A Patient With Hereditary ATTR and a Novel AGel p.Ala578Pro Amyloidosis
Hereditary amyloidosis represents a group of diseases in which mutant proteins are deposited in various organs leading to their dysfunction. Correct identification of the amyloid-causing protein is critical because this will determine the optimal therapy for the patient. The most common type of here...
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| Veröffentlicht in: | Mayo Clinic proceedings 2018-11, Vol.93 (11), p.1678-1682 |
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| creator | Sridharan, Meera Highsmith, W. Edward Kurtin, Paul J. Zimmermann, Michael T. Theis, Jason D. Dasari, Surendra Dingli, David |
| description | Hereditary amyloidosis represents a group of diseases in which mutant proteins are deposited in various organs leading to their dysfunction. Correct identification of the amyloid-causing protein is critical because this will determine the optimal therapy for the patient. The most common type of hereditary amyloidosis is due to mutant transthyretin (ATTRm) deposition and often presents with heart failure or peripheral neuropathy. We report the first known case of a patient who had amyloidosis both due to a mutant transthyretin (p.Val122Ile) and due to a novel variant in the gelsolin gene (p.Ala578Pro). Both mutant proteins were identified by mass spectrometry analysis of amyloid deposits as well as sequencing of the genes. Molecular dynamic simulations suggest that the gelsolin p.Ala578Pro variant is likely amyloidogenic. |
| doi_str_mv | 10.1016/j.mayocp.2018.06.016 |
| format | Article |
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Edward ; Kurtin, Paul J. ; Zimmermann, Michael T. ; Theis, Jason D. ; Dasari, Surendra ; Dingli, David</creator><creatorcontrib>Sridharan, Meera ; Highsmith, W. Edward ; Kurtin, Paul J. ; Zimmermann, Michael T. ; Theis, Jason D. ; Dasari, Surendra ; Dingli, David</creatorcontrib><description>Hereditary amyloidosis represents a group of diseases in which mutant proteins are deposited in various organs leading to their dysfunction. Correct identification of the amyloid-causing protein is critical because this will determine the optimal therapy for the patient. The most common type of hereditary amyloidosis is due to mutant transthyretin (ATTRm) deposition and often presents with heart failure or peripheral neuropathy. We report the first known case of a patient who had amyloidosis both due to a mutant transthyretin (p.Val122Ile) and due to a novel variant in the gelsolin gene (p.Ala578Pro). Both mutant proteins were identified by mass spectrometry analysis of amyloid deposits as well as sequencing of the genes. Molecular dynamic simulations suggest that the gelsolin p.Ala578Pro variant is likely amyloidogenic.</description><identifier>ISSN: 0025-6196</identifier><identifier>EISSN: 1942-5546</identifier><identifier>DOI: 10.1016/j.mayocp.2018.06.016</identifier><identifier>PMID: 30093168</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Amyloidogenesis ; Amyloidosis ; Apolipoproteins ; Biopsy ; Cardiomyopathy ; Care and treatment ; Cellular proteins ; Development and progression ; Gelsolin ; Genes ; Genetic aspects ; Health aspects ; Heart failure ; Mass spectrometry ; Mutation ; Novels ; Peptides ; Peripheral neuropathy ; Proteins ; Scientific imaging ; Simulation ; Spectroscopy ; Systemic diseases</subject><ispartof>Mayo Clinic proceedings, 2018-11, Vol.93 (11), p.1678-1682</ispartof><rights>2018 Mayo Foundation for Medical Education and Research</rights><rights>Copyright © 2018 Mayo Foundation for Medical Education and Research. Published by Elsevier Inc. All rights reserved.</rights><rights>COPYRIGHT 2018 Frontline Medical Communications Inc.</rights><rights>Copyright Mayo Foundation for Medical Education and Research Nov 2018</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c506t-2cf3e1970e6683e055fb1b57f94f302b43886722b78ad6d89c7b51b308bb1a943</citedby><cites>FETCH-LOGICAL-c506t-2cf3e1970e6683e055fb1b57f94f302b43886722b78ad6d89c7b51b308bb1a943</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/30093168$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sridharan, Meera</creatorcontrib><creatorcontrib>Highsmith, W. 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We report the first known case of a patient who had amyloidosis both due to a mutant transthyretin (p.Val122Ile) and due to a novel variant in the gelsolin gene (p.Ala578Pro). Both mutant proteins were identified by mass spectrometry analysis of amyloid deposits as well as sequencing of the genes. Molecular dynamic simulations suggest that the gelsolin p.Ala578Pro variant is likely amyloidogenic.</description><subject>Amyloidogenesis</subject><subject>Amyloidosis</subject><subject>Apolipoproteins</subject><subject>Biopsy</subject><subject>Cardiomyopathy</subject><subject>Care and treatment</subject><subject>Cellular proteins</subject><subject>Development and progression</subject><subject>Gelsolin</subject><subject>Genes</subject><subject>Genetic aspects</subject><subject>Health aspects</subject><subject>Heart failure</subject><subject>Mass spectrometry</subject><subject>Mutation</subject><subject>Novels</subject><subject>Peptides</subject><subject>Peripheral neuropathy</subject><subject>Proteins</subject><subject>Scientific imaging</subject><subject>Simulation</subject><subject>Spectroscopy</subject><subject>Systemic diseases</subject><issn>0025-6196</issn><issn>1942-5546</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kVGL1DAUhYMo7rj6D0QKwuJL603SpMmLUBadXVh0kREfQ5qmToa2GZN0Yf69Wbor6oMEEjh8J_dwD0KvMVQYMH9_qCZ98uZYEcCiAl5l8QnaYFmTkrGaP0UbAMJKjiU_Qy9iPABAI2X9HJ1RAEkxFxu0bYtbnZydU_HdpX1xZYPtXdLhVLS73ddCz32hi8_-zo5Fu83XsWpHzRpxG3zRTqfRu95HF1-iZ4Meo3318J6jb58-7i6vypsv2-vL9qY0DHgqiRmoxbIBy7mgFhgbOtyxZpD1QIF0NRWCN4R0jdA974U0TcdwR0F0Hdaypufo3frvMfifi41JTS4aO456tn6JioBomCRY0oy-_Qc9-CXMOZ0iuBYsBxAiU9VK_dCjVW4efAra5NPbyRk_28FlvWW85sAwJdlw8Ydhb_WY9tGPS3J-jn-D9Qqa4GMMdlDH4Ka8WYVB3VeoDmqtUN1XqICrLGbbm4fYSzfZ_rfpsbMMfFgBm_d852xQ0eQCTe4tWJNU793_J_wC4Hipag</recordid><startdate>201811</startdate><enddate>201811</enddate><creator>Sridharan, Meera</creator><creator>Highsmith, W. 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| source | Alma/SFX Local Collection |
| subjects | Amyloidogenesis Amyloidosis Apolipoproteins Biopsy Cardiomyopathy Care and treatment Cellular proteins Development and progression Gelsolin Genes Genetic aspects Health aspects Heart failure Mass spectrometry Mutation Novels Peptides Peripheral neuropathy Proteins Scientific imaging Simulation Spectroscopy Systemic diseases |
| title | A Patient With Hereditary ATTR and a Novel AGel p.Ala578Pro Amyloidosis |
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