an incurable neurodegenerative disorder in which dysfunction and loss of synapses and neurons lead to cognitive impairment and death. Accumulation and aggregation of neurotoxic amyloid-β (Aβ) peptides generated via amyloidogenic processing of amyloid precursor protein (AP...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-07-01
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| Series: | Frontiers in Cell and Developmental Biology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fcell.2022.969547/full |
| _version_ | 1818161147600175104 |
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| author | Grant Pfundstein Alexander G. Nikonenko Vladimir Sytnyk |
| author_facet | Grant Pfundstein Alexander G. Nikonenko Vladimir Sytnyk |
| author_sort | Grant Pfundstein |
| collection | DOAJ |
| description | Alzheimer’s disease (AD) is an incurable neurodegenerative disorder in which dysfunction and loss of synapses and neurons lead to cognitive impairment and death. Accumulation and aggregation of neurotoxic amyloid-β (Aβ) peptides generated via amyloidogenic processing of amyloid precursor protein (APP) is considered to play a central role in the disease etiology. APP interacts with cell adhesion molecules, which influence the normal physiological functions of APP, its amyloidogenic and non-amyloidogenic processing, and formation of Aβ aggregates. These cell surface glycoproteins also mediate attachment of Aβ to the neuronal cell surface and induce intracellular signaling contributing to Aβ toxicity. In this review, we discuss the current knowledge surrounding the interactions of cell adhesion molecules with APP and Aβ and analyze the evidence of the critical role these proteins play in regulating the processing and physiological function of APP as well as Aβ toxicity. This is a necessary piece of the complex AD puzzle, which we should understand in order to develop safe and effective therapeutic interventions for AD. |
| first_indexed | 2024-12-11T16:13:09Z |
| format | Article |
| id | doaj.art-2123f68107b744559a56de68854b1867 |
| institution | Directory Open Access Journal |
| issn | 2296-634X |
| language | English |
| last_indexed | 2024-12-11T16:13:09Z |
| publishDate | 2022-07-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cell and Developmental Biology |
| spelling | doaj.art-2123f68107b744559a56de68854b18672022-12-22T00:59:00ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2022-07-011010.3389/fcell.2022.969547969547Amyloid precursor protein (APP) and amyloid β (Aβ) interact with cell adhesion molecules: Implications in Alzheimer’s disease and normal physiologyGrant Pfundstein0Alexander G. Nikonenko1Vladimir Sytnyk2School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW, AustraliaDepartment of Cytology, Bogomoletz Institute of Physiology, Kyiv, UkraineSchool of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW, AustraliaAlzheimer’s disease (AD) is an incurable neurodegenerative disorder in which dysfunction and loss of synapses and neurons lead to cognitive impairment and death. Accumulation and aggregation of neurotoxic amyloid-β (Aβ) peptides generated via amyloidogenic processing of amyloid precursor protein (APP) is considered to play a central role in the disease etiology. APP interacts with cell adhesion molecules, which influence the normal physiological functions of APP, its amyloidogenic and non-amyloidogenic processing, and formation of Aβ aggregates. These cell surface glycoproteins also mediate attachment of Aβ to the neuronal cell surface and induce intracellular signaling contributing to Aβ toxicity. In this review, we discuss the current knowledge surrounding the interactions of cell adhesion molecules with APP and Aβ and analyze the evidence of the critical role these proteins play in regulating the processing and physiological function of APP as well as Aβ toxicity. This is a necessary piece of the complex AD puzzle, which we should understand in order to develop safe and effective therapeutic interventions for AD.https://www.frontiersin.org/articles/10.3389/fcell.2022.969547/fullcell adhesion molecule (CAM)Alzheimer’s diseaseamyloid precursor protein (APP)amyloid-betaimmunoglobulin superfamilyintegrin |
| spellingShingle | Grant Pfundstein Alexander G. Nikonenko Vladimir Sytnyk Amyloid precursor protein (APP) and amyloid β (Aβ) interact with cell adhesion molecules: Implications in Alzheimer’s disease and normal physiology Frontiers in Cell and Developmental Biology cell adhesion molecule (CAM) Alzheimer’s disease amyloid precursor protein (APP) amyloid-beta immunoglobulin superfamily integrin |
| title | Amyloid precursor protein (APP) and amyloid β (Aβ) interact with cell adhesion molecules: Implications in Alzheimer’s disease and normal physiology |
| title_full | Amyloid precursor protein (APP) and amyloid β (Aβ) interact with cell adhesion molecules: Implications in Alzheimer’s disease and normal physiology |
| title_fullStr | Amyloid precursor protein (APP) and amyloid β (Aβ) interact with cell adhesion molecules: Implications in Alzheimer’s disease and normal physiology |
| title_full_unstemmed | Amyloid precursor protein (APP) and amyloid β (Aβ) interact with cell adhesion molecules: Implications in Alzheimer’s disease and normal physiology |
| title_short | Amyloid precursor protein (APP) and amyloid β (Aβ) interact with cell adhesion molecules: Implications in Alzheimer’s disease and normal physiology |
| title_sort | amyloid precursor protein app and amyloid β aβ interact with cell adhesion molecules implications in alzheimer s disease and normal physiology |
| topic | cell adhesion molecule (CAM) Alzheimer’s disease amyloid precursor protein (APP) amyloid-beta immunoglobulin superfamily integrin |
| url | https://www.frontiersin.org/articles/10.3389/fcell.2022.969547/full |
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