Predicting the future of anti-tumor necrosis factor therapy

Tumor necrosis factor (TNF) antagonists are approved worldwide for the treatment of rheumatoid arthritis (RA). Clinical experience revealed that TNF-blocking therapy is effective for only approximately two thirds of patients, reflecting that there are 'responders' as well as 'nonresponders'. Given the destructive nature of RA, the risk of adverse effects, and considerable costs for therapy, there is a strong need to make predictions on success before the start of therapy. In the current issue of Arthritis Research & Therapy, Hueber and colleagues become the first to present a multi-parameter serum protein biomarker set that has predictive value prior to the start of anti-TNF treatment. Ultimately, this finding may contribute to a personalized form of medicine, whereby a specific therapy will be applied that is best suited to an individual patient.     

Detection of a C-insertion polymorphism within the human tumor necrosis factor alpha (TNFA) gene

We have identified a C-insertion polymorphism in the 5'UTR of the first exon of the human tumor necrosis factor alpha (TNFA) gene. TNFA is a cytokine that plays an important role in the inflammatory response.     

Characterization of the chromophores of pyoverdins and related siderophores by electrospray tandem mass spectrometry

Characteristic fragment ions of the various chromophores of the pyoverdin siderophore family obtained by collision activated dissociation of the [M+2H]²⁺ ions are reported allowing unambiguous identification. Tandem mass spectrometrical studies revealed the existence of the first example of a ferribactin with a succinamide side chain, and they add some information to the problem in which way a malic acid side chain is attached to the chromophore.     

The Nabidae (Insecta,Hemiptera, Heteroptera) of?Argentina

In Argentina, five genera and 14 species are recorded in the subfamilies Prostemmatinae and Nabinae: Hoplistoscelis sordidus Reuter, Lasiomerus constrictus Champion, Metatropiphorus alvarengai Reuter, Nabis argentinus Meyer-Dür, Nabis (Tropiconabis) capsiformis Germar, Nabis faminei Stål, Nabis paranensis Harris, Nabis punctipennis Blanchard, Nabis roripes Stål, Nabis setricus Harris, Nabis tandilensis Berg, Pagasa (Pagasa) costalis Reuter, Pagasa (Lampropagasa) fuscipennis Reuter and Pagasa (Pagasa) signatipennis Reuter.     

A quantitative histochemical study of NADPH-ferrihemoprotein reductase activity

Summary A quantitative histochemical assay for NADPH-ferrihemoprotein (P450) reductase had been developed. For optimal activity, it is necessary to use a relatively electropositive tetrazolium salt such as neotetrazolium chloride as the final acceptor. The apparentK _m of the reaction is 0.83 mM. Its specificity has been proven in two ways: (i) activity is increased selectively in the pericentral zone of liver from rats treated with phenobarbitone, an inducer of the reductase, though not in liver of rats injected with 3-methylcholanthrene, which induces NAD(P)H dehydrogenase; (ii) it is competitively inhibited by NADP⁺ (K _i=1.50mm) though unaffected by dicumarol, an inhibitor of NAD(P)H dehydrogenase activity. An NADP⁺ concentration ten times greater than the substrate concentration inhibits the histochemical reaction and the reaction in a microsomal fraction assayed biochemically to the same degree (70% inhibition). The amount of inhibition is independent of temperature, of the zone of the acinus and of the treatment of the animal.Continuous microdensitometric monitoring of the reaction product as it is formed has shown that the specific reaction is linear with incubation up to 10 min, thus allowing end-point measurements to be used for cytophotometric analysis.     

The binding of aromatic derivatives of β-d-galactopyranosides to the fab' of immunoglobulin J539. Observation on the nature of ligand-antibody interactions

A number of d-galactopyranosides bearing aromatic substituents have been prepared, and their binding to immunoglobulin J539 (Fab') has been studied. It appears that the main contribution of the 6-O-aromatic moiety to binding arises from the fact that it imparts an increased hydrophobicity to the ligand, causing a decrease in its hydration (solubility) that results in a greater free-energy of binding. In the d-galactosides having an aromatic aglycon, the phenyl group appears to partake in actual interactions with the protein.