A Portrait of Alzheimer Secretases: New Features and Familiar Faces
The amyloid β-peptide (Aβ) is a principal component of the cerebral plaques found in the brains of patients with Alzeheimer's disease (AD). This insoluble 40- to 42-amino acid peptide is formed by the cleavage of the Aβ precursor protein (APP). The three proteases that cleave APP, α-, β-, and γ...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2001-08, Vol.293 (5534), p.1449-1454 |
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| creator | Esler, William P. Wolfe, Michael S. |
| description | The amyloid β-peptide (Aβ) is a principal component of the cerebral plaques found in the brains of patients with Alzeheimer's disease (AD). This insoluble 40- to 42-amino acid peptide is formed by the cleavage of the Aβ precursor protein (APP). The three proteases that cleave APP, α-, β-, and γ-secretases, have been implicated in the etiology of AD. β-Secretase is a membrane-anchored protein with clear homology to soluble aspartyl proteases, and α-secretase displays characteristics of certain membrane-tethered metalloproteases. γ-Secretase is apparently an oligomeric complex that includes the presenilins, which may be the catalytic component of this protease. Identification of the α-, β-, and γ-secretases provides potential targets for designing new drugs to treat AD. |
| doi_str_mv | 10.1126/science.1064638 |
| format | Article |
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This insoluble 40- to 42-amino acid peptide is formed by the cleavage of the Aβ precursor protein (APP). The three proteases that cleave APP, α-, β-, and γ-secretases, have been implicated in the etiology of AD. β-Secretase is a membrane-anchored protein with clear homology to soluble aspartyl proteases, and α-secretase displays characteristics of certain membrane-tethered metalloproteases. γ-Secretase is apparently an oligomeric complex that includes the presenilins, which may be the catalytic component of this protease. Identification of the α-, β-, and γ-secretases provides potential targets for designing new drugs to treat AD.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1064638</identifier><identifier>PMID: 11520976</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Active sites ; ADAM Proteins ; ADAM17 Protein ; Alzheimer Disease - enzymology ; Alzheimer Disease - genetics ; Alzheimer Disease - metabolism ; Alzheimer Disease - pathology ; Alzheimer's disease ; Alzheimers disease ; Amyloid beta-Peptides - metabolism ; Amyloid beta-Protein Precursor - genetics ; Amyloid beta-Protein Precursor - metabolism ; Amyloid Precursor Protein Secretases ; Amyloids ; Animals ; Aspartic Acid Endopeptidases - chemistry ; Aspartic Acid Endopeptidases - metabolism ; Biochemistry ; Biological and medical sciences ; Brain ; Brain - enzymology ; Brain diseases ; Catalytic Domain ; Degenerative and inherited degenerative diseases of the nervous system. 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This insoluble 40- to 42-amino acid peptide is formed by the cleavage of the Aβ precursor protein (APP). The three proteases that cleave APP, α-, β-, and γ-secretases, have been implicated in the etiology of AD. β-Secretase is a membrane-anchored protein with clear homology to soluble aspartyl proteases, and α-secretase displays characteristics of certain membrane-tethered metalloproteases. γ-Secretase is apparently an oligomeric complex that includes the presenilins, which may be the catalytic component of this protease. Identification of the α-, β-, and γ-secretases provides potential targets for designing new drugs to treat AD.</description><subject>Active sites</subject><subject>ADAM Proteins</subject><subject>ADAM17 Protein</subject><subject>Alzheimer Disease - enzymology</subject><subject>Alzheimer Disease - genetics</subject><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer Disease - pathology</subject><subject>Alzheimer's disease</subject><subject>Alzheimers disease</subject><subject>Amyloid beta-Peptides - metabolism</subject><subject>Amyloid beta-Protein Precursor - genetics</subject><subject>Amyloid beta-Protein Precursor - metabolism</subject><subject>Amyloid Precursor Protein Secretases</subject><subject>Amyloids</subject><subject>Animals</subject><subject>Aspartic Acid Endopeptidases - chemistry</subject><subject>Aspartic Acid Endopeptidases - metabolism</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Brain</subject><subject>Brain - enzymology</subject><subject>Brain diseases</subject><subject>Catalytic Domain</subject><subject>Degenerative and inherited degenerative diseases of the nervous system. 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Prion diseases</subject><subject>Dimerization</subject><subject>Endopeptidases - chemistry</subject><subject>Endopeptidases - metabolism</subject><subject>Enzymes</subject><subject>Etiology</subject><subject>Genetic mutation</subject><subject>Humans</subject><subject>Individualized Instruction</subject><subject>Medical sciences</subject><subject>Membrane proteins</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Metalloendopeptidases - chemistry</subject><subject>Metalloendopeptidases - metabolism</subject><subject>Narcotics</subject><subject>Nervous system diseases</subject><subject>Neurology</subject><subject>Neuroscience</subject><subject>Peptides</subject><subject>Presenilin-1</subject><subject>Presenilin-2</subject><subject>Presenilins</subject><subject>Proteins</subject><subject>Receptors, Notch</subject><subject>Review</subject><subject>Signal Transduction</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqN0s-L1DAUB_Aiijuunr2IFBH1sN19adom8TYOzrgw7AirXkMmfR0zpM2atPjjrzc6RR0ZdMghIe-TQF6-SfKQwDkheXURtMFO4zmBqqgov5VMCIgyEznQ28kEgFYZB1aeJPdC2ALEmqB3kxNCyhwEqybJbJq-db73yvSpa9Kp_fYRTYs-vUbtsVcBw8v0Cj-nc1T94DGkqqvTuWqNNcrHhcZwP7nTKBvwwTifJu_nr9_N3mTL1eJyNl1muuKiz4ioiFo3vCRCEOR1xZUGUnNFeY25KBhtOOoaqEKEnFEsecnWQHMomIgVepo83917492nAUMvWxM0Wqs6dEOQrKDxrWUBUT77t4zNy0v4PyQ8drZkJMInf8GtG3wXnytzQsuqAi4iOtuhjbIoTde42Fi9wQ69sq7DxsTtKWOCgqA08uwAj6PG1uhD_sWej6THL_1GDSHIy-uro-nqw9H01eJYyhfLPXp2iGpnLW5QxlzMVnv8Yse1dyF4bOSNN63yXyUB-SPpcky6HJMeTzweP2RYt1j_9mO0I3g6AhW0so1XnTbhj3tFUfz8s0c7tg2987_KFHhRxBB-B-E3CK4</recordid><startdate>20010824</startdate><enddate>20010824</enddate><creator>Esler, William P.</creator><creator>Wolfe, Michael S.</creator><general>American Society for the Advancement of Science</general><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>0-V</scope><scope>3V.</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88B</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ALSLI</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CJNVE</scope><scope>D1I</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9-</scope><scope>K9.</scope><scope>KB.</scope><scope>KR7</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0K</scope><scope>M0P</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEDU</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20010824</creationdate><title>A Portrait of Alzheimer Secretases: New Features and Familiar Faces</title><author>Esler, William P. ; 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| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 2001-08, Vol.293 (5534), p.1449-1454 |
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| language | eng |
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| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Active sites ADAM Proteins ADAM17 Protein Alzheimer Disease - enzymology Alzheimer Disease - genetics Alzheimer Disease - metabolism Alzheimer Disease - pathology Alzheimer's disease Alzheimers disease Amyloid beta-Peptides - metabolism Amyloid beta-Protein Precursor - genetics Amyloid beta-Protein Precursor - metabolism Amyloid Precursor Protein Secretases Amyloids Animals Aspartic Acid Endopeptidases - chemistry Aspartic Acid Endopeptidases - metabolism Biochemistry Biological and medical sciences Brain Brain - enzymology Brain diseases Catalytic Domain Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Dimerization Endopeptidases - chemistry Endopeptidases - metabolism Enzymes Etiology Genetic mutation Humans Individualized Instruction Medical sciences Membrane proteins Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Metalloendopeptidases - chemistry Metalloendopeptidases - metabolism Narcotics Nervous system diseases Neurology Neuroscience Peptides Presenilin-1 Presenilin-2 Presenilins Proteins Receptors, Notch Review Signal Transduction |
| title | A Portrait of Alzheimer Secretases: New Features and Familiar Faces |
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