Complement factor H binds malondialdehyde epitopes and protects from oxidative stress

Oxidative stress and enhanced lipid peroxidation are linked to many chronic inflammatory diseases, including age-related macular degeneration (AMD). AMD is the leading cause of blindness in Western societies, but its aetiology remains largely unknown. Malondialdehyde (MDA) is a common lipid peroxidation product that accumulates in many pathophysiological processes, including AMD. Here we identify complement factor H (CFH) as a major MDA-binding protein that can block both the uptake of MDA-modified proteins by macrophages and MDA-induced proinflammatory effects in vivo in mice. The CFH polymorphism H402, which is strongly associated with AMD, markedly reduces the ability of CFH to bind MDA, indicating a causal link to disease aetiology. Our findings provide important mechanistic insights into innate immune responses to oxidative stress, which may be exploited in the prevention of and therapy for AMD and other chronic inflammatory diseases.     

Systematics and evolution of holarctic Pierinae (Lepidoptera). An enzyme electrophoretic approach

Summary Enzyme electrophoretic data show a remarkably high degree of genetic similarity within the European group ofnapi s.l. whereas genetic differences exist at several loci between the European and the North American taxa ofnapi s.l. It is concluded that the European taxa did not differentiate to the species level and form a phylogenetically young group. The North American taxa included in this study are specifically distinct from Europeannapi and separated much earlier. Within these North American taxamarginalis, oleracea andvirginiensis did undergo speciation. The data show a splitting of the genusPieris into three species groups, each genetically differentiated to the same level. The splitting ofPieris into two genera, as suggested by earlier investigators, is not supported here.     

Effect of insulin upon renal amino acid transport in lambs

Zusammenfassung An Nierenrindenschnitten von Lämmern und Schafen wurde untersucht, ob die Anwesenheit von Insulin bzw. Glukagon im Inkubationsmedium die gegen ein Konzentrationsgefälle erfolgende Aufnahme von -Aminoisobuttersäure in Nierenrindenzellen beeinflusst. Insulin stimulierte in diesen Versuchen (Inkubationszeit: 80 min) die Akkumulation von -Aminoisobuttersäure in Nierenrindenzellen bei jungen Lämmern, nicht jedoch bei älteren Lämmern und Schafen. Für Glukagon konnte kein Effekt nachgewiesen werden.

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Acknowledgment. The investigation was supported by the Deutsche Forschungsgemeinschaft (SFB 147 Jungtierkunde).     

Nachweis hoher Aktivitäten von Kreatin-Kinase bei dem ChaetognathenSagitta setosa

Summary Notably high activities of creatine kinase have been shown in tissues of Chaetognaths both by spectrophotometric assays and on agarose-gels, where the enzyme appears as a single band. Arginine kinase activity could not be detected. It is pointed out that these findings might be of significance in elucidating the systematic position of Chaetognaths.     

Zone electrophoretic studies on lactate dehydrogenase isoenzymes in South American Cichlids (Teleostei,Percomorphi)

Zusammenfassung Ein Vergleich der elektrophoretischen Mobilitäten der Laktatdehydrogenasen A₄ (Skelettmuskel), B₄ (Herz) und E₄ (Retina) zeigt bei 7 Arten der GattungCichlasoma weitgehende Übereinstimmungen. 10 Arten anderer Gattungen südamerikanischer Cichliden weisen, verglichen mit der GattungCichlasoma, zunehmende Divergenz der Isoenzymmuster auf. Es wird vermutet, dass sich hierin die phylogenetische Verwandtschaft der Gattungen widerspiegelt. Die auf Grund der Übereinstimmungen in LDH-Isoenzymmustern ermittelten phylogenetischen Zusammenhänge decken sich weitgehend mit den Beziehungen, die durch vergleichendmorphologische Untersuchungen aufgezeigt wurden. Das methodische Vorgehen scheint geeignet, taxonomische Beziehungen zu ergänzen, die durch klassische Kriterien dargelegt wurden

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The technical assistance of Mrs.Evelyne Perriard is gratefully acknowledged.     

The alpha 1 domain of the HLA-DR molecule is essential for high-affinity binding of the toxic shock syndrome toxin-1

Several exoproteins from the bacterium Staphylococcus aureus are highly potent polyclonal activators of T cells in the presence of cells bearing class II antigens of the major histocompatibility complex (MHC). These toxins, including the toxic shock syndrome toxin (TSST-1), act at nanomolar concentrations, bind directly to class II molecules, and do not require the processing typical of nominal antigen. Each toxin is capable of stimulating a subpopulation of peripheral T lymphocytes bearing particular V beta sequences as part of their alpha beta T-cell receptors. It is not known how these so-called 'superantigens' bind to class II and how this binding stimulates T cells. In this study, the different affinities of TSST-1 for human class II molecules DR and DP were exploited to define the region of a class II molecule necessary for high-affinity binding. Using chimaeric alpha- and beta-chains of DR and DP expressed at the surface of transfected murine fibroblasts and a binding assay with TSST-1, it was shown that the alpha 1 domain of DR is essential for high-affinity binding, and further that TSST-1 binding did not prevent subsequent binding of a DR-restricted antigenic peptide. This is compatible with a model of superantigen making external contacts with both class II and T cell receptor, and suggests that the V beta portion of the T-cell receptor interacts with the nonpolymorphic alpha-chain of DR.