Teilzulassung – neue Gestaltungsmöglichkeit ohne praktische Bedeutung?

Ohne Zusammenfassung     

Inhibition of Complement Regulation Is Key to the Pathogenesis of Active Heymann Nephritis

Crry (complement receptor 1–related protein/gene y) is a key cellular complement regulator in rodents. It is also present in Fx1A, the renal tubular preparation used to immunize rats to induce active Heymann nephritis (HN), a model of membranous nephropathy. We hypothesized that rats immunized with anti-Fx1A develop autoantibodies (auto-Abs) to Crry as well as to the megalin-containing HN antigenic complex, and that anti-Crry Abs promote the development of injury in HN by neutralizing the complement regulatory activity of Crry. Rats immunized with Fx1A lacking Crry remained free of proteinuria and glomerular deposits of C3 during a 10-wk follow-up despite typical granular immunoglobulin (Ig)G deposits in glomeruli. Anti-Fx1A auto-Abs were present in their sera at levels that were not different from sera pooled from proteinuric rats with HN induced with nephritogenic Fx1A. Passive administration of sheep anti-Crry Abs to rats immunized with Crry-deficient Fx1A led to proteinuria and glomerular C3 deposition, which were not seen in such rats injected with preimmune IgG, nor in rats with collagen-induced arthritis injected with anti-Crry IgG. To directly examine the role of Crry in HN, rats were immunized with Crry-deficient Fx1A reconstituted with rCrry. This led to typical HN, with 8 out of 15 rats developing proteinuria within 14 wk. Moreover, the extent of glomerular C3 deposition correlated with proteinuria, and anti-Crry Abs were present in glomerular eluates. Thus, Crry is a key nephritogenic immunogen in Fx1A. Formation of neutralizing auto-Abs to Crry impairs its function, leading to unrestricted complement activation by Abs reactive with the HN antigenic complex on the epithelial cell surface.     

Coincidence of schizophrenia and hyperbilirubinemia.

In a retrospective study, the bilirubin plasma concentrations of every patient admitted to the Psychiatric Hospital were collected. Patients suffering from liver disease, substance abuse, overt hemolysis, or increased liver enzymes were excluded. Schizophrenics showed a significantly higher incidence of hyperbilirubinemia than patients suffering from other psychiatric disorders. This phenomenon seems to be independent of drug usage and therefore points to a relationship between hyperbilirubinemia and schizophrenic psychosis. Hypothetic explanations, such as a possible genetic disposition for Gilbert Syndrome, an increased vulnerability of red-cell membranes, and the role of estrogens in schizophrenic patients, are discussed.     

5-Oxo-1H-3,4,5,6-tetrahydro-2,6-methano-2-benzazocin und seine Reduktionsprodukte

3,4,5,6-Tetrahydro-1H-2,6-methano-2-benzazocin-5-one and its Reduction Products 3,4,5,6-Tetrahydro-1H-2,6-methano-2-benzazocin-5-one 2 has been prepared by oxidation of N-benzyl-4-piperidone 1 with cerium(IV) sulfate. 2 was reduced by sodium borohydride or lithium aluminum hydride in various solvents. The stereoselectivity of these reductions is high. The configurations of the epimeric alcohols were determined by ¹H-NMR spectroscopy.     

Cerebrospinal fluidCHOLINESTERASES—MARKERS for loss ofcholinergic basal forebrain neurons?

The present study was conducted to test the hypothesis that cholinergic basalforebrain neurons are a major source of cerebrospinal fluid (CSF) cholinesterases. To address thisquestion enzyme activities of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inboth CSF and parietal cortex were assayed following selective lesion of basal forebrain cholinergicneurons by a single intracerebroventricular application of the cholinergic immunotoxin192IgG-saporin. Cholinergic immunolesions led to a dramatic decrease in total AChE activity inparietal cortex, which was due to the specific loss of the G4 molecular form while the activity ofthe G1 form was increased as compared to nonlesioned animals. In contrast, the total enzymeactivity of BChE and its molecular forms were not affected by cholinergic lesion in both parietalcortex and CSF. The data suggest, that cholinergic basal forebrain neurons are seemingly not amajor source of cholinesterases in the CSF, and do not provide any evidence for using CSFcholinesterases as a diagnostic marker of basal forebrain cholinergic cell loss in humans.