Mediastinal histoplasmosis presenting as dysphagia: a case report with literature review.

Histoplasmosis is an endemic infection of the Ohio and Mississippi River valleys. Clinical presentation of infection in immunocompetent hosts ranges from asymptomatic to minor flu-like symptoms; however, disseminated infection can occur in immunocompromised patients. Esophageal involvement in the form of dysphagia secondary to mediastinal histoplasmosis is rarely reported in the literature. We present a young female who complained of dysphagia and was found to have an esophageal stricture on barium esophagogram. Endoscopy revealed a submucosal nodule stricture situated 29 cm from the incisors. She underwent thoracotomy for lymph node removal. Histologic findings of the removed lymph node showed caseating granuloma with macrophages. The clinical findings together with the laboratory evaluation and biopsy features were suggestive of mediastinal histoplasmosis as the cause of the dysphagia.

Homophenotypic Aalpha R16H fibrinogen (Kingsport): uniquely altered polymerization associated with slower fibrinopeptide A than fibrinopeptide B release.

We detail for the first time the uniquely altered fibrin polymerization of homophenotypic Aalpha R16H dysfibrinogen. By polymerase chain reaction amplification and DNA sequencing, our new proposita's genotype consisted of a G>A transition encoding for Aalpha R16H, and an 11 kb Aalpha gene deletion. High-performance liquid chromatography disclosed fibrinopeptide A release approximately six times slower than its fibrinopeptide B. Turbidimetric analyses revealed unimpaired fibrin repolymerization, and abnormal thrombin-induced polymerization (1-7 mumol/l fibrinogen, > 96% coagulable), consisting of a prolonged lag time, slow rate, and abnormal clot turbidity maxima, all varying with thrombin concentration. For example, at 0.2-3 U/ml, the resulting turbidity maxima ranged from lower to higher than normal control values. By scanning electron microscopy, clots formed by 0.3 and 3 thrombin U/ml displayed mean fibril diameters 42 and 254% of the respective control values (n = 400). Virtually no such differences from control values were demonstrable, however, when clots formed in the presence of high ionic strength (micro = 0.30) or of monoclonal antibeta(15-42)IgG. The latter also prolonged the thrombin clotting time approximately three-fold. Additionally, thrombin-induced clots displayed decreased elastic moduli, with G' values of clots induced by 0.3, 0.7 and 3 thrombin U/ml corresponding to 11, 34, and 45% of control values. The results are consistent with increased des-BB fibrin monomer generation preceding and during polymerization. This limited the inherent gelation delay, decreased the clot stiffness, and enabled a progressively coarser, rather than finer, network induced by increasing thrombin concentrations. We hypothesize that during normal polymerization these constitutive des-BB fibrin monomer properties attenuate their des-AA fibrin counterparts.