Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0034186 (pyelonephritis)
 6,144 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Urease (urea amidohydrolase; EC 3.5.1.5) catalyzes the hydrolysis of urea to yield ammonia and carbamate. The latter compound spontaneously decomposes to yield another molecule of ammonia and carbonic acid. The urease phenotype is widely distributed across the bacterial kingdom, and the gene clusters encoding this enzyme have been cloned from numerous bacterial species. The complete nucleotide sequence, ranging from 5.15 to 6.45 kb, has been determined for five species including Bacillus sp. strain TB-90, Klebsiella aerogenes, Proteus mirabilis, Helicobacter pylori, and Yersinia enterocolitica. Sequences for selected genes have been determined for at least 10 other bacterial species and the jack bean enzyme. Urease synthesis can be nitrogen regulated, urea inducible, or constitutive. The crystal structure of the K. aerogenes enzyme has been determined. When combined with chemical modification studies, biophysical and spectroscopic analyses, site-directed mutagenesis results, and kinetic inhibition experiments, the structure provides important insight into the mechanism of catalysis. Synthesis of active enzyme requires incorporation of both carbon dioxide and nickel ions into the protein. Accessory genes have been shown to be required for activation of urease apoprotein, and roles for the accessory proteins in metallocenter assembly have been proposed. Urease is central to the virulence of P. mirabilis and H. pylori. Urea hydrolysis by P. mirabilis in the urinary tract leads directly to urolithiasis (stone formation) and contributes to the development of acute pyelonephritis. The urease of H. pylori is necessary for colonization of the gastric mucosa in experimental animal models of gastritis and serves as the major antigen and diagnostic marker for gastritis and peptic ulcer disease in humans. In addition, the urease of Y. enterocolitica has been implicated as an arthritogenic factor in the development of infection-induced reactive arthritis. The significant progress in our understanding of the molecular biology of microbial ureases is reviewed.
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PMID:Molecular biology of microbial ureases. 756 14

The aim of the study was to evaluate the lipid parameters of blood in patients with total or partial clinico-laboratory remission of chronic pyelonephritis (CP), and the role of these parameters in their metabolic status. The subjects were 93 CP patients (mean age 47.4 +/- 0.8 years). The metabolic status of each patient was evaluated according to the activity of the inflammatory reaction, glomerular filtration, and reabsorption, as well as indices of lipid exchange, lipid peroxidation (LPO), and antioxidative protection (AOP). Factor analysis revealed that lipid exchange and LPO-AOP system disturbances played a significant role in the metabolic status of CP patients with total or partial clinico-laboratory remission. There were three variants of these disturbances: an increased serum level of cholesterol (CS) of very low-density lipoproteins (VLDLP), and LPO-AOP disbalance; light hypercholesterinemia, an increased level of VLDLP CS, low-density lipoproteins (LDLP) CS, and a decreased level of LPO-AOP parameters; an increased level of total CS, VLDLP CS, LDLP CS, apoprotein B, and a prominent depression of AOP.
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PMID:[Disturbances of lipid exchange and peroxidation system in patients with chronic pyelonephritis]. 1682 82