Amino acid sequence determinants and molecular chaperones in amyloid fibril formation
Amyloid consists of cross-β-sheet fibrils and is associated with about 25 human diseases, including several neurodegenerative diseases, systemic and localized amyloidoses and type II diabetes mellitus. Amyloid-forming proteins differ in structures and sequences, and it is to a large extent unknown w...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2010-05, Vol.396 (1), p.2-6 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 6 |
|---|---|
| container_issue | 1 |
| container_start_page | 2 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 396 |
| creator | Nerelius, Charlotte Fitzen, Michael Johansson, Jan |
| description | Amyloid consists of cross-β-sheet fibrils and is associated with about 25 human diseases, including several neurodegenerative diseases, systemic and localized amyloidoses and type II diabetes mellitus. Amyloid-forming proteins differ in structures and sequences, and it is to a large extent unknown what makes them convert from their native conformations into amyloid. In this review, current understanding of amino acid sequence determinants and the effects of molecular chaperones on amyloid formation are discussed. Studies of the nonpolar, transmembrane surfactant protein C (SP-C) have revealed amino acid sequence features that determine its amyloid fibril formation, features that are also found in the amyloid β-peptide in Alzheimer’s disease and the prion protein. Moreover, a proprotein chaperone domain (CTC
Brichos) that prevents amyloid-like aggregation during proSP-C biosynthesis can prevent fibril formation also of other amyloidogenic proteins. |
| doi_str_mv | 10.1016/j.bbrc.2010.02.105 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_swepu</sourceid><recordid>TN_cdi_swepub_primary_oai_swepub_ki_se_551187</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X10003384</els_id><sourcerecordid>733358719</sourcerecordid><originalsourceid>FETCH-LOGICAL-c463t-2562fc77d763382d1649a7def6b43f0cf11b5f272f21a10fd529626e3a39ee4a3</originalsourceid><addsrcrecordid>eNqFkUuLFDEUhYMoTtv6B1xI7VxVm5tnFbgZBl8w4MYBdyGV3GDaqkqbVCnz703R7SzH1Q2H7xxu7iHkNdADUFDvjodhyO7AaBUoq5p8QnZAe9oyoOIp2VFKVct6-H5FXpRypBRAqP45uWJU9KJm7Mjd9RTn1FgXfVPw14qzw8bjgrnqdl5KY2ffTGlEt442N-6HPWFOM5Ymzo2d7sdUnSEOOY5NSHmyS0zzS_Is2LHgq8vck7uPH77dfG5vv376cnN92zqh-NIyqVhwWnutOO-YByV6qz0GNQgeqAsAgwxMs8DAAg1esl4xhdzyHlFYviftObf8wdM6mFOOk833JtloLtLP-kIjJUCnH-fHdbB5G5tBdFB32pO3Z_6UU71NWcwUi8NxtDOmtZiuLixBaPgvqTnnstPQV5KdSZdTKRnDwxZAzdarOZqtV7P1aiirmqymN5f4dZjQP1j-FVmB92cA67l_R6wfcXEr08eMbjE-xcfy_wJT-bVA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>733358719</pqid></control><display><type>article</type><title>Amino acid sequence determinants and molecular chaperones in amyloid fibril formation</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Nerelius, Charlotte ; Fitzen, Michael ; Johansson, Jan</creator><creatorcontrib>Nerelius, Charlotte ; Fitzen, Michael ; Johansson, Jan ; Sveriges lantbruksuniversitet</creatorcontrib><description>Amyloid consists of cross-β-sheet fibrils and is associated with about 25 human diseases, including several neurodegenerative diseases, systemic and localized amyloidoses and type II diabetes mellitus. Amyloid-forming proteins differ in structures and sequences, and it is to a large extent unknown what makes them convert from their native conformations into amyloid. In this review, current understanding of amino acid sequence determinants and the effects of molecular chaperones on amyloid formation are discussed. Studies of the nonpolar, transmembrane surfactant protein C (SP-C) have revealed amino acid sequence features that determine its amyloid fibril formation, features that are also found in the amyloid β-peptide in Alzheimer’s disease and the prion protein. Moreover, a proprotein chaperone domain (CTC
Brichos) that prevents amyloid-like aggregation during proSP-C biosynthesis can prevent fibril formation also of other amyloidogenic proteins.</description><identifier>ISSN: 0006-291X</identifier><identifier>ISSN: 1090-2104</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2010.02.105</identifier><identifier>PMID: 20494101</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Alzheimer’s disease ; Amino Acid Sequence ; Amyloid - chemistry ; Amyloid - metabolism ; Amyloidosis - metabolism ; Biochemistry and Molecular Biology ; Biofysik ; Biokemi och molekylärbiologi ; Biophysics ; Brichos ; Humans ; Molecular Chaperones - metabolism ; Neurodegenerative Diseases - metabolism ; Prion ; Protein Folding ; Protein misfolding ; Pulmonary Surfactant-Associated Protein C - chemistry ; Pulmonary Surfactant-Associated Protein C - metabolism ; Secondary structure ; Surfactant protein C</subject><ispartof>Biochemical and biophysical research communications, 2010-05, Vol.396 (1), p.2-6</ispartof><rights>2010 Elsevier Inc.</rights><rights>2010 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-2562fc77d763382d1649a7def6b43f0cf11b5f272f21a10fd529626e3a39ee4a3</citedby><cites>FETCH-LOGICAL-c463t-2562fc77d763382d1649a7def6b43f0cf11b5f272f21a10fd529626e3a39ee4a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2010.02.105$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,777,781,882,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20494101$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://res.slu.se/id/publ/48163$$DView record from Swedish Publication Index$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:120539389$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Nerelius, Charlotte</creatorcontrib><creatorcontrib>Fitzen, Michael</creatorcontrib><creatorcontrib>Johansson, Jan</creatorcontrib><creatorcontrib>Sveriges lantbruksuniversitet</creatorcontrib><title>Amino acid sequence determinants and molecular chaperones in amyloid fibril formation</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Amyloid consists of cross-β-sheet fibrils and is associated with about 25 human diseases, including several neurodegenerative diseases, systemic and localized amyloidoses and type II diabetes mellitus. Amyloid-forming proteins differ in structures and sequences, and it is to a large extent unknown what makes them convert from their native conformations into amyloid. In this review, current understanding of amino acid sequence determinants and the effects of molecular chaperones on amyloid formation are discussed. Studies of the nonpolar, transmembrane surfactant protein C (SP-C) have revealed amino acid sequence features that determine its amyloid fibril formation, features that are also found in the amyloid β-peptide in Alzheimer’s disease and the prion protein. Moreover, a proprotein chaperone domain (CTC
Brichos) that prevents amyloid-like aggregation during proSP-C biosynthesis can prevent fibril formation also of other amyloidogenic proteins.</description><subject>Alzheimer’s disease</subject><subject>Amino Acid Sequence</subject><subject>Amyloid - chemistry</subject><subject>Amyloid - metabolism</subject><subject>Amyloidosis - metabolism</subject><subject>Biochemistry and Molecular Biology</subject><subject>Biofysik</subject><subject>Biokemi och molekylärbiologi</subject><subject>Biophysics</subject><subject>Brichos</subject><subject>Humans</subject><subject>Molecular Chaperones - metabolism</subject><subject>Neurodegenerative Diseases - metabolism</subject><subject>Prion</subject><subject>Protein Folding</subject><subject>Protein misfolding</subject><subject>Pulmonary Surfactant-Associated Protein C - chemistry</subject><subject>Pulmonary Surfactant-Associated Protein C - metabolism</subject><subject>Secondary structure</subject><subject>Surfactant protein C</subject><issn>0006-291X</issn><issn>1090-2104</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuLFDEUhYMoTtv6B1xI7VxVm5tnFbgZBl8w4MYBdyGV3GDaqkqbVCnz703R7SzH1Q2H7xxu7iHkNdADUFDvjodhyO7AaBUoq5p8QnZAe9oyoOIp2VFKVct6-H5FXpRypBRAqP45uWJU9KJm7Mjd9RTn1FgXfVPw14qzw8bjgrnqdl5KY2ffTGlEt442N-6HPWFOM5Ymzo2d7sdUnSEOOY5NSHmyS0zzS_Is2LHgq8vck7uPH77dfG5vv376cnN92zqh-NIyqVhwWnutOO-YByV6qz0GNQgeqAsAgwxMs8DAAg1esl4xhdzyHlFYviftObf8wdM6mFOOk833JtloLtLP-kIjJUCnH-fHdbB5G5tBdFB32pO3Z_6UU71NWcwUi8NxtDOmtZiuLixBaPgvqTnnstPQV5KdSZdTKRnDwxZAzdarOZqtV7P1aiirmqymN5f4dZjQP1j-FVmB92cA67l_R6wfcXEr08eMbjE-xcfy_wJT-bVA</recordid><startdate>20100521</startdate><enddate>20100521</enddate><creator>Nerelius, Charlotte</creator><creator>Fitzen, Michael</creator><creator>Johansson, Jan</creator><general>Elsevier Inc</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>7X8</scope><scope>7TM</scope><scope>ADTPV</scope><scope>AOWAS</scope></search><sort><creationdate>20100521</creationdate><title>Amino acid sequence determinants and molecular chaperones in amyloid fibril formation</title><author>Nerelius, Charlotte ; Fitzen, Michael ; Johansson, Jan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-2562fc77d763382d1649a7def6b43f0cf11b5f272f21a10fd529626e3a39ee4a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Alzheimer’s disease</topic><topic>Amino Acid Sequence</topic><topic>Amyloid - chemistry</topic><topic>Amyloid - metabolism</topic><topic>Amyloidosis - metabolism</topic><topic>Biochemistry and Molecular Biology</topic><topic>Biofysik</topic><topic>Biokemi och molekylärbiologi</topic><topic>Biophysics</topic><topic>Brichos</topic><topic>Humans</topic><topic>Molecular Chaperones - metabolism</topic><topic>Neurodegenerative Diseases - metabolism</topic><topic>Prion</topic><topic>Protein Folding</topic><topic>Protein misfolding</topic><topic>Pulmonary Surfactant-Associated Protein C - chemistry</topic><topic>Pulmonary Surfactant-Associated Protein C - metabolism</topic><topic>Secondary structure</topic><topic>Surfactant protein C</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nerelius, Charlotte</creatorcontrib><creatorcontrib>Fitzen, Michael</creatorcontrib><creatorcontrib>Johansson, Jan</creatorcontrib><creatorcontrib>Sveriges lantbruksuniversitet</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Nucleic Acids Abstracts</collection><collection>SwePub</collection><collection>SwePub Articles</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nerelius, Charlotte</au><au>Fitzen, Michael</au><au>Johansson, Jan</au><aucorp>Sveriges lantbruksuniversitet</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amino acid sequence determinants and molecular chaperones in amyloid fibril formation</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2010-05-21</date><risdate>2010</risdate><volume>396</volume><issue>1</issue><spage>2</spage><epage>6</epage><pages>2-6</pages><issn>0006-291X</issn><issn>1090-2104</issn><eissn>1090-2104</eissn><abstract>Amyloid consists of cross-β-sheet fibrils and is associated with about 25 human diseases, including several neurodegenerative diseases, systemic and localized amyloidoses and type II diabetes mellitus. Amyloid-forming proteins differ in structures and sequences, and it is to a large extent unknown what makes them convert from their native conformations into amyloid. In this review, current understanding of amino acid sequence determinants and the effects of molecular chaperones on amyloid formation are discussed. Studies of the nonpolar, transmembrane surfactant protein C (SP-C) have revealed amino acid sequence features that determine its amyloid fibril formation, features that are also found in the amyloid β-peptide in Alzheimer’s disease and the prion protein. Moreover, a proprotein chaperone domain (CTC
Brichos) that prevents amyloid-like aggregation during proSP-C biosynthesis can prevent fibril formation also of other amyloidogenic proteins.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>20494101</pmid><doi>10.1016/j.bbrc.2010.02.105</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2010-05, Vol.396 (1), p.2-6 |
| issn | 0006-291X 1090-2104 1090-2104 |
| language | eng |
| recordid | cdi_swepub_primary_oai_swepub_ki_se_551187 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Alzheimer’s disease Amino Acid Sequence Amyloid - chemistry Amyloid - metabolism Amyloidosis - metabolism Biochemistry and Molecular Biology Biofysik Biokemi och molekylärbiologi Biophysics Brichos Humans Molecular Chaperones - metabolism Neurodegenerative Diseases - metabolism Prion Protein Folding Protein misfolding Pulmonary Surfactant-Associated Protein C - chemistry Pulmonary Surfactant-Associated Protein C - metabolism Secondary structure Surfactant protein C |
| title | Amino acid sequence determinants and molecular chaperones in amyloid fibril formation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-17T11%3A46%3A28IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_swepu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Amino%20acid%20sequence%20determinants%20and%20molecular%20chaperones%20in%20amyloid%20fibril%20formation&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Nerelius,%20Charlotte&rft.aucorp=Sveriges%20lantbruksuniversitet&rft.date=2010-05-21&rft.volume=396&rft.issue=1&rft.spage=2&rft.epage=6&rft.pages=2-6&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2010.02.105&rft_dat=%3Cproquest_swepu%3E733358719%3C/proquest_swepu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=733358719&rft_id=info:pmid/20494101&rft_els_id=S0006291X10003384&rfr_iscdi=true |