Interaction of the Anthracycline 4'-Iodo-4'-Deoxydoxorubicin with Amyloid Fibrils: Inhibition of Amyloidogenesis
All types of amyloidosis are structurally characterized by the cross β-pleated sheet conformation of the fibrils, irrespective of their biochemical composition. The clinical observation that the anthracycline 4'-iodo-4'-deoxydoxorubicin (IDOX) can induce amyloid resorption in patients with...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1995-03, Vol.92 (7), p.2959-2963 |
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| creator | Merlini, Giampaolo Ascari, Edoardo Amboldi, Nadia Bellotti, Vittorio Arbustini, Eloisa Perfetti, Vittorio Ferrari, Mario Zorzoli, Irene Marinone, Maria G. Garini, Pietro Diegoli, Marta Trizio, Domenico Ballinari, Dario |
| description | All types of amyloidosis are structurally characterized by the cross β-pleated sheet conformation of the fibrils, irrespective of their biochemical composition. The clinical observation that the anthracycline 4'-iodo-4'-deoxydoxorubicin (IDOX) can induce amyloid resorption in patients with immunoglobulin light chain amyloidosis was the starting point for this investigation of its possible mechanism of action. IDOX binds strongly to all five types of natural amyloid fibrils tested: immunoglobulin light chains, amyloid A, transthyretin (methionine-30 variant), β-protein (Alzheimer), and β2-microglobulin. Quantitative binding studies showed that IDOX, but not doxorubicin, binds strongly to amyloid fibrils. This binding is saturable and involves two apparently distinct binding sites with Kdvalues of 5.9 * 10-11M and 3.4 * 10-9M. IDOX inhibited in vitro insulin amyloid fibrillogenesis. In vivo studies using the experimental amyloid murine model confirmed the specific targeting of IDOX to amyloid deposits. Preincubation of amyloid enhancing factor with IDOX significantly reduced the formation of amyloid deposits. It is hypothesized that IDOX exerts its beneficial effects through the inhibition of fibril growth, thus increasing the solubility of existing amyloid deposits and facilitating their clearance. IDOX may represent the progenitor of a class of amyloid-binding agents that could have both diagnostic and therapeutic potential in all types of amyloidoses. |
| doi_str_mv | 10.1073/pnas.92.7.2959 |
| format | Article |
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The clinical observation that the anthracycline 4'-iodo-4'-deoxydoxorubicin (IDOX) can induce amyloid resorption in patients with immunoglobulin light chain amyloidosis was the starting point for this investigation of its possible mechanism of action. IDOX binds strongly to all five types of natural amyloid fibrils tested: immunoglobulin light chains, amyloid A, transthyretin (methionine-30 variant), β-protein (Alzheimer), and β2-microglobulin. Quantitative binding studies showed that IDOX, but not doxorubicin, binds strongly to amyloid fibrils. This binding is saturable and involves two apparently distinct binding sites with Kdvalues of 5.9 * 10-11M and 3.4 * 10-9M. IDOX inhibited in vitro insulin amyloid fibrillogenesis. In vivo studies using the experimental amyloid murine model confirmed the specific targeting of IDOX to amyloid deposits. Preincubation of amyloid enhancing factor with IDOX significantly reduced the formation of amyloid deposits. It is hypothesized that IDOX exerts its beneficial effects through the inhibition of fibril growth, thus increasing the solubility of existing amyloid deposits and facilitating their clearance. IDOX may represent the progenitor of a class of amyloid-binding agents that could have both diagnostic and therapeutic potential in all types of amyloidoses.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.92.7.2959</identifier><identifier>PMID: 7708755</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amyloid - chemistry ; Amyloid - drug effects ; Amyloid - metabolism ; Amyloid plaque ; Amyloidosis ; Amyloidosis - prevention & control ; Amyloids ; Animals ; Anthracyclines ; Biochemistry ; Doxorubicin - analogs & derivatives ; Doxorubicin - metabolism ; Doxorubicin - pharmacology ; Doxorubicin - therapeutic use ; Female ; Fluorescence ; Glycoproteins ; Immunoglobulin Light Chains - chemistry ; Immunoglobulin Light Chains - drug effects ; Immunoglobulin Light Chains - metabolism ; Insulin ; Insulin - chemistry ; Insulin - metabolism ; Mice ; Mice, Inbred Strains ; Prealbumin - chemistry ; Prealbumin - drug effects ; Prealbumin - metabolism ; Protein Structure, Secondary ; Proteins ; Serum Amyloid A Protein - analysis ; Solar fibrils ; Spleen ; Spleen - drug effects ; Spleen - pathology</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1995-03, Vol.92 (7), p.2959-2963</ispartof><rights>Copyright 1995 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Mar 28, 1995</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c484t-34b549a7639ee733af46b74bc159d766b247b2eee0d47562e55a6794111fed273</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/92/7.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2367240$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2367240$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7708755$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Merlini, Giampaolo</creatorcontrib><creatorcontrib>Ascari, Edoardo</creatorcontrib><creatorcontrib>Amboldi, Nadia</creatorcontrib><creatorcontrib>Bellotti, Vittorio</creatorcontrib><creatorcontrib>Arbustini, Eloisa</creatorcontrib><creatorcontrib>Perfetti, Vittorio</creatorcontrib><creatorcontrib>Ferrari, Mario</creatorcontrib><creatorcontrib>Zorzoli, Irene</creatorcontrib><creatorcontrib>Marinone, Maria G.</creatorcontrib><creatorcontrib>Garini, Pietro</creatorcontrib><creatorcontrib>Diegoli, Marta</creatorcontrib><creatorcontrib>Trizio, Domenico</creatorcontrib><creatorcontrib>Ballinari, Dario</creatorcontrib><title>Interaction of the Anthracycline 4'-Iodo-4'-Deoxydoxorubicin with Amyloid Fibrils: Inhibition of Amyloidogenesis</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>All types of amyloidosis are structurally characterized by the cross β-pleated sheet conformation of the fibrils, irrespective of their biochemical composition. The clinical observation that the anthracycline 4'-iodo-4'-deoxydoxorubicin (IDOX) can induce amyloid resorption in patients with immunoglobulin light chain amyloidosis was the starting point for this investigation of its possible mechanism of action. IDOX binds strongly to all five types of natural amyloid fibrils tested: immunoglobulin light chains, amyloid A, transthyretin (methionine-30 variant), β-protein (Alzheimer), and β2-microglobulin. Quantitative binding studies showed that IDOX, but not doxorubicin, binds strongly to amyloid fibrils. This binding is saturable and involves two apparently distinct binding sites with Kdvalues of 5.9 * 10-11M and 3.4 * 10-9M. IDOX inhibited in vitro insulin amyloid fibrillogenesis. In vivo studies using the experimental amyloid murine model confirmed the specific targeting of IDOX to amyloid deposits. Preincubation of amyloid enhancing factor with IDOX significantly reduced the formation of amyloid deposits. It is hypothesized that IDOX exerts its beneficial effects through the inhibition of fibril growth, thus increasing the solubility of existing amyloid deposits and facilitating their clearance. IDOX may represent the progenitor of a class of amyloid-binding agents that could have both diagnostic and therapeutic potential in all types of amyloidoses.</description><subject>Amyloid - chemistry</subject><subject>Amyloid - drug effects</subject><subject>Amyloid - metabolism</subject><subject>Amyloid plaque</subject><subject>Amyloidosis</subject><subject>Amyloidosis - prevention & control</subject><subject>Amyloids</subject><subject>Animals</subject><subject>Anthracyclines</subject><subject>Biochemistry</subject><subject>Doxorubicin - analogs & derivatives</subject><subject>Doxorubicin - metabolism</subject><subject>Doxorubicin - pharmacology</subject><subject>Doxorubicin - therapeutic use</subject><subject>Female</subject><subject>Fluorescence</subject><subject>Glycoproteins</subject><subject>Immunoglobulin Light Chains - chemistry</subject><subject>Immunoglobulin Light Chains - drug effects</subject><subject>Immunoglobulin Light Chains - metabolism</subject><subject>Insulin</subject><subject>Insulin - chemistry</subject><subject>Insulin - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred Strains</subject><subject>Prealbumin - chemistry</subject><subject>Prealbumin - drug effects</subject><subject>Prealbumin - metabolism</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Serum Amyloid A Protein - analysis</subject><subject>Solar fibrils</subject><subject>Spleen</subject><subject>Spleen - drug effects</subject><subject>Spleen - pathology</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkU2P0zAYhC0EWsrClRNIEQc4JfgzjhGXamGh0kpc4GzZyZuNq9QutgPtvydVu1VBnF7J88xorEHoJcEVwZK933qTKkUrWVEl1CO0IFiRsuYKP0YLjKksG075U_QspTXGWIkGX6ErKXEjhVig7cpniKbNLvgi9EUeoFj6PMxP-3Z0Hgr-rlyFLpTz_QRht-_CLsTJutb54rfLQ7Hc7MfguuLW2ejG9KFY-cFZ95B4ksM9eEguPUdPejMmeHG61-jH7efvN1_Lu29fVjfLu7LlDc8l41ZwZWTNFIBkzPS8tpLblgjVybq2lEtLAQB3XIqaghCmlooTQnroqGTX6OMxdzvZDXQt-BzNqLfRbUzc62Cc_lvxbtD34ZfmlLFmtr892WP4OUHKeuNSC-NoPIQpaSkpoUTUM_jmH3Adpujnr2mKCZUNpWKGqiPUxpBShP7cg2B9mFEfZtSKaqkPM86G15ftz_hpt4t6B9-DevbrfhrHDLt8EfRfcNZfHfV1yiGeAcpqSTlmfwCV0rtH</recordid><startdate>19950328</startdate><enddate>19950328</enddate><creator>Merlini, Giampaolo</creator><creator>Ascari, Edoardo</creator><creator>Amboldi, Nadia</creator><creator>Bellotti, Vittorio</creator><creator>Arbustini, Eloisa</creator><creator>Perfetti, Vittorio</creator><creator>Ferrari, Mario</creator><creator>Zorzoli, Irene</creator><creator>Marinone, Maria G.</creator><creator>Garini, Pietro</creator><creator>Diegoli, Marta</creator><creator>Trizio, Domenico</creator><creator>Ballinari, Dario</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19950328</creationdate><title>Interaction of the Anthracycline 4'-Iodo-4'-Deoxydoxorubicin with Amyloid Fibrils: Inhibition of Amyloidogenesis</title><author>Merlini, Giampaolo ; 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The clinical observation that the anthracycline 4'-iodo-4'-deoxydoxorubicin (IDOX) can induce amyloid resorption in patients with immunoglobulin light chain amyloidosis was the starting point for this investigation of its possible mechanism of action. IDOX binds strongly to all five types of natural amyloid fibrils tested: immunoglobulin light chains, amyloid A, transthyretin (methionine-30 variant), β-protein (Alzheimer), and β2-microglobulin. Quantitative binding studies showed that IDOX, but not doxorubicin, binds strongly to amyloid fibrils. This binding is saturable and involves two apparently distinct binding sites with Kdvalues of 5.9 * 10-11M and 3.4 * 10-9M. IDOX inhibited in vitro insulin amyloid fibrillogenesis. In vivo studies using the experimental amyloid murine model confirmed the specific targeting of IDOX to amyloid deposits. Preincubation of amyloid enhancing factor with IDOX significantly reduced the formation of amyloid deposits. It is hypothesized that IDOX exerts its beneficial effects through the inhibition of fibril growth, thus increasing the solubility of existing amyloid deposits and facilitating their clearance. IDOX may represent the progenitor of a class of amyloid-binding agents that could have both diagnostic and therapeutic potential in all types of amyloidoses.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>7708755</pmid><doi>10.1073/pnas.92.7.2959</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1995-03, Vol.92 (7), p.2959-2963 |
| issn | 0027-8424 1091-6490 |
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| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amyloid - chemistry Amyloid - drug effects Amyloid - metabolism Amyloid plaque Amyloidosis Amyloidosis - prevention & control Amyloids Animals Anthracyclines Biochemistry Doxorubicin - analogs & derivatives Doxorubicin - metabolism Doxorubicin - pharmacology Doxorubicin - therapeutic use Female Fluorescence Glycoproteins Immunoglobulin Light Chains - chemistry Immunoglobulin Light Chains - drug effects Immunoglobulin Light Chains - metabolism Insulin Insulin - chemistry Insulin - metabolism Mice Mice, Inbred Strains Prealbumin - chemistry Prealbumin - drug effects Prealbumin - metabolism Protein Structure, Secondary Proteins Serum Amyloid A Protein - analysis Solar fibrils Spleen Spleen - drug effects Spleen - pathology |
| title | Interaction of the Anthracycline 4'-Iodo-4'-Deoxydoxorubicin with Amyloid Fibrils: Inhibition of Amyloidogenesis |
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