Structural specificity of haemosiderin iron cores in iron-overload diseases
Haemosiderin iron cores isolated from patients with secondary haemochromatosis have a goethite-like (α-FeOOH) crystal structure whereas those from patients with primary haemochromatosis are amorphous Fe (III) oxide. Haemosiderin cores isolated from normal human spleen are crystalline ferrihydrite (5...
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| Veröffentlicht in: | FEBS letters 1988-07, Vol.234 (1), p.69-72 |
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| container_title | FEBS letters |
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| creator | Mann, S. Wade, V.J. Dickson, D.P.E. Reid, N.M.K. Ward, R.J. O'Connell, M. Peters, T.J. |
| description | Haemosiderin iron cores isolated from patients with secondary haemochromatosis have a goethite-like (α-FeOOH) crystal structure whereas those from patients with primary haemochromatosis are amorphous Fe (III) oxide. Haemosiderin cores isolated from normal human spleen are crystalline ferrihydrite (5Fe
2O
3·9H
2O). The disease-specific structures are significantly different from the ferrihydrite structure of associated ferritin cores. The results are important in understanding the biological processing of iron in pathological states and in the clinical treatment of iron-overload diseases. |
| doi_str_mv | 10.1016/0014-5793(88)81305-X |
| format | Article |
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2O
3·9H
2O). The disease-specific structures are significantly different from the ferrihydrite structure of associated ferritin cores. The results are important in understanding the biological processing of iron in pathological states and in the clinical treatment of iron-overload diseases.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(88)81305-X</identifier><identifier>PMID: 3391272</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Crystallization ; Dialysis ; Electrophoresis, Polyacrylamide Gel ; Ferric Compounds ; Ferritins - analysis ; Fundamental and applied biological sciences. Psychology ; hemochromatosis ; Hemochromatosis - metabolism ; Hemosiderin ; Hemosiderin - analysis ; Humans ; Iron - analysis ; Iron - metabolism ; Iron-core structure ; Iron-overload ; Liver - analysis ; Metalloproteins ; Microscopy, Electron ; Other metalloproteins ; Oxalates ; Oxalic Acid ; Proteins ; Proteins - analysis ; Solubility ; Spectrometry, Gamma ; Spleen - analysis</subject><ispartof>FEBS letters, 1988-07, Vol.234 (1), p.69-72</ispartof><rights>1988</rights><rights>FEBS Letters 234 (1988) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c441X-47cff164d1707e73890bccdb9d860cef0260ccb265bd94471b10fd85e680aeb63</citedby><cites>FETCH-LOGICAL-c441X-47cff164d1707e73890bccdb9d860cef0260ccb265bd94471b10fd85e680aeb63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(88)81305-X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7184195$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3391272$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mann, S.</creatorcontrib><creatorcontrib>Wade, V.J.</creatorcontrib><creatorcontrib>Dickson, D.P.E.</creatorcontrib><creatorcontrib>Reid, N.M.K.</creatorcontrib><creatorcontrib>Ward, R.J.</creatorcontrib><creatorcontrib>O'Connell, M.</creatorcontrib><creatorcontrib>Peters, T.J.</creatorcontrib><title>Structural specificity of haemosiderin iron cores in iron-overload diseases</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Haemosiderin iron cores isolated from patients with secondary haemochromatosis have a goethite-like (α-FeOOH) crystal structure whereas those from patients with primary haemochromatosis are amorphous Fe (III) oxide. Haemosiderin cores isolated from normal human spleen are crystalline ferrihydrite (5Fe
2O
3·9H
2O). The disease-specific structures are significantly different from the ferrihydrite structure of associated ferritin cores. The results are important in understanding the biological processing of iron in pathological states and in the clinical treatment of iron-overload diseases.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Crystallization</subject><subject>Dialysis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Ferric Compounds</subject><subject>Ferritins - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hemochromatosis</subject><subject>Hemochromatosis - metabolism</subject><subject>Hemosiderin</subject><subject>Hemosiderin - analysis</subject><subject>Humans</subject><subject>Iron - analysis</subject><subject>Iron - metabolism</subject><subject>Iron-core structure</subject><subject>Iron-overload</subject><subject>Liver - analysis</subject><subject>Metalloproteins</subject><subject>Microscopy, Electron</subject><subject>Other metalloproteins</subject><subject>Oxalates</subject><subject>Oxalic Acid</subject><subject>Proteins</subject><subject>Proteins - analysis</subject><subject>Solubility</subject><subject>Spectrometry, Gamma</subject><subject>Spleen - analysis</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEGP1DAMhSMEWoaFfwBSDwjBoWA3aZNekGC1A4iVOADS3KI0cURQpxmSdtH8e9qdao7AybLf83PyMfYU4TUCNm8AUJS1bPlLpV4p5FCXu3tsg0rykotG3Webs-Uhe5TzT5h7he0Fu-C8xUpWG_b565gmO07J9EU-kA0-2DAei-iLH4b2MQdHKQxFSHEobEyUi7Ur4y2lPhpXuJDJZMqP2QNv-kxP1nrJvm-vv119LG--fPh09e6mtELgrhTSeo-NcChBkuSqhc5a17VONWDJQzUX21VN3blWCIkdgneqpkaBoa7hl-zFKfeQ4q-J8qj3IVvqezNQnLKWigOvAP5pxBpmOO2SKE5Gm2LOibw-pLA36agR9AJbLyT1QlIrpe9g69289mzNn7o9ufPSSnfWn6-6ydb0PpnBhny2SVQC23q2bU-236Gn43-d1tvr99UiLHOl7qbLe96egmimfxso6WwDDZZcSGRH7WL4-4f-AKmvrws</recordid><startdate>19880704</startdate><enddate>19880704</enddate><creator>Mann, S.</creator><creator>Wade, V.J.</creator><creator>Dickson, D.P.E.</creator><creator>Reid, N.M.K.</creator><creator>Ward, R.J.</creator><creator>O'Connell, M.</creator><creator>Peters, T.J.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19880704</creationdate><title>Structural specificity of haemosiderin iron cores in iron-overload diseases</title><author>Mann, S. ; Wade, V.J. ; Dickson, D.P.E. ; Reid, N.M.K. ; Ward, R.J. ; O'Connell, M. ; Peters, T.J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c441X-47cff164d1707e73890bccdb9d860cef0260ccb265bd94471b10fd85e680aeb63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Crystallization</topic><topic>Dialysis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Ferric Compounds</topic><topic>Ferritins - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hemochromatosis</topic><topic>Hemochromatosis - metabolism</topic><topic>Hemosiderin</topic><topic>Hemosiderin - analysis</topic><topic>Humans</topic><topic>Iron - analysis</topic><topic>Iron - metabolism</topic><topic>Iron-core structure</topic><topic>Iron-overload</topic><topic>Liver - analysis</topic><topic>Metalloproteins</topic><topic>Microscopy, Electron</topic><topic>Other metalloproteins</topic><topic>Oxalates</topic><topic>Oxalic Acid</topic><topic>Proteins</topic><topic>Proteins - analysis</topic><topic>Solubility</topic><topic>Spectrometry, Gamma</topic><topic>Spleen - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mann, S.</creatorcontrib><creatorcontrib>Wade, V.J.</creatorcontrib><creatorcontrib>Dickson, D.P.E.</creatorcontrib><creatorcontrib>Reid, N.M.K.</creatorcontrib><creatorcontrib>Ward, R.J.</creatorcontrib><creatorcontrib>O'Connell, M.</creatorcontrib><creatorcontrib>Peters, T.J.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mann, S.</au><au>Wade, V.J.</au><au>Dickson, D.P.E.</au><au>Reid, N.M.K.</au><au>Ward, R.J.</au><au>O'Connell, M.</au><au>Peters, T.J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural specificity of haemosiderin iron cores in iron-overload diseases</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1988-07-04</date><risdate>1988</risdate><volume>234</volume><issue>1</issue><spage>69</spage><epage>72</epage><pages>69-72</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Haemosiderin iron cores isolated from patients with secondary haemochromatosis have a goethite-like (α-FeOOH) crystal structure whereas those from patients with primary haemochromatosis are amorphous Fe (III) oxide. Haemosiderin cores isolated from normal human spleen are crystalline ferrihydrite (5Fe
2O
3·9H
2O). The disease-specific structures are significantly different from the ferrihydrite structure of associated ferritin cores. The results are important in understanding the biological processing of iron in pathological states and in the clinical treatment of iron-overload diseases.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>3391272</pmid><doi>10.1016/0014-5793(88)81305-X</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; ScienceDirect Journals (5 years ago - present); Alma/SFX Local Collection |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Crystallization Dialysis Electrophoresis, Polyacrylamide Gel Ferric Compounds Ferritins - analysis Fundamental and applied biological sciences. Psychology hemochromatosis Hemochromatosis - metabolism Hemosiderin Hemosiderin - analysis Humans Iron - analysis Iron - metabolism Iron-core structure Iron-overload Liver - analysis Metalloproteins Microscopy, Electron Other metalloproteins Oxalates Oxalic Acid Proteins Proteins - analysis Solubility Spectrometry, Gamma Spleen - analysis |
| title | Structural specificity of haemosiderin iron cores in iron-overload diseases |
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