Strausberg RL, Feingold EA, Grouse LH, et al."Aberrant promoter methylation and silencing of the RASSF1A gene in pediatric tumors and cell lines". "Albers-Schönberg disease (autosomal dominant osteopetrosis, type II) results from mutations in the ClCN7 chloride channel gene". Cleiren E, Bénichou O, Van Hul E, et al."Loss of the ClC-7 chloride channel leads to osteopetrosis in mice and man". "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16". "Locus heterogeneity of autosomal dominant osteopetrosis (ADO)". "The exon-intron architecture of human chloride channel genes is not conserved". Consortium: an integrated molecular analysis of genomes and their expression". Lennon G, Auffray C, Polymeropoulos M, Soares MB (1996)."Linkage of autosomal dominant radial drusen (malattia leventinese) to chromosome 2p16-21". "ClC-6 and ClC-7 are two novel broadly expressed members of the CLC chloride channel family". "Differentially expressed genes in autosomal dominant osteopetrosis type II osteoclasts reveal known and novel pathways for osteoclast biology" (PDF). ^ Coudert AE, Del Fattore A, Baulard C, Olaso R, Schiltz C, Collet C, Teti A, de Vernejoul MC (2014)."Novel MITF targets identified using a two-step DNA microarray strategy". ^ Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E (2008)."The expression of Clcn7 and Ostm1 in osteoclasts is coregulated by microphthalmia transcription factor". ^ Meadows NA, Sharma SM, Faulkner GJ, Ostrowski MC, Hume DA, Cassady AI (2007).^ "Entrez Gene: CLCN7 chloride channel 7".National Center for Biotechnology Information, U.S. This represents an advance in the study of NAD metabolism in Giardia spp. Double-reciprocal plots showed no cooperativity for this enzyme. Michaelis–Menten kinetics were observed for NMN and ATP, but saturation was not accomplished with NAMN, implying low affinity yet detectable activity with this substrate. Optimal reaction pH and temperature were 7.3 and 26 ☌. The recombinant protein (His-GlNMNAT) was purified by nickel-affinity binding and was used in direct in vitro enzyme assays assessed by C18-HPLC, verifying adenylyltransferase activity with both nicotinamide (NMN) and nicotinic acid (NAMN) mononucleotides. Subsequently, glnmnat-a was cloned into an expression vector. We first verified the identity of the sequences in silico. Using bioinformatics tools, we found two NMNAT sequences in Giardia lamblia ( glnmnat-a and glnmnat-b). There are two pathways for NAD biosynthesis, which converge at the step catalyzed by nicotinamide/nicotinate mononucleotide adenylyltransferase (NMNAT, EC 2.7.7.1/18). This molecule is widely known as a coenzyme in multiple redox reactions and as a substrate in cellular processes such as synthesis of Ca 2+ mobilizing agents, DNA repair and gene expression regulation. One of the most important and conserved metabolic pathways is the biosynthesis of nicotinamide adenine dinucleotide (NAD). In addition to its clinical importance, this parasite is of special biological interest due to its basal evolutionary position and simplified metabolism, which has not been studied thoroughly. Giardiasis leads to poor absorption of nutrients, severe electrolyte loss and growth retardation. Giardia lamblia is an intestinal protozoan parasite that causes giardiasis, a disease of high prevalence in Latin America, Asia and Africa.
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