ABSTRACT
A 77-year-old man underwent echocardiography-guided right ventricular endomyocardial biopsy for suspected cardiac amyloidosis. After the procedure, severe tricuspid regurgitation with a flail posterior leaflet was detected. A myocardial biopsy specimen contained a segment of tricuspid valve chorda tendinea. Endomyocardial biopsy is considered the standard for detecting transplant rejection and evaluating infiltrative cardiomyopathies and myocarditis. Echocardiography complements, and in some institutions has replaced, fluoroscopy as a method of bioptome guidance because of its superior resolution of the tricuspid valve anatomy, endocardial surface, and thin right ventricular free wall and apex. Nevertheless, because of the limitations of 2-dimensional imaging, complications do occur.
Subject(s)
Biopsy, Needle/methods , Endocardium/diagnostic imaging , Endocardium/injuries , Ultrasonography, Interventional/adverse effects , Aged , Humans , Male , Ultrasonography, Interventional/methodsABSTRACT
A 50-year-old man without previous coronary disease presented with an inferior myocardial infarction following exercise. He was initially treated with thrombolytic therapy and nitroglycerin. Subsequent coronary angio-graphy and cardiac computed tomography demonstrated an anomalous right coronary artery originating from the left coronary sinus and passing between the aorta and main pulmonary artery. The coronary arteries were otherwise patent. The patient later underwent transaortic unroofing of the anomalous right coronary artery and was discharged in good condition.
Subject(s)
Coronary Vessel Anomalies/complications , Coronary Vessel Anomalies/surgery , Myocardial Infarction/etiology , Vascular Surgical Procedures/methods , Chest Pain/diagnosis , Chest Pain/etiology , Coronary Angiography , Coronary Vessel Anomalies/diagnostic imaging , Follow-Up Studies , Humans , Male , Middle Aged , Myocardial Infarction/diagnostic imaging , Risk Assessment , Tomography, X-Ray Computed , Treatment OutcomeABSTRACT
Many protein conformational diseases arise when proteins form alternative stable conformations, resulting in aggregation and accumulation of the protein as fibrillar deposits, or amyloids. Interestingly, numerous proteins implicated in amyloid protein formation show similar structural and functional properties. Given this similarity, we tested the notion that carboxymethylated bovine alpha-lactalbumin (1SS-alpha-lac) could serve as a general amyloid fibrillation/aggregation model system. Like most amyloid forming systems, Mg2+ ions accelerate 1SS-alpha-lac amyloid fibril formation. While osmolytes such as trimethylamine N-oxide (TMAO), and sucrose enhanced thioflavin T detected aggregation, a mixture of trehalose and TMAO substantially inhibited aggregation. Most importantly however, the flavonoid, baicalein, known to inhibit alpha-synuclein amyloid fibril formation, also inhibits 1SS-alpha-lac amyloid with the same apparent efficacy. These data suggest that the easily obtainable 1SS-alpha-lac protein can serve as a general amyloid model and that some small molecule amyloid inhibitors may function successfully with many different amyloid systems.
