Circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist
Cardiac amyloidosis (CA) is due to extracellular myocardial deposition of misfolded proteins resulting in severe cardiac dysfunction and death. The precursors of amyloid fibrils, able of determining a relevant cardiac infiltration, are immunoglobulin-free light chains (AL amyloidosis) and transthyre...
Ausführliche Beschreibung
Autor*in: |
Perfetto, Federico [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2022 |
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Schlagwörter: |
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Anmerkung: |
© The Author(s) 2022 |
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Übergeordnetes Werk: |
Enthalten in: Internal and emergency medicine - Milan : Springer Milan, 2006, 17(2022), 4 vom: 24. März, Seite 957-969 |
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Übergeordnetes Werk: |
volume:17 ; year:2022 ; number:4 ; day:24 ; month:03 ; pages:957-969 |
Links: |
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DOI / URN: |
10.1007/s11739-022-02958-2 |
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Katalog-ID: |
SPR047112344 |
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520 | |a Cardiac amyloidosis (CA) is due to extracellular myocardial deposition of misfolded proteins resulting in severe cardiac dysfunction and death. The precursors of amyloid fibrils, able of determining a relevant cardiac infiltration, are immunoglobulin-free light chains (AL amyloidosis) and transthyretin (TTR) (both wild and mutated types). The diagnosis of amyloidosis represents a challenge for the clinician given its rarity and its protean clinical presentation, thus an early diagnosis remains a cornerstone for the prognosis of these patients, also in light of the growing available treatments. There is great interest in identifying and applying biomarkers to help diagnose, inform prognosis, guide therapy, and serve as surrogate endpoints in these patients. In AL amyloidosis, biomarkers such as free light chains, natriuretic peptides and troponins are the most extensively studied and validated; they have proved useful in risk stratification, guiding treatment choice and monitoring hematological and organ response. A similar biomarker-based prognostic score is also proposed for ATTR amyloidosis, although studies are small and need to be validated for wild-type and mutant forms. Graphical abstract | ||
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10.1007/s11739-022-02958-2 doi (DE-627)SPR047112344 (SPR)s11739-022-02958-2-e DE-627 ger DE-627 rakwb eng Perfetto, Federico verfasserin (orcid)0000-0003-0276-8331 aut Circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2022 Cardiac amyloidosis (CA) is due to extracellular myocardial deposition of misfolded proteins resulting in severe cardiac dysfunction and death. The precursors of amyloid fibrils, able of determining a relevant cardiac infiltration, are immunoglobulin-free light chains (AL amyloidosis) and transthyretin (TTR) (both wild and mutated types). The diagnosis of amyloidosis represents a challenge for the clinician given its rarity and its protean clinical presentation, thus an early diagnosis remains a cornerstone for the prognosis of these patients, also in light of the growing available treatments. There is great interest in identifying and applying biomarkers to help diagnose, inform prognosis, guide therapy, and serve as surrogate endpoints in these patients. In AL amyloidosis, biomarkers such as free light chains, natriuretic peptides and troponins are the most extensively studied and validated; they have proved useful in risk stratification, guiding treatment choice and monitoring hematological and organ response. A similar biomarker-based prognostic score is also proposed for ATTR amyloidosis, although studies are small and need to be validated for wild-type and mutant forms. Graphical abstract Transthyretin (dpeaa)DE-He213 NT-proBNP (dpeaa)DE-He213 Troponin (dpeaa)DE-He213 Free light chains (dpeaa)DE-He213 AL cardiac amyloidosis (dpeaa)DE-He213 ATTR cardiac amyloidosis (dpeaa)DE-He213 Zampieri, Mattia (orcid)0000-0002-1140-134X aut Fumagalli, Carlo (orcid)0000-0001-7963-5049 aut Allinovi, Marco (orcid)0000-0001-9949-3543 aut Cappelli, Francesco (orcid)0000-0002-1622-0732 aut Enthalten in Internal and emergency medicine Milan : Springer Milan, 2006 17(2022), 4 vom: 24. März, Seite 957-969 (DE-627)538216425 (DE-600)2378342-4 1970-9366 nnns volume:17 year:2022 number:4 day:24 month:03 pages:957-969 https://dx.doi.org/10.1007/s11739-022-02958-2 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 17 2022 4 24 03 957-969 |
spelling |
10.1007/s11739-022-02958-2 doi (DE-627)SPR047112344 (SPR)s11739-022-02958-2-e DE-627 ger DE-627 rakwb eng Perfetto, Federico verfasserin (orcid)0000-0003-0276-8331 aut Circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2022 Cardiac amyloidosis (CA) is due to extracellular myocardial deposition of misfolded proteins resulting in severe cardiac dysfunction and death. The precursors of amyloid fibrils, able of determining a relevant cardiac infiltration, are immunoglobulin-free light chains (AL amyloidosis) and transthyretin (TTR) (both wild and mutated types). The diagnosis of amyloidosis represents a challenge for the clinician given its rarity and its protean clinical presentation, thus an early diagnosis remains a cornerstone for the prognosis of these patients, also in light of the growing available treatments. There is great interest in identifying and applying biomarkers to help diagnose, inform prognosis, guide therapy, and serve as surrogate endpoints in these patients. In AL amyloidosis, biomarkers such as free light chains, natriuretic peptides and troponins are the most extensively studied and validated; they have proved useful in risk stratification, guiding treatment choice and monitoring hematological and organ response. A similar biomarker-based prognostic score is also proposed for ATTR amyloidosis, although studies are small and need to be validated for wild-type and mutant forms. Graphical abstract Transthyretin (dpeaa)DE-He213 NT-proBNP (dpeaa)DE-He213 Troponin (dpeaa)DE-He213 Free light chains (dpeaa)DE-He213 AL cardiac amyloidosis (dpeaa)DE-He213 ATTR cardiac amyloidosis (dpeaa)DE-He213 Zampieri, Mattia (orcid)0000-0002-1140-134X aut Fumagalli, Carlo (orcid)0000-0001-7963-5049 aut Allinovi, Marco (orcid)0000-0001-9949-3543 aut Cappelli, Francesco (orcid)0000-0002-1622-0732 aut Enthalten in Internal and emergency medicine Milan : Springer Milan, 2006 17(2022), 4 vom: 24. März, Seite 957-969 (DE-627)538216425 (DE-600)2378342-4 1970-9366 nnns volume:17 year:2022 number:4 day:24 month:03 pages:957-969 https://dx.doi.org/10.1007/s11739-022-02958-2 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 17 2022 4 24 03 957-969 |
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10.1007/s11739-022-02958-2 doi (DE-627)SPR047112344 (SPR)s11739-022-02958-2-e DE-627 ger DE-627 rakwb eng Perfetto, Federico verfasserin (orcid)0000-0003-0276-8331 aut Circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2022 Cardiac amyloidosis (CA) is due to extracellular myocardial deposition of misfolded proteins resulting in severe cardiac dysfunction and death. The precursors of amyloid fibrils, able of determining a relevant cardiac infiltration, are immunoglobulin-free light chains (AL amyloidosis) and transthyretin (TTR) (both wild and mutated types). The diagnosis of amyloidosis represents a challenge for the clinician given its rarity and its protean clinical presentation, thus an early diagnosis remains a cornerstone for the prognosis of these patients, also in light of the growing available treatments. There is great interest in identifying and applying biomarkers to help diagnose, inform prognosis, guide therapy, and serve as surrogate endpoints in these patients. In AL amyloidosis, biomarkers such as free light chains, natriuretic peptides and troponins are the most extensively studied and validated; they have proved useful in risk stratification, guiding treatment choice and monitoring hematological and organ response. A similar biomarker-based prognostic score is also proposed for ATTR amyloidosis, although studies are small and need to be validated for wild-type and mutant forms. Graphical abstract Transthyretin (dpeaa)DE-He213 NT-proBNP (dpeaa)DE-He213 Troponin (dpeaa)DE-He213 Free light chains (dpeaa)DE-He213 AL cardiac amyloidosis (dpeaa)DE-He213 ATTR cardiac amyloidosis (dpeaa)DE-He213 Zampieri, Mattia (orcid)0000-0002-1140-134X aut Fumagalli, Carlo (orcid)0000-0001-7963-5049 aut Allinovi, Marco (orcid)0000-0001-9949-3543 aut Cappelli, Francesco (orcid)0000-0002-1622-0732 aut Enthalten in Internal and emergency medicine Milan : Springer Milan, 2006 17(2022), 4 vom: 24. März, Seite 957-969 (DE-627)538216425 (DE-600)2378342-4 1970-9366 nnns volume:17 year:2022 number:4 day:24 month:03 pages:957-969 https://dx.doi.org/10.1007/s11739-022-02958-2 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 17 2022 4 24 03 957-969 |
allfieldsGer |
10.1007/s11739-022-02958-2 doi (DE-627)SPR047112344 (SPR)s11739-022-02958-2-e DE-627 ger DE-627 rakwb eng Perfetto, Federico verfasserin (orcid)0000-0003-0276-8331 aut Circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2022 Cardiac amyloidosis (CA) is due to extracellular myocardial deposition of misfolded proteins resulting in severe cardiac dysfunction and death. The precursors of amyloid fibrils, able of determining a relevant cardiac infiltration, are immunoglobulin-free light chains (AL amyloidosis) and transthyretin (TTR) (both wild and mutated types). The diagnosis of amyloidosis represents a challenge for the clinician given its rarity and its protean clinical presentation, thus an early diagnosis remains a cornerstone for the prognosis of these patients, also in light of the growing available treatments. There is great interest in identifying and applying biomarkers to help diagnose, inform prognosis, guide therapy, and serve as surrogate endpoints in these patients. In AL amyloidosis, biomarkers such as free light chains, natriuretic peptides and troponins are the most extensively studied and validated; they have proved useful in risk stratification, guiding treatment choice and monitoring hematological and organ response. A similar biomarker-based prognostic score is also proposed for ATTR amyloidosis, although studies are small and need to be validated for wild-type and mutant forms. Graphical abstract Transthyretin (dpeaa)DE-He213 NT-proBNP (dpeaa)DE-He213 Troponin (dpeaa)DE-He213 Free light chains (dpeaa)DE-He213 AL cardiac amyloidosis (dpeaa)DE-He213 ATTR cardiac amyloidosis (dpeaa)DE-He213 Zampieri, Mattia (orcid)0000-0002-1140-134X aut Fumagalli, Carlo (orcid)0000-0001-7963-5049 aut Allinovi, Marco (orcid)0000-0001-9949-3543 aut Cappelli, Francesco (orcid)0000-0002-1622-0732 aut Enthalten in Internal and emergency medicine Milan : Springer Milan, 2006 17(2022), 4 vom: 24. März, Seite 957-969 (DE-627)538216425 (DE-600)2378342-4 1970-9366 nnns volume:17 year:2022 number:4 day:24 month:03 pages:957-969 https://dx.doi.org/10.1007/s11739-022-02958-2 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 17 2022 4 24 03 957-969 |
allfieldsSound |
10.1007/s11739-022-02958-2 doi (DE-627)SPR047112344 (SPR)s11739-022-02958-2-e DE-627 ger DE-627 rakwb eng Perfetto, Federico verfasserin (orcid)0000-0003-0276-8331 aut Circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2022 Cardiac amyloidosis (CA) is due to extracellular myocardial deposition of misfolded proteins resulting in severe cardiac dysfunction and death. The precursors of amyloid fibrils, able of determining a relevant cardiac infiltration, are immunoglobulin-free light chains (AL amyloidosis) and transthyretin (TTR) (both wild and mutated types). The diagnosis of amyloidosis represents a challenge for the clinician given its rarity and its protean clinical presentation, thus an early diagnosis remains a cornerstone for the prognosis of these patients, also in light of the growing available treatments. There is great interest in identifying and applying biomarkers to help diagnose, inform prognosis, guide therapy, and serve as surrogate endpoints in these patients. In AL amyloidosis, biomarkers such as free light chains, natriuretic peptides and troponins are the most extensively studied and validated; they have proved useful in risk stratification, guiding treatment choice and monitoring hematological and organ response. A similar biomarker-based prognostic score is also proposed for ATTR amyloidosis, although studies are small and need to be validated for wild-type and mutant forms. Graphical abstract Transthyretin (dpeaa)DE-He213 NT-proBNP (dpeaa)DE-He213 Troponin (dpeaa)DE-He213 Free light chains (dpeaa)DE-He213 AL cardiac amyloidosis (dpeaa)DE-He213 ATTR cardiac amyloidosis (dpeaa)DE-He213 Zampieri, Mattia (orcid)0000-0002-1140-134X aut Fumagalli, Carlo (orcid)0000-0001-7963-5049 aut Allinovi, Marco (orcid)0000-0001-9949-3543 aut Cappelli, Francesco (orcid)0000-0002-1622-0732 aut Enthalten in Internal and emergency medicine Milan : Springer Milan, 2006 17(2022), 4 vom: 24. März, Seite 957-969 (DE-627)538216425 (DE-600)2378342-4 1970-9366 nnns volume:17 year:2022 number:4 day:24 month:03 pages:957-969 https://dx.doi.org/10.1007/s11739-022-02958-2 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 17 2022 4 24 03 957-969 |
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Enthalten in Internal and emergency medicine 17(2022), 4 vom: 24. März, Seite 957-969 volume:17 year:2022 number:4 day:24 month:03 pages:957-969 |
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Enthalten in Internal and emergency medicine 17(2022), 4 vom: 24. März, Seite 957-969 volume:17 year:2022 number:4 day:24 month:03 pages:957-969 |
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Transthyretin NT-proBNP Troponin Free light chains AL cardiac amyloidosis ATTR cardiac amyloidosis |
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Perfetto, Federico @@aut@@ Zampieri, Mattia @@aut@@ Fumagalli, Carlo @@aut@@ Allinovi, Marco @@aut@@ Cappelli, Francesco @@aut@@ |
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The precursors of amyloid fibrils, able of determining a relevant cardiac infiltration, are immunoglobulin-free light chains (AL amyloidosis) and transthyretin (TTR) (both wild and mutated types). The diagnosis of amyloidosis represents a challenge for the clinician given its rarity and its protean clinical presentation, thus an early diagnosis remains a cornerstone for the prognosis of these patients, also in light of the growing available treatments. There is great interest in identifying and applying biomarkers to help diagnose, inform prognosis, guide therapy, and serve as surrogate endpoints in these patients. In AL amyloidosis, biomarkers such as free light chains, natriuretic peptides and troponins are the most extensively studied and validated; they have proved useful in risk stratification, guiding treatment choice and monitoring hematological and organ response. A similar biomarker-based prognostic score is also proposed for ATTR amyloidosis, although studies are small and need to be validated for wild-type and mutant forms. 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author |
Perfetto, Federico |
spellingShingle |
Perfetto, Federico misc Transthyretin misc NT-proBNP misc Troponin misc Free light chains misc AL cardiac amyloidosis misc ATTR cardiac amyloidosis Circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist |
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Circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist Transthyretin (dpeaa)DE-He213 NT-proBNP (dpeaa)DE-He213 Troponin (dpeaa)DE-He213 Free light chains (dpeaa)DE-He213 AL cardiac amyloidosis (dpeaa)DE-He213 ATTR cardiac amyloidosis (dpeaa)DE-He213 |
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misc Transthyretin misc NT-proBNP misc Troponin misc Free light chains misc AL cardiac amyloidosis misc ATTR cardiac amyloidosis |
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Circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist |
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Circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist |
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Perfetto, Federico Zampieri, Mattia Fumagalli, Carlo Allinovi, Marco Cappelli, Francesco |
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title_sort |
circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist |
title_auth |
Circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist |
abstract |
Cardiac amyloidosis (CA) is due to extracellular myocardial deposition of misfolded proteins resulting in severe cardiac dysfunction and death. The precursors of amyloid fibrils, able of determining a relevant cardiac infiltration, are immunoglobulin-free light chains (AL amyloidosis) and transthyretin (TTR) (both wild and mutated types). The diagnosis of amyloidosis represents a challenge for the clinician given its rarity and its protean clinical presentation, thus an early diagnosis remains a cornerstone for the prognosis of these patients, also in light of the growing available treatments. There is great interest in identifying and applying biomarkers to help diagnose, inform prognosis, guide therapy, and serve as surrogate endpoints in these patients. In AL amyloidosis, biomarkers such as free light chains, natriuretic peptides and troponins are the most extensively studied and validated; they have proved useful in risk stratification, guiding treatment choice and monitoring hematological and organ response. A similar biomarker-based prognostic score is also proposed for ATTR amyloidosis, although studies are small and need to be validated for wild-type and mutant forms. Graphical abstract © The Author(s) 2022 |
abstractGer |
Cardiac amyloidosis (CA) is due to extracellular myocardial deposition of misfolded proteins resulting in severe cardiac dysfunction and death. The precursors of amyloid fibrils, able of determining a relevant cardiac infiltration, are immunoglobulin-free light chains (AL amyloidosis) and transthyretin (TTR) (both wild and mutated types). The diagnosis of amyloidosis represents a challenge for the clinician given its rarity and its protean clinical presentation, thus an early diagnosis remains a cornerstone for the prognosis of these patients, also in light of the growing available treatments. There is great interest in identifying and applying biomarkers to help diagnose, inform prognosis, guide therapy, and serve as surrogate endpoints in these patients. In AL amyloidosis, biomarkers such as free light chains, natriuretic peptides and troponins are the most extensively studied and validated; they have proved useful in risk stratification, guiding treatment choice and monitoring hematological and organ response. A similar biomarker-based prognostic score is also proposed for ATTR amyloidosis, although studies are small and need to be validated for wild-type and mutant forms. Graphical abstract © The Author(s) 2022 |
abstract_unstemmed |
Cardiac amyloidosis (CA) is due to extracellular myocardial deposition of misfolded proteins resulting in severe cardiac dysfunction and death. The precursors of amyloid fibrils, able of determining a relevant cardiac infiltration, are immunoglobulin-free light chains (AL amyloidosis) and transthyretin (TTR) (both wild and mutated types). The diagnosis of amyloidosis represents a challenge for the clinician given its rarity and its protean clinical presentation, thus an early diagnosis remains a cornerstone for the prognosis of these patients, also in light of the growing available treatments. There is great interest in identifying and applying biomarkers to help diagnose, inform prognosis, guide therapy, and serve as surrogate endpoints in these patients. In AL amyloidosis, biomarkers such as free light chains, natriuretic peptides and troponins are the most extensively studied and validated; they have proved useful in risk stratification, guiding treatment choice and monitoring hematological and organ response. A similar biomarker-based prognostic score is also proposed for ATTR amyloidosis, although studies are small and need to be validated for wild-type and mutant forms. Graphical abstract © The Author(s) 2022 |
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title_short |
Circulating biomarkers in diagnosis and management of cardiac amyloidosis: a review for internist |
url |
https://dx.doi.org/10.1007/s11739-022-02958-2 |
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author2 |
Zampieri, Mattia Fumagalli, Carlo Allinovi, Marco Cappelli, Francesco |
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Zampieri, Mattia Fumagalli, Carlo Allinovi, Marco Cappelli, Francesco |
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doi_str |
10.1007/s11739-022-02958-2 |
up_date |
2024-07-04T01:55:07.132Z |
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score |
7.397691 |