Tropical pyomyositis

A 22 year old male presented with symptoms of diffuse muscle pain and multiple abnormal laboratory findings that were eventually attributed to tropical myositis. Computed tomography scan was more reliable than ultrasound and served as a guide to needle aspiration and pathologic diagnosis.     

The geometry of triple-balloon dilation

Triple-balloon dilation (TBD) of a variety of luminal structures has been successfully, though infrequently, used. A mathematical model is presented for the selection of balloon sizes, and equations and tables are derived that allow the user to estimate more accurately the size of balloons needed for TBD of structures with large lumina. With TBD, an approximately circular lumen can be formed. Also, TBD allows smaller, higher-pressure balloons to be used instead of single, low-pressure, large balloons. However, multiple puncture sites may be required for TBD.     

Studies on the blood group antigen Ina

Anti-Ina antibodies have been observed in 30 of the 41 anti-Rh donors hyperimmunised with group O Ror In(a+) blood. They have also been found in four of 60 Rh immunised women. In three of these the husbands and previous children were In(a+). However, there was no evidence of haemolytic disease of the newborn due to anti-Ina antibodies alone. The Ina antigen is developed at birth though it is weaker than in adults. The strength of the Ina antigen decreases during pregnancy and returns to the previous level three months afer termination of pregnancy. The Ina antigen is affected by papain, trypsin, bromelin and neuraminidase. The antibodies in all the donors, even though their sera were preserved for more than 10 years at -20 degrees C, reacted in saline and albumin milieux and in the indirect antiglobulin procedure using anti-IgG reagents. These antibodies are complement binding as shown by the two-stage complement binding test. Treatment with 2-mercaptoethanol and DEAE-column chromatography suggested the anti-Ina antibodies were of the IgG class. Anti-Ina antibodies could possibly cause a transfusion reaction since In(a+) red cells when transfused into individuals possessing anti-Ina antibodies are eliminated from the circulation within 20 minutes.     

Immune responses to Aspergillus antigen in IL‐4‐/‐ mice and the effect of eosinophil ablation

BACKGROUND: Exposure to Aspergillus fumigatus allergens results in enhanced total serum IgE and peripheral blood eosinophils in mice. The associated pulmonary inflammation and immunologic responses are comparable to those detected in human allergic bronchopulmonary aspergillosis. Allergen-induced cytokines are thought to regulate the inflammatory and immune responses in these animals. METHODS: In the present study, we exposed C57BL/6 and BALB/c mice to A. fumigatus antigen. Both wild-type and IL-4 knockout phenotypes of animals of both strains were used. Some animals were also treated with anti-IL-5 or anti-IFN-gamma. Total serum IgE, Aspergillus species IgG subclass, peripheral blood eosinophils, and lung histology were studied. RESULTS: The results demonstrate similar lung inflammation in all wild-type and IL-4-/- animals exposed to A. fumigatus antigen. Similarly, in spite of the diverse immune response produced by the anticytokine treatment, no major differences were detected among any of the animal groups studied. CONCLUSIONS: It can be concluded that A. fumigatus exposure in an immunologically unaltered host is predominantly of a Th2 type, and that depletion of the Th2 cytokine leads to a similar lung inflammation but with a characteristic Th1 response, suggesting that the pathogenesis of allergic aspergillosis is the result of multiple induction pathways.     

GLUT-1 glucose transporters in the blood-brain barrier: differential phosphorylation

Glucose is the primary metabolic fuel for the mammalian brain, and a continuous supply is required to maintain normal CNS function. The transport of glucose across the blood-brain barrier (BBB) into the brain is mediated by the facilitative glucose transporter GLUT-1. Prior studies (Simpson et al. [2001] J Biol Chem 276:12725-12729) had revealed that the conformations of the GLUT-1 transporter were different in luminal (blood facing) and abluminal (brain facing) membranes of bovine cerebral endothelial cells, based on differential antibody recognition. This study has extended these observations and, by using a combination of 2D-PAGE/Western blotting and immunogold electron microscopy, determined that these different conformations are exhibited in vivo and arise from differential phosphorylation of GLUT-1 and not from alternative splicing or altered O- or N-linked glycosylation.