Amyloid heart disease

Twenty-eight cases of cardiac amyloidosis were observed on reviewing 21,300 postmortem examinations performed at Barnes Hospital between 1916 and 1962. Five of these have been presented in detail.

The clinical, electrocardiographic and in some instances vectorcardiographic findings have been correlated with the postmortem findings of cardiac amyloidosis.

Pertinent antemortem features are described which may permit a more accurate diagnosis of amyloid heart disease; particularly the combination of left axis deviation of QRS, low QRS voltage in the limb leads, a QS configuration and/or small R waves in V₁ to V₃, with or without atrial fibrillation, occurring in the electrocardiogram of elderly patients in intractable congestive heart failure without a history of heart disease.     

Amyloid disease of the heart

A 70-year-old woman with a history of hypertension had been well until 3 years before when she developed atrial fibrillation and subsequently congestive heart failure. The heart failure became worse and she had three fainting spells. Low voltage on electrocardiogram and global hypokinesis on echocardiography were suggestive of cardiac amyloidosis. The patient died suddenly of intractable ventricular fibrillation. Autopsy confirmed heavy infiltration of the myocardium by amyloid.     

Amyloid heart disease mimicking hypertrophic cardiomyopathy

OBJECTIVE: To investigate the importance of transthyretin (TTR) gene mutations in explaining the phenotypic expression in patients diagnosed with hypertrophic cardiomyopathy (HCM) in northern Sweden. BACKGROUND: Hypertrophic cardiomyopathy is relatively common and often caused by mutations in sarcomeric protein genes. Mutations in the TTR gene are also common, one of which causes familial amyloid polyneuropathy (FAP), with peripheral polyneuropathy and frequently, cardiac hypertrophy. These circumstances were highlighted by the finding of an index case with amyloidosis, presenting itself as HCM. Initial rectal and fat biopsies did not show amyloid deposits. Later on, the patient was shown to carry a TTR gene mutation, and cardiac amyloidosis was confirmed by myocardial biopsy. Only then was a repeated fat biopsy positive for amyloid deposits. DESIGN: Cross-sectional study. SETTING: Cardiology tertiary referral centre. SUBJECTS: Forty-six unrelated individuals with HCM and the index case were included. Common diagnostic criteria for HCM were used. The 46 patients with HCM were previously analysed for mutations in eight sarcomeric protein genes and the TTR gene was now analysed by denaturing high-performance liquid chromatography and direct sequencing. RESULTS: One mutation in the TTR gene (Val30Met) was found in three individuals and the index case. CONCLUSIONS: Three of the 46 cases with HCM carried the Val30Met mutation, and were considered likely to have cardiac amyloidosis, like the index case. As a correct diagnosis of cardiac amyloidosis is mandatory for a potentially life-saving treatment, TTR mutation analysis should be considered in cases of HCM not explained by mutations in sarcomeric protein genes.     

Amyloid heart disease diagnosed with echocardiography

A sixty years old woman with amyloid heart disease has been presented. Postural hypotension was the main symptom in this case. Pneumonia and the developing congestive heart failure was the cause of death. Only the last echocardiographic examination: hypertrophied interventicular septum with a peculiar speckled appearance of myocardium, together with low voltage electrocardiography made possible to confirm this diagnosis. It was shown in this case, how difficult it is to diagnose amyloid heart disease. Low ejection fraction together with diastolic abnormalities is usually a forecast of bad prognosis.     

Amyloid heart disease manifested by systemic arterial thromboemboli.

Amyloid heart disease characteristically produces a stiff heart syndrome whereby diastolic filling is impaired yet systolic function is well preserved. We report two patients with this pattern of amyloid heart disease, both of whom developed cardiogenic thromboemboli. The rarity of this complication is striking given the pathophysiologic bases of amyloid heart disease. Investigation of contributing causes revealed that the phenomena appeared to represent the cumulative effects of disorders producing stasis, endothelial disturbance, and probable abnormalities in blood coagulability, the classic Virchow's triad revisited. Understanding of the pathophysiologic basis of this event leads to specific suggestions for workup and management in this patient population.     

Amyloid heart disease. New frontiers and insights in pathophysiology, diagnosis, and management

Amyloidosis comprises a unique group of diseases that share in common the extracellular deposition of insoluble fibrillar proteins in organs and tissues. Cardiovascular amyloidosis can be primary, a part of systemic amyloidosis, or a result of chronic systemic diseases elsewhere in the body. The most common presentations are congestive heart failure-mainly a restrictive infiltrative pattern--and conduction system disturbances. Recent developments in imaging techniques and extracardiac tissue sampling have minimized the need for invasive endomyocardial biopsy for amyloidosis. Despite advances in treatment, the prognosis for patients with amyloidosis is still poor and depends on the underlying disease type. Herein, we present new insights and recent advances in cardiovascular amyloidosis.     

Amyloid arthritis simulating rheumatoid disease in five patients with multiple myeloma

Five patients with multiple myeloma, three of whom had kappa light chain disease, presented with a symmetrical polyarthritis simulating rheumatoid arthritis. In all instances amyloid infiltration of synovial tissues appeared to account for the articular manifestations. Synovial fluids examined in four of these cases lacked the inflammatory characteristics of rheumatoid synovial fluid and three of them contained M components. In the course of synovial fluid analysis, small fragments of amyloid-containing material were detected in the aspirates from three of the patients, thereby establishing the diagnosis prior to confirmation by tissue biopsy. In the past patients with verified amyloidosis involving synovial tissues have been erroneously considered to have rheumatoid arthritis.     

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

We have purified and characterized the cerebral amyloid protein that forms the plaque core in Alzheimer disease and in aged individuals with Down syndrome. The protein consists of multimeric aggregates of a polypeptide of about 40 residues (4 kDa). The amino acid composition, molecular mass, and NH2-terminal sequence of this amyloid protein are almost identical to those described for the amyloid deposited in the congophilic angiopathy of Alzheimer disease and Down syndrome, but the plaque core proteins have ragged NH2 termini. The shared 4-kDa subunit indicates a common origin for the amyloids of the plaque core and of the congophilic angiopathy. There are superficial resemblances between the solubility characteristics of the plaque core and some of the properties of scrapie infectivity, but there are no similarities in amino acid sequences between the plaque core and scrapie polypeptides.