No abstract

Microsporidia are emerging as opportunistic pathogens in patients with AIDS. Enterocytozoon bieneusi and Encephalitozoon (Septata) intestinalis have been implicated in enteric infections in AIDS patients with chronic diarrhea, a wasting syndrome, and malabsorption. We used the polymerase chain reaction (PCR) and primers that amplify the conserved regions of the small-subunit rRNA (SSU-rRNA) gene of E. bieneusi and E. intestinalis in tissue specimens from HIV-infected patients with and without diarrhea to examine the association between microsporidia and diarrhea in patients with AIDS. Tissue specimens were obtained from 68 patients with AIDS and diarrhea (mean CD4 lymphocyte count, 21/mm3) and 43 AIDS patients without diarrhea (mean CD4 lymphocyte count, 60/mm3). By means of PCR with use of the SSU-rRNA primers specific for E. bieneusi and E. intestinalis, we found that 44% of patients with diarrhea were infected with microsporidia, whereas only 2.3% of the patients without diarrhea were infected with microsporidia (P < .001). There was a clear association between the presence of microsporidia and diarrhea. In addition, the SSU-rRNA primers proved to be sensitive and specific when used in this clinical setting.

Autoantibodies from rare patients with primary bili-gens. [1][2][3][4] Antibodies against the E2 subunits of the mitoary cirrhosis (PBC) recognize LBR, or lamin B receptor, chondrial oxo acid dehydrogenase complexes are found an integral membrane protein of the inner nuclear mem-in approximately 90% of patients with PBC and are brane. Human LBR has a nucleoplasmic, amino-terminal specific for this disease. [4][5][6][7] Approximately 30% of padomain of 208 amino acids followed by a carboxyl-termi-tients with PBC have autoantibodies against proteins nal domain with eight putative transmembrane seg-of the nuclear envelope. 10 Autoantimains and that autoantibodies from patients with PBC bodies against LBR and gp210 are specific for PBC and predominantly react with one domain of a protein anti-rarely, if ever, found in patients with other liver or gen. This work also provides further characterization of autoimmune diseases. been shown to trigger the disease, and specific autoantibodies are related to the pathological process. 13 In Primary biliary cirrhosis (PBC) is characterized by others, autoantibodies of different specificities and unintrahepatic bile duct destruction accompanied by im-clear pathophysiological significance recognize a distrimune system abnormalities, most notably the presence bution of epitopes on different proteins. 13 In PBC, the of autoantibodies against intracellular protein anti-autoantibodies characterized so far primarily recognize restricted regions of their respective protein antigens. Antibodies against the E2 subunit of the mitochondrial

Ascites in systemic lupus erythematosus (SLE) is rarely massive, and either accompanies the typical manifestations of active disease or results from nephrotic syndrome, protein-losing enteropathy, constrictive pericarditis, and conditions unrelated to lupus. Marked ascites has been attributed to chronic lupus peritonitis, characterized by the insidious onset of massive, painless ascites and unrelated to disease activity. Regardless of the etiology, ascites typically has a gradual onset and occurs after a diagnosis of SLE has been made. We describe a young woman presenting with the rapid development of massive ascites as the initial manifestation of SLE.

Although it is known that circulating heme accumulates in liver cells, the process by which heme enters hepatocytes is only partly understood. Hemopexin and a putative hemopexin receptor on hepatocyte membranes may mediate the uptake process. However, whether there are sufficient hemopexin receptors on rat hepatocytes to account for the bulk of heme entering cells is unknown. It is likely that heme may be transferred directly from albumin with the help of a plasma membrane heme transporter. To clarify the transport mechanism of heme into liver cells, we studied the uptake by short-term cultured rat hepatocytes of 55 Feheme incubated with rat serum albumin. In these cells, the initial uptake of 55 Fe-heme at 37ЊC was five-to eightfold higher than that at 4ЊC, linear for at least 5 minutes, and saturable. The K m of heme uptake was 0.95 ؎ 0.27 mol/L, and the V max was 0.12 ؎ 0.01 pmol/min/mg protein (n ‫؍‬ 3). Neither isosmotic substitution of sucrose for NaCl in the medium nor adenosine triphosphate (ATP) depletion, perturbations that are known to reduce uptake of bilirubin, sulfobromophthalein (BSP), and taurocholate, had any influence on 55 Fe-heme uptake. In addition, heme uptake was not reduced in the presence of a greater than 500-fold molar excess of BSP. These results indicate that hepatocytes take up heme by a process that is distinct from that of these other organic anions. (HEPATOLOGY 1998;28:150-155.)