Citations 88

Prevalence and Burden of Cardiac Amyloidosis in a Population-Based Autopsy Cohort

Circulation | June 8, 2026 | Volume: 153 | Issue: 23 | Pages: 1874-1876

10.1161/circulationaha.126.079522 | PMID 42258576

Current Standards and Perspectives in Proteomics for Cardiac Amyloidosis

Analytical Chemistry | March 4, 2026 | Volume: 98 | Issue: 10 | Pages: 7149-7158

10.1021/acs.analchem.5c06139 | PMID 41777219

Epidermal Growth Factor‐Containing Fibulin‐Like Extracellular Matrix Protein 1 ( EFEMP1 ) Amyloid Elastosis: Report of a Patient and Review of the Literature

Journal of Cutaneous Pathology | November 26, 2025 | Volume: 53 | Issue: 7 | Pages: 571-575

10.1111/cup.70020 | PMID 41292418

Laboratory Workup of Amyloidosis

Archives of Pathology & Laboratory Medicine | November 24, 2025 | Volume: 150 | Issue: 3 | Pages: 179-193

10.5858/arpa.2025-0275-cp | PMID 41277424

Context.— Treatments are available for common forms of systemic amyloidosis that show promise for extending and improving the quality of life for patients. Early diagnosis and accurate identification of amyloid fibril type are crucial for successful treatment, but the diagnosis and workup of amyloidosis is inconsistent among pathologists and laboratories. Thus, the goal of this guideline is to offer recommendations for proper testing and workup for amyloidosis to optimize patient care. Objective.— To establish evidence-based recommendations for appropriate laboratory testing to detect amyloidosis and identify the specific amyloidogenic protein. Design.— The College of American Pathologists convened a panel of experts to develop recommendations following the standards established by the National Academy of Medicine for developing trustworthy clinical practice guidelines. The panel conducted a systematic literature review addressing 6 key questions. Using the Grading of Recommendations Assessment, Development and Evaluation framework, recommendations were created based on the available evidence, certainty of that evidence, and key judgments as defined in the framework. Results.— Four conditional recommendations and 3 good practice statements were established to provide guidance for proper testing and workup of amyloidosis. Conclusions.— This guideline summarizes the available evidence on the diagnosis and workup of systemic amyloidosis in tissue samples, including the challenges and limitations of common approaches and techniques. Recommendations for pathologists and laboratories receiving these samples are provided.
Gallbladder amyloidosis is often unexpected and may have systemic implications

American Journal of Clinical Pathology | August 29, 2025 | Volume: 164 | Issue: 4 | Pages: 613-619

10.1093/ajcp/aqaf090 | PMID 40878366

Abstract Objective The aim of this study was to evaluate a large cohort of gallbladder amyloid cases to determine clinical and morphologic features. Methods Cholecystectomy specimens (N = 118) typed using proteomics-based techniques between 2008 and 2023 were identified. Clinical and morphologic features were reviewed. Results Six amyloid types were identified: ATTR (n = 63, 53.4%), AL (n = 46, 39.0%), AA (n = 4, 3.4%), AApoA1 (n = 2, 1.7%), ALECT2 (n = 2, 1.7%), and AEFEMP1 (n = 1, 0.8%). Amyloidogenic mutations were detected in 3 ATTR cases and 2 AApoA1 cases. Morphologic review (n = 26) revealed perimuscular vessel involvement in all cases. Amyloidosis was an unexpected diagnosis first made on the cholecystectomy specimen in half of the patients with clinical information (n = 10). All 9 patients with follow-up had evidence of systemic disease. In 2 patients, cholecystic involvement was initially missed and only retrospectively identified after the diagnosis of cardiac amyloidosis. Conclusions In patients with clinical data, amyloidosis was often unexpected, the gallbladder was commonly the first tissue sampled with amyloidosis, and all patients had systemic disease. Thorough review of cholecystectomy specimens with careful inspection of perimuscular vessels, coupled with a low threshold for ordering Congo red stain in elderly individuals and amyloid typing using a robust method such as proteomics, can prevent a delay in amyloid diagnosis and management.
Isolated Mu Heavy Chain Deposition Disease—A Rare Cause of Spontaneous Splenic Rupture in a Young Adult

eJHaem | July 18, 2025 | Volume: 6 | Issue: 4 | Pages: No page available

10.1002/jha2.70107 | PMID 40688187

The Amyloidosis Intersection: Dual Amyloid Types in a Single Host

European Journal of Haematology | June 17, 2025 | Volume: 115 | Issue: 3 | Pages: 287-298

10.1111/ejh.14429 | PMID 40526008

ABSTRACTBackgroundAdvances in fibril typing by mass spectrometry have improved the accuracy of amyloidosis diagnosis. Dual amyloidogenic proteins have been reported in deposits in sole and multiple different organs.MethodsFive patients with dual amyloidoses were diagnosed between 1995 and 2022 by Congo red staining and fibril typing using the best available methods at the time of evaluation. Sequencing of TTR and GSN genes was performed. Literature search identified 46 additional cases.ResultsThree patients exhibited Waldenström macroglobulinemia‐associated AL (n = 3) amyloidoses in conjunction with ATTRwt or AGel amyloidosis; two patients featured AL/ATTRwt and AA/ATTRwt amyloidoses. One patient demonstrated dual amyloidoses within one anatomical site; three patients featured two amyloidosis types at different anatomical sites; and one patient had dual amyloid deposits in a single anatomical site along with different sites. The time interval between diagnoses was 0–288 months, with the heart and kidneys being the most affected organs.ConclusionsOur findings underscore the complexity of clinical presentation in amyloidosis, as multiple amyloid types can co‐exist in a single individual and affect various anatomical sites. Accurate assessment of the clinical phenotype and thorough amyloid fibril typing from the target organs are essential for precise diagnosis and tailored treatment. Trial Registration: ClinicalTrials.gov Identifier: NCT00898235
Enhanced analytic methodology enables postmortem diagnosis of hereditary AApoAI amyloidosis

Amyloid | June 12, 2025 | Volume: 32 | Issue: 4 | Pages: 361-363

10.1080/13506129.2025.2515938 | PMID 40503944

Proteomic determinants of renal organ response in light-chain amyloidosis

Amyloid | February 20, 2025 | Volume: 32 | Issue: 2 | Pages: 200-202

10.1080/13506129.2025.2467282 | PMID 39972595

Whole tissue proteomic analyses of cardiac ATTR and AL unveil mechanisms of tissue damage

Amyloid | January 8, 2025 | Volume: 32 | Issue: 1 | Pages: 72-80

10.1080/13506129.2024.2448440 | PMID 39773246