Nuclear factor kappa B plays a pivotal role in renal protection against apoptosis during unilateral ureteral obstruction in rats

Obstructive nephropathy constitutes a major cause of renal impairment in children. Unilateral ureteral obstruction [UUO] model of renal injury in rat is characterized by interstitial inflammatory cell infiltration, nuclear factor kappa b [NF-kappa B] activation, oxidative stress, fibrosis, and apoptosis. Curcumin, the major component found in turmeric spice has been reported to provide protection against the renal interstitial inflammation and fibrosis elicited by UUO in addition to renal tubular cell apoptosis. The present work study examined the effect of curcumin-rich diet [5% w/w] on the apoptotic pathway induced by UUO in rats after 30 days of legation. 30 male Wistar rats were subjected to UUO. The animals were treated with curcumin rich diet. Obstructed and contralateral kidneys were collected at the day 30, post-surgery and analyzed for inflammatory change 409s and apoptosis-related markers. Kidney functions [serum creatinine and urea], mRNA expressions of TNF- alpha, NF-kappa B and caspase 8, histological examination by hematoxylin and eosin, Mallory Trichrome were carried out. Ureteral obstruction was associated with increase in serum creatinine, and urea. mRNA expression of TNF- alpha and caspase 8 in obstructed kidney as well as NF-kappa B in both kidneys were also increased in comparison to sham-operated rats [p<0.05]. Histological examination showed absence of renal tubules, medulla, and damaged cortex glomeruli. Curcumin-rich diet administration demonstrated significant decrease [p<0.05] in all the previous biochemical and molecular parameters except NF-kappa B expression. These changes may attributed to the protective role of curcumin-rich diet as revealed by the reappearance of large numbers of cortex glomeruli and some renal tubules and delaying of the apoptotic stage till fibrosis. The curcumin-rich diet administration can delay apoptosis without modulating NF-kappa B which may protect the mesingial cells from the apoptotic stimuli TNF-alpha

Distribution and biosynthesis requirements for L-Asparaginase activities in bacteria and yeasts

Screening of 40 bacterial cultures, belonging to 16 genera and 24 yeasts, belonging to 10 genera, for levels of L-asparaginase activities was carried using a simple medium with L-asparagine asthe major carbon and nitrogen source. Among bacteria highestenzyme levels were noted for certain cultures of Erwinia, Arthrobacter and Serratia; whereas some species of Rlhodotorula, Debaryomyces and Schwanniomyces yielded the highest L-asparaginase activities among the yeast cultures tested. The use of cells stored frozen for a few days was necessary to obtain reliable information about the enzyme levels in the surveyed cultures. Physiological studies on selected cultures have revealed that the enzyme is inducible with L-asparagine and some structurally-related metabolites in Rhodvmruia rubra and Aerobacter aerogenes, whereas in several other cultures the enzyme is formed constitutively. Ammonium ion was a potent supressor of enzyme biosynthesis. Highest enzym levels were detected in cultures during the exponential and at the beginning of the stationary phases of growth whereas a wide variation in the enzyme stability was noted in different cultures upon extended incubation

Formation and properties of L-Glutaminase and L-Asparaginase activities in pichia polymorpha

An ascogenous yeast with high potentialities for L-glutaminase and L-asparaginase formation was isolated from Egyptian soils by the application of the method of enrichment culture. The organism, identified as pichia polymorpha, was obtained through the enrichment of the soil samples with a simple medium containing 0.5% L-glutamine as a major carbon and nitrogen source at low pH values. - The amidase activities were produced constitutively on a variety of media irrespective to the presence of their substrates in the growth medium. The assays of enzyme activity have revealed that optimum pH values for L-glutamine and L-asparagine hydrolysis are 6 and 6.7 respectively. The L-asparaginase activity of the cells were heat-stable at least up to 10 min at 600. The enzyme exhibited apparent km of 1.37 x 10[-2] M and 1.95 x 10[-2] M for L-asparagine and L-glutamine respectively. No metal requirements were detected for the amidase activities of the organism under study