The activity of BcsZ of Typhimurium and its role in -plants interactions.

is one of the most common human pathogens associated with fresh produce outbreaks. The present study suggests that expression of BcsZ, one of the proteins in the complex, enhances the survival of Typhimurium on parsley. BcsZ demonstrated glucanase activity with the substrates carboxymethylcellulose and crystalline cellulose, and was responsible for a major part of the .

N-VEGF, the Autoregulatory Arm of VEGF-A.

Vascular endothelial growth factor A (VEGF-A) is a secreted protein that stimulates angiogenesis in response to hypoxia. Under hypoxic conditions, a non-canonical long isoform called is concomitantly expressed with . Once translated, L-VEGF is proteolytically cleaved to generate N-VEGF and VEGF-A.

[Anticoagulant treatment in pericardial effusion--a therapeutic dilemma].

Anticoagulant treatment for acute myocardial infarction (AMI) and pericardial effusion is controversial, since the treatment might cause hemopericardium and tamponade. On the other hand, anticoagulants are strongly indicated in many situations in AMI, including: left ventricular thrombus, unstable angina, severe heart failure, deep vein thrombophlebitis, pulmonary embolism, atrial fibrillation, as part of thrombolytic treatment, and during cardiac catheterization. We describe a 70-year-old man who presented with both pericardial effusion and a left ventricular thrombus 3 weeks after an extensive, anterior wall AMI.

Subcellular co-localization and potential interaction of glucuronosyltransferases with nascent proteochondroitin sulphate at Golgi sites of chondroitin synthesis.

Microsomal membranes from chick embryo epiphyseal cartilage were fractionated by equilibrium sucrose-density-gradient centrifugation and assayed for GlcA (glucuronic acid) transferase I (the enzyme that transfers GlcA from UDP-GlcA to Gal-Gal-Xyl of proteochondroitin linkage region), for comparison with GlcA transferase II (the GlcA transferase of chondroitin polymerization). Gal(beta1-3)Galbeta1-methyl (disaccharide) and GalNAc(beta1-4)GlcA(beta1-3)GalNAc(beta1-4) GlcA(beta1-3)GalNAc(pentasaccharide) were used respectively as acceptors of [14C]GlcA from UDP-[14C]GlcA. Distributions of the two GlcA transferase activities in the sucrose-density-gradient fractions were compared with each other and with the previously reported distribution of the activities of Gal transferases (UDP-Gal to ovalbumin, and to xylose of the proteochondroitin linkage region) and GalNAc (N-acetylgalactosamine) transferase II of chondroitin polymerization.

Biosynthesis of chondroitin sulfate. Purification of glucuronosyl transferase II and use of photoaffinity labeling for characterization of the enzyme as an 80-kDa protein.

A photoaffinity analogue, [beta-32P]5-azido-UDP-GlcA, was used to photolabel the enzymes that utilize UDP-GlcA in cartilage microsomes and rat liver microsomes. SDS-polyacrylamide gel electrophoresis analysis of photolabeled cartilage microsomes, which are specialized in chondroitin sulfate synthesis, showed a major radiolabeled band at 80 kDa and other minor radiolabeled bands near 40 and 60 kDa. Rat liver microsomes, which are enriched for enzymes of detoxification by glucuronidation, had a different pattern with multiple major labeled bands near 50-60 and 35 kDa.

Purification, photoaffinity labeling, and characterization of a single enzyme for 6-sulfation of both chondroitin sulfate and keratan sulfate.

A soluble sulfotransferase that could 6-sulfate both chondroitin sulfate and corneal keratan sulfate was purified 27,500-fold using a sequence of affinity chromatographic steps with heparin-Sepharose, wheat germ agglutinin-agarose, and 3',5'-ADP-agarose. The essentially pure enzyme had a specific activity 40 times greater than the most purified chondroitin 6-sulfotransferase previously reported and exhibited a single sharp Coomassie Blue-stained and a heavy silver-stained protein band of 75 kDa on SDS-polyacrylamide gel electrophoresis. Chromatography of the purified enzyme on Sephacryl demonstrated a size of 150 kDa, which indicated that the native enzyme exists as a dimer.

Effects of brefeldin A on the localization of chondroitin sulfate-synthesizing enzymes. Activities in subfractions of the Golgi from chick embryo epiphyseal cartilage.

Membranes from brefeldin A-treated and untreated chick embryo epiphyseal cartilage were fractionated separately by equilibrium sucrose density gradient centrifugation. Fractions were assayed for Gal I transferase, Gal II transferase, Gal ovalbumin transferase, chondroitin polymerization on endogenous acceptors, GalNAc transfer to exogenous chondroitin hexasaccharide, and sulfate transfer to exogenous chondroitin. Gal I transferase and Gal II transferase activities were found in heavier cis- and medial-Golgi fractions, but with distributions different from each other.

Effects of brefeldin A on the synthesis of chondroitin 4-sulfate by cultures of mouse mastocytoma cells.

Mouse mastocytoma cells were cultured with brefeldin A in medium containing [35S]sulfate and [3H]glucosamine in order to determine the effects of this fungal metabolite on the formation of chondroitin 4-sulfate by these cells. There was a marked reduction in the incorporation of [35S]sulfate into the glycosaminoglycan which was approximately equal to the reduction in the incorporation of [3H]hexosamine into the same molecule. The chondroitin 4-sulfate chain size was greatly diminished, while the number of chains appeared to remain relatively constant, indicating that the brefeldin A partially disrupted the polymerizing system, but had little effect upon movement of the nascent proteochondroitin to the site for chondroitin polymerization and sulfation.

[Improvement of practical assistance to public health facilities in detecting cancer pathology].

Weekly consultations have been offered to general public at the Institute since 1982. This resulted in a spontaneous distribution of patients into high-risk groups on the basis of psychological considerations. The rate of neoplasm detection has grown to 4.

[Changes in the concentration of free radicals in the organs of rats during experimental chemotherapy of Guérin tumor].

Kinetic description of the changes of free radical concentration in Geren tumour tissue and in the tissues of liver, lungs, brain at chemotherapeutic application of licopine, selenium and cyclophosphane was obtained by ESR method. Licopine application decreases free radical concentration in the tumour (after the stage of a short-time rise). Similar effects during some periods of the action of carotinoids and of a valuable inhibitor of oxidation--selenium, as well as the citostatics of cyclophosphane allow to suggest that the application of the drug of vitamine A group is expedient in tumour therapy.