The Alzheimer A beta peptide develops protease resistance in association with its polymerization into fibrils
An intriguing property of the polypeptide constituents of amyloid is that they apparently can escape the proteolytic mechanisms that normally catalyze turnover and prevent abnormal tissue accumulation of polypeptides. Here, we demonstrate that the A beta peptide, the principal component of cerebrova...
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| Veröffentlicht in: | The Journal of biological chemistry 1994-12, Vol.269 (49), p.30773-30776 |
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| container_end_page | 30776 |
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| container_issue | 49 |
| container_start_page | 30773 |
| container_title | The Journal of biological chemistry |
| container_volume | 269 |
| creator | Nordstedt, C Näslund, J Tjernberg, L O Karlström, A R Thyberg, J Terenius, L |
| description | An intriguing property of the polypeptide constituents of amyloid is that they apparently can escape the proteolytic mechanisms
that normally catalyze turnover and prevent abnormal tissue accumulation of polypeptides. Here, we demonstrate that the A
beta peptide, the principal component of cerebrovascular amyloid deposits in Alzheimer's disease, becomes resistant to an
array of proteases as a result of structural changes associated with its polymerization into amyloid fibrils. It is further
demonstrated that fibril formation per se does not lead to protease resistance but probably structural changes associated
with polymerization. The results suggest that higher order structural changes, regulated by the primary structure, enable
amyloidogenic polypeptides to escape proteolytic degradation and accumulate in tissues. |
| doi_str_mv | 10.1016/S0021-9258(18)47347-4 |
| format | Article |
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that normally catalyze turnover and prevent abnormal tissue accumulation of polypeptides. Here, we demonstrate that the A
beta peptide, the principal component of cerebrovascular amyloid deposits in Alzheimer's disease, becomes resistant to an
array of proteases as a result of structural changes associated with its polymerization into amyloid fibrils. It is further
demonstrated that fibril formation per se does not lead to protease resistance but probably structural changes associated
with polymerization. The results suggest that higher order structural changes, regulated by the primary structure, enable
amyloidogenic polypeptides to escape proteolytic degradation and accumulate in tissues.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)47347-4</identifier><identifier>PMID: 7983005</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Alzheimer Disease - metabolism ; Amino Acid Sequence ; Amyloid beta-Peptides - chemistry ; Amyloid beta-Peptides - metabolism ; Humans ; Microscopy, Electron ; Molecular Sequence Data ; Polymers ; Trypsin - metabolism</subject><ispartof>The Journal of biological chemistry, 1994-12, Vol.269 (49), p.30773-30776</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c411t-2a90d6b94fe07f1ba4c6de1ba01cd95d10bbaf0b51c2ff6869452932819eb4b33</citedby><cites>FETCH-LOGICAL-c411t-2a90d6b94fe07f1ba4c6de1ba01cd95d10bbaf0b51c2ff6869452932819eb4b33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7983005$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nordstedt, C</creatorcontrib><creatorcontrib>Näslund, J</creatorcontrib><creatorcontrib>Tjernberg, L O</creatorcontrib><creatorcontrib>Karlström, A R</creatorcontrib><creatorcontrib>Thyberg, J</creatorcontrib><creatorcontrib>Terenius, L</creatorcontrib><title>The Alzheimer A beta peptide develops protease resistance in association with its polymerization into fibrils</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>An intriguing property of the polypeptide constituents of amyloid is that they apparently can escape the proteolytic mechanisms
that normally catalyze turnover and prevent abnormal tissue accumulation of polypeptides. Here, we demonstrate that the A
beta peptide, the principal component of cerebrovascular amyloid deposits in Alzheimer's disease, becomes resistant to an
array of proteases as a result of structural changes associated with its polymerization into amyloid fibrils. It is further
demonstrated that fibril formation per se does not lead to protease resistance but probably structural changes associated
with polymerization. The results suggest that higher order structural changes, regulated by the primary structure, enable
amyloidogenic polypeptides to escape proteolytic degradation and accumulate in tissues.</description><subject>Alzheimer Disease - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Amyloid beta-Peptides - chemistry</subject><subject>Amyloid beta-Peptides - metabolism</subject><subject>Humans</subject><subject>Microscopy, Electron</subject><subject>Molecular Sequence Data</subject><subject>Polymers</subject><subject>Trypsin - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vFDEMhiMEKkvhJ1TKASE4DMSTzEeOq4ovqRIHisQtSjIexmhmMiRZqvbXk3ZXveKLJft5bcsvYxcg3oOA9sN3IWqodN30b6F_pzqpuko9YTsQvaxkAz-fst0j8py9SOm3KKE0nLGzTvdSiGbHlusJ-X6-m5AWjHzPHWbLN9wyDcgH_Itz2BLfYshoE_KIiVK2q0dOK7cpBU82U1j5DeWJUy5smG_LLLo71mnNgY_kIs3pJXs22jnhq1M-Zz8-fby-_FJdffv89XJ_VXkFkKvaajG0TqsRRTeCs8q3A5YswA-6GUA4Z0fhGvD1OLZ9q1VTa1n3oNEpJ-U5e3OcW-7-c8CUzULJ4zzbFcMhma5oigD-C0InoDyxLWBzBH0MKUUczRZpsfHWgDD3fpgHP8z9sw305sEPo4ru4rTg4BYcHlUnA0r_9bE_0a_phiIaR8FPuJi61UZpI0XXSfkP84aUDg</recordid><startdate>19941209</startdate><enddate>19941209</enddate><creator>Nordstedt, C</creator><creator>Näslund, J</creator><creator>Tjernberg, L O</creator><creator>Karlström, A R</creator><creator>Thyberg, J</creator><creator>Terenius, L</creator><general>American Society for Biochemistry and Molecular Biology</general><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>7TK</scope><scope>7X8</scope></search><sort><creationdate>19941209</creationdate><title>The Alzheimer A beta peptide develops protease resistance in association with its polymerization into fibrils</title><author>Nordstedt, C ; Näslund, J ; Tjernberg, L O ; Karlström, A R ; Thyberg, J ; Terenius, L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-2a90d6b94fe07f1ba4c6de1ba01cd95d10bbaf0b51c2ff6869452932819eb4b33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Alzheimer Disease - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Amyloid beta-Peptides - chemistry</topic><topic>Amyloid beta-Peptides - metabolism</topic><topic>Humans</topic><topic>Microscopy, Electron</topic><topic>Molecular Sequence Data</topic><topic>Polymers</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nordstedt, C</creatorcontrib><creatorcontrib>Näslund, J</creatorcontrib><creatorcontrib>Tjernberg, L O</creatorcontrib><creatorcontrib>Karlström, A R</creatorcontrib><creatorcontrib>Thyberg, J</creatorcontrib><creatorcontrib>Terenius, L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nordstedt, C</au><au>Näslund, J</au><au>Tjernberg, L O</au><au>Karlström, A R</au><au>Thyberg, J</au><au>Terenius, L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Alzheimer A beta peptide develops protease resistance in association with its polymerization into fibrils</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1994-12-09</date><risdate>1994</risdate><volume>269</volume><issue>49</issue><spage>30773</spage><epage>30776</epage><pages>30773-30776</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>An intriguing property of the polypeptide constituents of amyloid is that they apparently can escape the proteolytic mechanisms
that normally catalyze turnover and prevent abnormal tissue accumulation of polypeptides. Here, we demonstrate that the A
beta peptide, the principal component of cerebrovascular amyloid deposits in Alzheimer's disease, becomes resistant to an
array of proteases as a result of structural changes associated with its polymerization into amyloid fibrils. It is further
demonstrated that fibril formation per se does not lead to protease resistance but probably structural changes associated
with polymerization. The results suggest that higher order structural changes, regulated by the primary structure, enable
amyloidogenic polypeptides to escape proteolytic degradation and accumulate in tissues.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7983005</pmid><doi>10.1016/S0021-9258(18)47347-4</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1994-12, Vol.269 (49), p.30773-30776 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76862931 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Alzheimer Disease - metabolism Amino Acid Sequence Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - metabolism Humans Microscopy, Electron Molecular Sequence Data Polymers Trypsin - metabolism |
| title | The Alzheimer A beta peptide develops protease resistance in association with its polymerization into fibrils |
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