Detection of cytochromes on sodium dodecylsulphate-polyacrylamide gels by their intrinsic fluorescence

Heme-containing polypeptides can be detected on sodium dodecylsulphate (SDS)-polyacrylamide gels by the intrinsic fluorescence of their prosthetic group. The fluorescence is stable and specific; approximately 0.2 μg of cytochrome c/band can be detected in this way. No equipment is necessary beyond a camera, an ultraviolet lamp, and some filters.     

The induction of Guerin’s carcinoma cytochrome P450 hydroxylase activity by retinoids

Using Guerin’s carcinoma as a model the interrelationship between the tumor growth process and supplementation of the body with vitamin A has been studied. The replenishment of vitamin A resources of vitamin-deficient tumor bearing animals modulated the Guerin’s carcinoma growth rate in a dose dependent manner (r = 0.83). The morphological parameters of tumor growth under conditions of supplementation with vitamin A (0–3000 IU) positively correlated with hydroxylase (r = 0.81) and demethylase (r = 0.49) activities of the Guerin’s carcinoma cytochrome P450 system. The increase in the tumor growth rate together with the induction of hydroxylase and demethylase activities of cytochrome P450 in the Guerin’s carcinoma microsomal fraction, observed either under conditions of retinyl acetate overdose supplementation, or selective liposomal form of all-trans-retinoic acid, suggests the stimulatory effect of retinoids on tumor growth.     

Copeptin is associated with mortality and outcome in patients with acute intracerebral hemorrhage

Background  

Spontaneous intracerebral hemorrhage (ICH) accounts for a high mortality and morbidity. Early prediction of outcome is crucial for optimized care and treatment decision. Copeptin, the C-terminal part of provasopressin, has emerged as a new prognostic marker in a variety of diseases, but its prognostic value in ICH is unknown.     

NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 3 in apo state and in complex with inhibitor PD173074

Fibroblast growth factors receptors (FGFR) are transmembrane protein tyrosine kinases involved in many cellular process, including growth, differentiation and angiogenesis. Dysregulation of FGFR enzymatic activity is associated with developmental disorders and cancers; therefore FGFRs have become attractive targets for drug discovery, with a number of agents in late-stage clinical trials. Here, we present the backbone resonance assignments of FGFR3 tyrosine kinase domain in the ligand-free form and in complex with the canonical FGFR kinase inhibitor PD173074. Analysis of chemical shift changes upon inhibitor binding highlights a characteristic pattern of allosteric network perturbations that is of relevance for future drug discovery activities aimed at development of conformationally-selective FGFR inhibitors.