{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T01:46:29Z","timestamp":1793324789661,"version":"4.5.0"},"reference-count":121,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2022,12,5]],"date-time":"2022-12-05T00:00:00Z","timestamp":1670198400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Cardiovasc. Med."],"abstract":"<jats:p>Since the mid-nineteenth century pathology has followed the convoluted story of amyloidosis, recognized its morphology in tissues and made identification possible using specific staining. Since then, pathology studies have made a significant contribution and advanced knowledge of the disease, so providing valuable information on the pathophysiology of amyloid aggregation and opening the way to clinical studies and non-invasive diagnostic techniques. As amyloidosis is a heterogeneous disease with various organ and tissue deposition patterns, histology evaluation, far from offering a simple yes\/no indication of amyloid presence, can provide a wide spectrum of qualitative and quantitative information related to and changing with the etiology of the disease, the comorbidities and the clinical characteristics of patients. With the exception of cardiac transthyretin related amyloidosis cases, which today can be diagnosed using non-biopsy algorithms when stringent clinical criteria are met, tissue biopsy is still an essential tool for a definitive diagnosis in doubtful cases and also to define etiology by typing amyloid fibrils. This review describes the histologic approach to amyloidosis today and the current role of tissue screening biopsy or targeted organ biopsy protocols in the light of present diagnostic algorithms and various clinical situations, with particular focus on endomyocardial and renal biopsies. Special attention is given to techniques for typing amyloid fibril proteins, necessary for the new therapies available today for cardiac transthyretin related amyloidosis and to avoid patients receiving inappropriate chemotherapy in presence of plasma cell dyscrasia unrelated to amyloidosis. As the disease is still burdened with high mortality, the role of tissue biopsy in early diagnosis to assure prompt treatment is also mentioned.<\/jats:p>","DOI":"10.3389\/fcvm.2022.1081098","type":"journal-article","created":{"date-parts":[[2022,12,5]],"date-time":"2022-12-05T00:22:57Z","timestamp":1670199777000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":36,"title":["Amyloidosis: What does pathology offer? The evolving field of tissue biopsy"],"prefix":"10.3389","volume":"9","author":[{"given":"Mattia","family":"Riefolo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matteo","family":"Conti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Simone","family":"Longhi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benedetta","family":"Fabbrizio","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ornella","family":"Leone","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2022,12,5]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1080\/13506129.2020.1835263","article-title":"Amyloid nomenclature 2020: update and recommendations by the international society of amyloidosis (ISA) nomenclature committee.","volume":"27","author":"Benson","year":"2020","journal-title":"Amyloid."},{"key":"B2","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1007\/BF01930815","article-title":"Ueber eine im Gehirn und R\u00fcckenmark des Menschen aufgefundene Substanz mit der chemischen Reaction der Cellulose.","volume":"6","author":"Virchow","year":"1854","journal-title":"Arch Pathol Anat Physiol Klin Med."},{"key":"B3","doi-asserted-by":"publisher","first-page":"529","DOI":"10.1046\/j.1365-2141.2001.02999.x","article-title":"Amyloidosis: a convoluted story.","volume":"114","author":"Kyle","year":"2001","journal-title":"Br J Haematol."},{"key":"B4","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1006\/jsbi.2000.4221","article-title":"Review: history of the amyloid fibril.","volume":"130","author":"Sipe","year":"2000","journal-title":"J Struct Biol."},{"key":"B5","first-page":"1010","article-title":"Specific staining of amyloid by Congo red.","volume":"69","author":"Bennhold","year":"1922","journal-title":"Muenchen Med Wochenschr."},{"key":"B6","first-page":"1808","article-title":"Sur les propri\u00e9t\u00e9 optiques de l \u2018amylo\u0131de.","volume":"97","author":"Divry","year":"1927","journal-title":"C R Seances Soc Biol Fil."},{"key":"B7","doi-asserted-by":"publisher","first-page":"BSR20181415","DOI":"10.1042\/BSR20181415","article-title":"Congo red and amyloids: history and relationship.","volume":"39","author":"Yakupova","year":"2019","journal-title":"Biosci Rep."},{"key":"B8","doi-asserted-by":"publisher","first-page":"1202","DOI":"10.1038\/1831202a0","article-title":"Electron microscopic observations on a fibrous component in amyloid of diverse origins.","volume":"183","author":"Cohen","year":"1959","journal-title":"Nature."},{"key":"B9","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1177\/16.11.673","article-title":"X-ray diffraction studies on amyloid filaments.","volume":"16","author":"Eanes","year":"1968","journal-title":"J Histochem Cytochem."},{"key":"B10","doi-asserted-by":"publisher","first-page":"1373","DOI":"10.3181\/00379727-131-34110","article-title":"Characterization of the amyloid fibril as a cross-beta protein.","volume":"131","author":"Bonar","year":"1969","journal-title":"Proc Soc Exp Biol Med."},{"key":"B11","doi-asserted-by":"publisher","first-page":"3487","DOI":"10.1073\/pnas.0915166107","article-title":"Identifying the amylome, proteins capable of forming amyloid-like fibrils.","volume":"107","author":"Goldschmidt","year":"2010","journal-title":"Proc Natl Acad Sci USA."},{"key":"B12","doi-asserted-by":"publisher","first-page":"50869","DOI":"10.3791\/50869","article-title":"Rapid generation of amyloid from native proteins in vitro.","volume":"82","author":"Dorta-Estremera","year":"2013","journal-title":"J Vis Exp."},{"key":"B13","doi-asserted-by":"publisher","first-page":"268","DOI":"10.1111\/joim.13169","article-title":"Systemic amyloidosis from A (AA) to T (ATTR): a review.","volume":"289","author":"Muchtar","year":"2021","journal-title":"J Intern Med."},{"key":"B14","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1080\/13506129.2021.1994386","article-title":"Tissue biopsy for the diagnosis of amyloidosis: experience from some centres.","volume":"29","author":"Benson","year":"2022","journal-title":"Amyloid."},{"key":"B15","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1111\/echo.14245","article-title":"A histopathologic schema to quantify the burden of cardiac amyloidosis: relationship with survival and echocardiographic parameters.","volume":"36","author":"Mehta","year":"2019","journal-title":"Echocardiography."},{"key":"B16","doi-asserted-by":"publisher","first-page":"322","DOI":"10.1159\/000506696","article-title":"The pathology of amyloidosis in classification: a review.","volume":"143","author":"Picken","year":"2020","journal-title":"Acta Haematol."},{"key":"B17","doi-asserted-by":"publisher","first-page":"1852","DOI":"10.1016\/j.mayocp.2020.06.029","article-title":"Amyloid typing by mass spectrometry in clinical practice: a comprehensive review of 16,175 samples.","volume":"95","author":"Dasari","year":"2020","journal-title":"Mayo Clin Proc."},{"key":"B18","doi-asserted-by":"publisher","first-page":"520","DOI":"10.1093\/eurheartj\/ehs123","article-title":"Disease profile and differential diagnosis of hereditary transthyretin-related amyloidosis with exclusively cardiac phenotype: an Italian perspective.","volume":"34","author":"Rapezzi","year":"2013","journal-title":"Eur Heart J."},{"key":"B19","doi-asserted-by":"publisher","first-page":"1017","DOI":"10.1002\/hep.22742","article-title":"American association for the study of liver D. Liver biopsy.","volume":"49","author":"Rockey","year":"2009","journal-title":"Hepatology."},{"key":"B20","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.1681\/ASN.2015060612","article-title":"Mayo clinic\/renal pathology society consensus report on pathologic classification, diagnosis, and reporting of GN.","volume":"27","author":"Sethi","year":"2016","journal-title":"J Am Soc Nephrol."},{"key":"B21","doi-asserted-by":"publisher","first-page":"2404","DOI":"10.1161\/CIRCULATIONAHA.116.021612","article-title":"Nonbiopsy Diagnosis of Cardiac Transthyretin Amyloidosis.","volume":"133","author":"Gillmore","year":"2016","journal-title":"Circulation."},{"key":"B22","doi-asserted-by":"publisher","first-page":"593460","DOI":"10.1155\/2012\/593460","article-title":"Amyloidosis presenting with negative Congo red staining in the setting of high clinical suspicion: a case report.","volume":"2012","author":"Bowen","year":"2012","journal-title":"Case Rep Nephrol."},{"key":"B23","doi-asserted-by":"publisher","first-page":"11","DOI":"10.4103\/1742-6413.82278","article-title":"Detection of amyloid in abdominal fat pad aspirates in early amyloidosis: role of electron microscopy and Congo red stained cell block sections.","volume":"8","author":"Devata","year":"2011","journal-title":"Cytojournal."},{"key":"B24","doi-asserted-by":"publisher","first-page":"24","DOI":"10.4103\/1742-6413.58950","article-title":"Diagnosis and typing of systemic amyloidosis: the role of abdominal fat pad fine needle aspiration biopsy.","volume":"6","author":"Halloush","year":"2009","journal-title":"Cytojournal."},{"key":"B25","first-page":"1","article-title":"Nonspecific green birefringence in Congo red-stained tissues.","volume":"56","author":"Klatskin","year":"1969","journal-title":"Am J Pathol."},{"key":"B26","doi-asserted-by":"publisher","first-page":"208","DOI":"10.1111\/iep.12330","article-title":"Origins of a pervasive, erroneous idea: the \u201cgreen birefringence\u201d of Congo red-stained amyloid.","volume":"100","author":"Howie","year":"2019","journal-title":"Int J Exp Pathol."},{"key":"B27","doi-asserted-by":"publisher","first-page":"317","DOI":"10.1007\/s40120-020-00210-7","article-title":"Transthyretin amyloidosis: update on the clinical spectrum, pathogenesis, and disease-modifying therapies.","volume":"9","author":"Koike","year":"2020","journal-title":"Neurol Ther."},{"key":"B28","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1002\/path.2411","article-title":"Amyloid fibril composition is related to the phenotype of hereditary transthyretin V30M amyloidosis.","volume":"216","author":"Ihse","year":"2008","journal-title":"J Pathol."},{"key":"B29","doi-asserted-by":"publisher","first-page":"142","DOI":"10.3109\/13506129.2013.797890","article-title":"Amyloid fibrils containing fragmented ATTR may be the standard fibril composition in ATTR amyloidosis.","volume":"20","author":"Ihse","year":"2013","journal-title":"Amyloid."},{"key":"B30","doi-asserted-by":"publisher","first-page":"2047","DOI":"10.1161\/CIRCULATIONAHA.104.489187","article-title":"Diagnosis and management of the cardiac amyloidoses.","volume":"112","author":"Falk","year":"2005","journal-title":"Circulation."},{"key":"B31","doi-asserted-by":"publisher","first-page":"e000098","DOI":"10.1161\/JAHA.113.000098","article-title":"Senile systemic amyloidosis: clinical features at presentation and outcome.","volume":"2","author":"Pinney","year":"2013","journal-title":"J Am Heart Assoc."},{"key":"B32","doi-asserted-by":"publisher","first-page":"1203","DOI":"10.1161\/CIRCULATIONAHA.108.843334","article-title":"Systemic cardiac amyloidoses: disease profiles and clinical courses of the 3 main types.","volume":"120","author":"Rapezzi","year":"2009","journal-title":"Circulation."},{"key":"B33","doi-asserted-by":"publisher","first-page":"2361","DOI":"10.1056\/NEJMoa070265","article-title":"Natural history and outcome in systemic AA amyloidosis.","volume":"356","author":"Lachmann","year":"2007","journal-title":"N Engl J Med."},{"key":"B34","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/j.jcmg.2021.06.022","article-title":"Clinical importance of left atrial infiltration in cardiac transthyretin amyloidosis.","volume":"15","author":"Bandera","year":"2022","journal-title":"JACC Cardiovasc Imaging."},{"key":"B35","doi-asserted-by":"publisher","first-page":"99","DOI":"10.3109\/13506129.2012.684810","article-title":"New pathological insights into cardiac amyloidosis: implications for non-invasive diagnosis.","volume":"19","author":"Leone","year":"2012","journal-title":"Amyloid."},{"key":"B36","doi-asserted-by":"publisher","first-page":"1174","DOI":"10.1016\/j.jcmg.2018.07.007","article-title":"Relative left ventricular apical sparing of longitudinal strain in cardiac amyloidosis: is it just amyloid infiltration?.","volume":"12","author":"Rapezzi","year":"2019","journal-title":"JACC Cardiovasc Imaging."},{"key":"B37","doi-asserted-by":"publisher","first-page":"648","DOI":"10.1111\/his.12793","article-title":"Correlation of histomorphological pattern of cardiac amyloid deposition with amyloid type: a histological and proteomic analysis of 108 cases.","volume":"68","author":"Larsen","year":"2016","journal-title":"Histopathology."},{"key":"B38","doi-asserted-by":"publisher","first-page":"2980","DOI":"10.3389\/fimmu.2019.02980","article-title":"Amyloids in site-specific autoimmune reactions and inflammatory responses.","volume":"10","author":"Huang","year":"2019","journal-title":"Front Immunol."},{"key":"B39","doi-asserted-by":"publisher","first-page":"e2213903119","DOI":"10.1073\/pnas.2213903119","article-title":"Do amyloid fibrils induce inflammation, or does inflammation generate amyloid fibrils?.","volume":"119","author":"Rothbard","year":"2022","journal-title":"Proc Natl Acad Sci USA."},{"key":"B40","doi-asserted-by":"publisher","first-page":"751","DOI":"10.1002\/ejhf.1039","article-title":"Intramyocardial inflammation predicts adverse outcome in patients with cardiac AL amyloidosis.","volume":"20","author":"Siegismund","year":"2018","journal-title":"Eur J Heart Fail."},{"key":"B41","doi-asserted-by":"publisher","first-page":"758","DOI":"10.1002\/ejhf.1062","article-title":"Inflammation in cardiac amyloidosis: prognostic marker or therapeutic target?.","volume":"20","author":"Sinagra","year":"2018","journal-title":"Eur J Heart Fail."},{"key":"B42","doi-asserted-by":"publisher","first-page":"378","DOI":"10.1007\/s00395-013-0378-5","article-title":"Stanniocalcin1 is a key mediator of amyloidogenic light chain induced cardiotoxicity.","volume":"108","author":"Guan","year":"2013","journal-title":"Basic Res Cardiol."},{"key":"B43","doi-asserted-by":"publisher","first-page":"11","DOI":"10.3390\/biomedicines7010011","article-title":"Ultrastructure in transthyretin amyloidosis: from pathophysiology to therapeutic insights.","volume":"7","author":"Koike","year":"2019","journal-title":"Biomedicines."},{"key":"B44","doi-asserted-by":"publisher","first-page":"1777","DOI":"10.1111\/echo.13365","article-title":"A rare presentation of cardiac amyloid deposits isolated to intramural vessels.","volume":"33","author":"Clemmensen","year":"2016","journal-title":"Echocardiography."},{"key":"B45","doi-asserted-by":"publisher","first-page":"347","DOI":"10.1016\/j.pcad.2009.11.007","article-title":"Amyloid heart disease.","volume":"52","author":"Falk","year":"2010","journal-title":"Prog Cardiovasc Dis."},{"key":"B46","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1056\/NEJMra023144","article-title":"Molecular mechanisms of amyloidosis.","volume":"349","author":"Merlini","year":"2003","journal-title":"N Engl J Med."},{"key":"B47","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1016\/0002-9149(83)90084-X","article-title":"Cardiac amyloidosis causing cardiac dysfunction: analysis of 54 necropsy patients.","volume":"52","author":"Roberts","year":"1983","journal-title":"Am J Cardiol."},{"key":"B48","doi-asserted-by":"publisher","first-page":"1769","DOI":"10.1016\/j.jacc.2009.12.040","article-title":"Infiltrative cardiovascular diseases: cardiomyopathies that look alike.","volume":"55","author":"Seward","year":"2010","journal-title":"J Am Coll Cardiol."},{"key":"B49","doi-asserted-by":"publisher","first-page":"770","DOI":"10.1093\/ndt\/gfw305","article-title":"Systemic amyloidosis: novel therapies and role of biomarkers.","volume":"32","author":"Nuvolone","year":"2017","journal-title":"Nephrol Dial Transplant."},{"key":"B50","doi-asserted-by":"publisher","first-page":"1198","DOI":"10.1097\/PAS.0b013e3181abdfa7","article-title":"Prevalence and origin of amyloid in kidney biopsies.","volume":"33","author":"von Hutten","year":"2009","journal-title":"Am J Surg Pathol."},{"key":"B51","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1016\/j.path.2014.04.006","article-title":"Renal amyloidosis.","volume":"7","author":"Mohamed","year":"2014","journal-title":"Surg Pathol Clin."},{"key":"B52","doi-asserted-by":"publisher","first-page":"816","DOI":"10.1038\/ki.2010.9","article-title":"Prevalence and morphology of leukocyte chemotactic factor 2-associated amyloid in renal biopsies.","volume":"77","author":"Larsen","year":"2010","journal-title":"Kidney Int."},{"key":"B53","doi-asserted-by":"publisher","first-page":"3458","DOI":"10.1681\/ASN.2006050460","article-title":"Amyloidosis-associated kidney disease.","volume":"17","author":"Dember","year":"2006","journal-title":"J Am Soc Nephrol."},{"key":"B54","doi-asserted-by":"publisher","first-page":"2877","DOI":"10.1093\/ndt\/gfq831","article-title":"Renal amyloidosis revisited: amyloid distribution, dynamics and biochemical type.","volume":"26","author":"Hopfer","year":"2011","journal-title":"Nephrol Dial Transplant."},{"key":"B55","doi-asserted-by":"publisher","first-page":"1005","DOI":"10.1016\/j.kint.2019.05.027","article-title":"The sensitivity and specificity of the routine kidney biopsy immunofluorescence panel are inferior to diagnosing renal immunoglobulin-derived amyloidosis by mass spectrometry.","volume":"96","author":"Gonzalez Suarez","year":"2019","journal-title":"Kidney Int."},{"key":"B56","doi-asserted-by":"publisher","first-page":"205","DOI":"10.1080\/13506129.2017.1360272","article-title":"Novel pathologic scoring tools predict end-stage kidney disease in light chain (AL) amyloidosis.","volume":"24","author":"Rubinstein","year":"2017","journal-title":"Amyloid."},{"key":"B57","doi-asserted-by":"publisher","first-page":"855","DOI":"10.1093\/ckj\/sfaa019","article-title":"Renal amyloidosis: validation of a proposed histological scoring system in an independent cohort.","volume":"14","author":"Hoelbeek","year":"2021","journal-title":"Clin Kidney J."},{"key":"B58","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1002\/cjp2.126","article-title":"The complementary role of histology and proteomics for diagnosis and typing of systemic amyloidosis.","volume":"5","author":"Rezk","year":"2019","journal-title":"J Pathol Clin Res."},{"key":"B59","doi-asserted-by":"publisher","first-page":"488","DOI":"10.1182\/blood-2011-06-358507","article-title":"Immunohistochemistry in the classification of systemic forms of amyloidosis: a systematic investigation of 117 patients.","volume":"119","author":"Schonland","year":"2012","journal-title":"Blood."},{"key":"B60","doi-asserted-by":"publisher","first-page":"e0256306","DOI":"10.1371\/journal.pone.0256306","article-title":"Immunohistochemical typing of amyloid in fixed paraffin-embedded samples by an automatic procedure: comparison with immunofluorescence data on fresh-frozen tissue.","volume":"16","author":"Barreca","year":"2021","journal-title":"PLoS One."},{"key":"B61","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1080\/13506129.2017.1292905","article-title":"Sensitive and reliable immunohistochemical typing of 21 different amyloid classes in 782 patients using amyloid-type specific antibodies directed against the amyloidotic conformation. With comments on the gold standard debate.","volume":"24","author":"Linke","year":"2017","journal-title":"Amyloid."},{"key":"B62","doi-asserted-by":"publisher","first-page":"661","DOI":"10.1136\/jclinpath-2014-202231","article-title":"Value of antibodies to free light chains in immunoperoxidase studies of renal biopsies.","volume":"67","author":"Owen-Casey","year":"2014","journal-title":"J Clin Pathol."},{"key":"B63","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1097\/00000478-200606000-00002","article-title":"Immunohistochemical classification of amyloid in surgical pathology revisited.","volume":"30","author":"Kebbel","year":"2006","journal-title":"Am J Surg Pathol."},{"key":"B64","doi-asserted-by":"publisher","first-page":"385","DOI":"10.1016\/j.jaip.2019.05.052","article-title":"Diagnostic accuracy of T2 biomarkers for the prediction of airway eosinophilia in treated smoking asthmatic patients with loss of asthma control.","volume":"8","author":"Papathanasiou","year":"2020","journal-title":"J Allergy Clin Immunol Pract."},{"key":"B65","doi-asserted-by":"publisher","first-page":"e000364","DOI":"10.1161\/JAHA.111.000364","article-title":"Updates in cardiac amyloidosis: a review.","volume":"1","author":"Banypersad","year":"2012","journal-title":"J Am Heart Assoc."},{"key":"B66","doi-asserted-by":"publisher","first-page":"1786","DOI":"10.1056\/NEJMoa013354","article-title":"Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis.","volume":"346","author":"Lachmann","year":"2002","journal-title":"N Engl J Med."},{"key":"B67","doi-asserted-by":"publisher","first-page":"1685","DOI":"10.1097\/PAS.0b013e3182263d74","article-title":"Strong transthyretin immunostaining: potential pitfall in cardiac amyloid typing.","volume":"35","author":"Satoskar","year":"2011","journal-title":"Am J Surg Pathol."},{"key":"B68","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1016\/S0344-0338(86)80040-1","article-title":"Characterization of different amyloids with immunological techniques.","volume":"181","author":"Chastonay","year":"1986","journal-title":"Pathol Res Pract."},{"key":"B69","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1016\/j.acthis.2006.03.010","article-title":"Classification of amyloidosis: misdiagnosing by way of incomplete immunohistochemistry and how to prevent it.","volume":"108","author":"Linke","year":"2006","journal-title":"Acta Histochem."},{"key":"B70","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1016\/j.proghi.2012.03.001","article-title":"On typing amyloidosis using immunohistochemistry. Detailled illustrations, review and a note on mass spectrometry.","volume":"47","author":"Linke","year":"2012","journal-title":"Prog Histochem Cytochem."},{"key":"B71","doi-asserted-by":"publisher","first-page":"76","DOI":"10.3109\/13506129.2011.574354027","article-title":"Classification of four chemically different amyloid types in routine endomyocardial biopsies by advanced immunohistochemistry.","volume":"18","author":"Lassner","year":"2011","journal-title":"Amyloid."},{"key":"B72","doi-asserted-by":"publisher","first-page":"314","DOI":"10.1136\/jclinpath-2014-202722","article-title":"A comparison of immunohistochemistry and mass spectrometry for determining the amyloid fibril protein from formalin-fixed biopsy tissue.","volume":"68","author":"Gilbertson","year":"2015","journal-title":"J Clin Pathol."},{"key":"B73","doi-asserted-by":"publisher","first-page":"p. 599","DOI":"10.1007\/978-1-4613-2199-6_75","article-title":"Classification of amyloid syndromes from tissue sections using antibodies against various amyloid fibril proteins: report of 142 cases.","author":"Linke","year":"1986","journal-title":"Amyloidosis."},{"key":"B74","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1146\/annurev-pathol-052016-100200","article-title":"Amyloidosis: insights from proteomics.","volume":"12","author":"Dogan","year":"2017","journal-title":"Annu Rev Pathol."},{"key":"B75","doi-asserted-by":"publisher","first-page":"4957","DOI":"10.1182\/blood-2009-07-230722","article-title":"Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens.","volume":"114","author":"Vrana","year":"2009","journal-title":"Blood."},{"key":"B76","doi-asserted-by":"publisher","first-page":"2352","DOI":"10.1021\/pr4011475","article-title":"Clinical proteome informatics workbench detects pathogenic mutations in hereditary amyloidoses.","volume":"13","author":"Dasari","year":"2014","journal-title":"J Proteome Res."},{"key":"B77","doi-asserted-by":"publisher","first-page":"976","DOI":"10.1016\/1044-0305(94)80016-2","article-title":"An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database.","volume":"5","author":"Eng","year":"1994","journal-title":"J Am Soc Mass Spectrom."},{"key":"B78","doi-asserted-by":"publisher","first-page":"768","DOI":"10.1021\/ac0258709","article-title":"A method for assessing the statistical significance of mass spectrometry-based protein identifications using general scoring schemes.","volume":"75","author":"Fenyo","year":"2003","journal-title":"Anal Chem."},{"key":"B79","doi-asserted-by":"publisher","first-page":"3551","DOI":"10.1002\/(SICI)1522-2683(19991201)20:18<3551::AID-ELPS3551>3.0.CO;2-2","article-title":"Probability-based protein identification by searching sequence databases using mass spectrometry data.","volume":"20","author":"Perkins","year":"1999","journal-title":"Electrophoresis."},{"key":"B80","doi-asserted-by":"publisher","first-page":"581374","DOI":"10.3389\/fnagi.2020.581374","article-title":"Molecular chaperones: a double-edged sword in neurodegenerative diseases.","volume":"12","author":"Tittelmeier","year":"2020","journal-title":"Front Aging Neurosci."},{"key":"B81","doi-asserted-by":"publisher","first-page":"3155","DOI":"10.1021\/acs.biochem.9b00311","article-title":"Mechanistic insights into the early events in the aggregation of immunoglobulin light chains.","volume":"58","author":"Misra","year":"2019","journal-title":"Biochemistry."},{"key":"B82","doi-asserted-by":"publisher","first-page":"e2000079","DOI":"10.1002\/prca.202000079","article-title":"MALDI mass spectrometry imaging unravels organ and amyloid-type specific peptide signatures in pulmonary and gastrointestinal amyloidosis.","volume":"15","author":"Schurmann","year":"2021","journal-title":"Proteomics Clin Appl."},{"key":"B83","doi-asserted-by":"publisher","first-page":"921","DOI":"10.1515\/cclm-2015-0938","article-title":"Free light chain testing for the diagnosis, monitoring and prognostication of AL amyloidosis.","volume":"54","author":"Mollee","year":"2016","journal-title":"Clin Chem Lab Med."},{"key":"B84","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1016\/j.clinms.2018.02.001","article-title":"A targeted proteomics approach to amyloidosis typing.","volume":"7","author":"Conti","year":"2018","journal-title":"Clin Mass Spectrom."},{"key":"B85","doi-asserted-by":"publisher","first-page":"1700236","DOI":"10.1002\/pmic.201700236","article-title":"MALDI mass spectrometry imaging: a novel tool for the identification and classification of amyloidosis.","volume":"17","author":"Winter","year":"2017","journal-title":"Proteomics."},{"key":"B86","doi-asserted-by":"publisher","first-page":"772","DOI":"10.1369\/0022155415595264","article-title":"MALDI-mass spectrometry imaging identifies vitronectin as a common constituent of amyloid deposits.","volume":"63","author":"Winter","year":"2015","journal-title":"J Histochem Cytochem."},{"key":"B87","doi-asserted-by":"publisher","first-page":"e1700353","DOI":"10.1002\/pmic.201700353","article-title":"Proteomics with mass spectrometry imaging: beyond amyloid typing.","volume":"18","author":"Lavatelli","year":"2018","journal-title":"Proteomics."},{"key":"B88","doi-asserted-by":"publisher","first-page":"9826","DOI":"10.1021\/acs.analchem.1c01377","article-title":"Mass spectrometry imaging of lipids with isomer resolution using high-pressure ozone-induced dissociation.","volume":"93","author":"Claes","year":"2021","journal-title":"Anal Chem."},{"key":"B89","doi-asserted-by":"publisher","first-page":"345","DOI":"10.1007\/978-1-4939-7592-1_26","article-title":"Mass spectrometry imaging of metabolites.","volume":"1730","author":"Balluff","year":"2018","journal-title":"Methods Mol Biol."},{"key":"B90","doi-asserted-by":"publisher","first-page":"7080","DOI":"10.1039\/D2SC01278B","article-title":"Molecular mechanisms of amyloid formation in living systems.","volume":"13","author":"Sinnige","year":"2022","journal-title":"Chem Sci."},{"key":"B91","doi-asserted-by":"publisher","first-page":"157","DOI":"10.3109\/13506129709014380","article-title":"Light and electron microscopy immunohistochemical characterization of amyloid deposits.","volume":"4","author":"Arbustini","year":"1997","journal-title":"Amyloid."},{"key":"B92","doi-asserted-by":"publisher","first-page":"108","DOI":"10.3109\/13506120208995243","article-title":"Electron and immuno-electron microscopy of abdominal fat identifies and characterizes amyloid fibrils in suspected cardiac amyloidosis.","volume":"9","author":"Arbustini","year":"2002","journal-title":"Amyloid."},{"key":"B93","doi-asserted-by":"publisher","first-page":"2239","DOI":"10.1182\/blood-2014-11-609883","article-title":"A practical approach to the diagnosis of systemic amyloidoses.","volume":"125","author":"Fern\u00e1ndez de Larrea","year":"2015","journal-title":"Blood."},{"key":"B94","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1080\/13506129.2019.1688289","article-title":"Immunoelectron microscopy and mass spectrometry for classification of amyloid deposits.","volume":"27","author":"Abildgaard","year":"2020","journal-title":"Amyloid."},{"key":"B95","doi-asserted-by":"publisher","first-page":"64","DOI":"10.3109\/13506129.2011.574354023","article-title":"Mass spectrometry-based proteomics as a diagnostic tool when immunoelectron microscopy fails in typing amyloid deposits.","volume":"18","author":"Lavatelli","year":"2011","journal-title":"Amyloid."},{"key":"B96","doi-asserted-by":"publisher","first-page":"697","DOI":"10.1093\/ajcp\/70.4.697","article-title":"A reliable method for electron microscopic examination of specific areas from paraffin-embedded tissue mounted on glass slides.","volume":"70","author":"Gonzalez-Angulo","year":"1978","journal-title":"Am J Clin Pathol."},{"key":"B97","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1080\/13506129.2018.1436048","article-title":"Monoclonal gammopathy of undetermined significance in systemic transthyretin amyloidosis (ATTR).","volume":"25","author":"Phull","year":"2018","journal-title":"Amyloid."},{"key":"B98","doi-asserted-by":"publisher","first-page":"312","DOI":"10.1159\/000508022","article-title":"Confirming the diagnosis of amyloidosis.","volume":"143","author":"Wisniowski","year":"2020","journal-title":"Acta Haematol."},{"key":"B99","doi-asserted-by":"publisher","first-page":"1076","DOI":"10.1016\/j.jacc.2005.05.073","article-title":"Noninvasive etiologic diagnosis of cardiac amyloidosis using 99mTc-3,3-diphosphono-1,2-propanodicarboxylic acid scintigraphy.","volume":"46","author":"Perugini","year":"2005","journal-title":"J Am Coll Cardiol."},{"key":"B100","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1002\/ejhf.2140","article-title":"Diagnosis and treatment of cardiac amyloidosis. A position statement of the European society of cardiology working group on myocardial and pericardial diseases.","volume":"23","author":"Garcia-Pavia","year":"2021","journal-title":"Eur J Heart Fail."},{"key":"B101","doi-asserted-by":"publisher","first-page":"1700","DOI":"10.1002\/ejhf.2606","article-title":"Progression of echocardiographic parameters and prognosis in transthyretin cardiac amyloidosis.","volume":"24","author":"Chacko","year":"2022","journal-title":"Eur J Heart Fail."},{"key":"B102","doi-asserted-by":"publisher","first-page":"e7","DOI":"10.1161\/CIR.0000000000000792","article-title":"Cardiac amyloidosis: evolving diagnosis and management: a scientific statement from the American heart association.","volume":"142","author":"Kittleson","year":"2020","journal-title":"Circulation."},{"key":"B103","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1080\/13506129.2021.2002841","article-title":"Guidelines for high dose chemotherapy and stem cell transplantation for systemic AL amyloidosis: EHA-ISA working group guidelines.","volume":"29","author":"Sanchorawala","year":"2022","journal-title":"Amyloid."},{"key":"B104","doi-asserted-by":"publisher","first-page":"545","DOI":"10.1080\/07853890.2017.1304649","article-title":"Overuse of organ biopsies in immunoglobulin light chain amyloidosis (AL): the consequence of failure of early recognition.","volume":"49","author":"Muchtar","year":"2017","journal-title":"Ann Med."},{"key":"B105","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1111\/imj.12288","article-title":"How to diagnose amyloidosis.","volume":"44","author":"Mollee","year":"2014","journal-title":"Intern Med J."},{"key":"B106","doi-asserted-by":"publisher","first-page":"1723","DOI":"10.1016\/j.amjcard.2014.02.030","article-title":"Yield of noncardiac biopsy for the diagnosis of transthyretin cardiac amyloidosis.","volume":"113","author":"Fine","year":"2014","journal-title":"Am J Cardiol."},{"key":"B107","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1016\/j.humpath.2017.11.001","article-title":"Abdominal fat pad excisional biopsy for the diagnosis and typing of systemic amyloidosis.","volume":"72","author":"Garcia","year":"2018","journal-title":"Hum Pathol."},{"key":"B108","doi-asserted-by":"publisher","first-page":"929","DOI":"10.1001\/archinte.148.4.929","article-title":"Utility of subcutaneous fat aspiration for the diagnosis of systemic amyloidosis (immunoglobulin light chain).","volume":"148","author":"Gertz","year":"1988","journal-title":"Arch Intern Med."},{"key":"B109","doi-asserted-by":"publisher","first-page":"1905","DOI":"10.1093\/eurheartj\/ehx047","article-title":"Diagnostic sensitivity of abdominal fat aspiration in cardiac amyloidosis.","volume":"38","author":"Quarta","year":"2017","journal-title":"Eur Heart J."},{"key":"B110","doi-asserted-by":"publisher","first-page":"2015","DOI":"10.1002\/art.21902","article-title":"Diagnostic accuracy of subcutaneous abdominal fat tissue aspiration for detecting systemic amyloidosis and its utility in clinical practice.","volume":"54","author":"van","year":"2006","journal-title":"Arthritis Rheum."},{"key":"B111","doi-asserted-by":"publisher","first-page":"232","DOI":"10.3109\/13506120903421850","article-title":"Usefulness of labial salivary gland biopsy in familial amyloid polyneuropathy Portuguese type.","volume":"16","author":"Do Amaral","year":"2009","journal-title":"Amyloid."},{"key":"B112","doi-asserted-by":"publisher","first-page":"691","DOI":"10.1002\/art.1780360518","article-title":"Labial salivary gland biopsy is a reliable test for the diagnosis of primary and secondary amyloidosis. A prospective clinical and immunohistologic study in 59 patients.","volume":"36","author":"Hachulla","year":"1993","journal-title":"Arthritis Rheum."},{"key":"B113","doi-asserted-by":"publisher","first-page":"279","DOI":"10.1007\/s00277-015-2549-y","article-title":"Labial salivary gland biopsy for diagnosing immunoglobulin light chain amyloidosis: a retrospective analysis.","volume":"95","author":"Suzuki","year":"2016","journal-title":"Ann Hematol."},{"key":"B114","doi-asserted-by":"publisher","first-page":"501","DOI":"10.1097\/00000441-196605000-00001","article-title":"Value of rectal biopsy in the diagnosis of primary systemic amyloidosis.","volume":"251","author":"Kyle","year":"1966","journal-title":"Am J Med Sci."},{"key":"B115","doi-asserted-by":"publisher","first-page":"44","DOI":"10.1038\/s41408-018-0080-9","article-title":"Immunoglobulin light chain amyloidosis diagnosis and treatment algorithm 2018.","volume":"8","author":"Gertz","year":"2018","journal-title":"Blood Cancer J."},{"key":"B116","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1159\/000495455","article-title":"Recent advances in the diagnosis, risk stratification, and management of systemic light-chain amyloidosis.","volume":"141","author":"Vaxman","year":"2019","journal-title":"Acta Haematol."},{"key":"B117","doi-asserted-by":"publisher","first-page":"170","DOI":"10.1111\/bjh.14205","article-title":"Natural history of amyloidosis isolated to fat and bone marrow aspirate.","volume":"179","author":"Chakraborty","year":"2017","journal-title":"Br J Haematol."},{"key":"B118","doi-asserted-by":"publisher","first-page":"507","DOI":"10.1002\/ejhf.1742","article-title":"Carpal tunnel syndrome in cardiac amyloidosis: implications for early diagnosis and prognostic role across the spectrum of aetiologies.","volume":"22","author":"Milandri","year":"2020","journal-title":"Eur J Heart Fail."},{"key":"B119","doi-asserted-by":"publisher","first-page":"2040","DOI":"10.1016\/j.jacc.2018.07.092","article-title":"Tenosynovial and cardiac amyloidosis in patients undergoing carpal tunnel release.","volume":"72","author":"Sperry","year":"2018","journal-title":"J Am Coll Cardiol."},{"key":"B120","doi-asserted-by":"publisher","first-page":"338","DOI":"10.1253\/circrep.CR-21-0046","article-title":"Tenosynovial and cardiac transthyretin amyloidosis in Japanese patients undergoing carpal tunnel release.","volume":"3","author":"Sugiura","year":"2021","journal-title":"Circ Rep."},{"key":"B121","doi-asserted-by":"publisher","first-page":"2109","DOI":"10.1007\/s00415-019-09688-0","article-title":"Expert consensus recommendations to improve diagnosis of ATTR amyloidosis with polyneuropathy.","volume":"268","author":"Adams","year":"2021","journal-title":"J Neurol."}],"container-title":["Frontiers in Cardiovascular Medicine"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fcvm.2022.1081098\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,12,5]],"date-time":"2022-12-05T00:23:02Z","timestamp":1670199782000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fcvm.2022.1081098\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,12,5]]},"references-count":121,"alternative-id":["10.3389\/fcvm.2022.1081098"],"URL":"https:\/\/doi.org\/10.3389\/fcvm.2022.1081098","relation":{},"ISSN":["2297-055X"],"issn-type":[{"value":"2297-055X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,12,5]]},"article-number":"1081098"}}