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)

We investigated the relationship between urinary prostaglandin E2 (UPGE2), kallikrein (UKal), graft function and complications after renal transplantation in 11 patients. Grafts of 9 patients were from living-related donors (LRD), and other 2 patients were from a cadaveric donor (CAD). UPGE2 was measured by the radio immunoassay, and UKal was measured by the amidolytic method using Pro-Phe-Arg-MCA. The results were as follows. 1. In 5 of 6 patients from LRD without acute rejection episode (ARE), both UPGE2 and UKAL were within normal and/or slightly less than normal. UKal values of the other patient were high in his donor. 2. In 2 of 3 recipients from LRD who experienced ARE, UKal increased prior to ARE. UPGE2 also increased at the time of ARE, but it showed a periodic rise in the stable condition. 3. In 1 of 2 recipients from CAD, UKal exhibited a transient elevation at the time of acute tubular necrosis (ATN) and pyelonephritis while UPGE2 was low. In another recipient, UKal was almost within normal range at the time of ATN, and UPGE2 showed a periodic rise. 4. A significant correlation was seen between UKal, UPGE2 and UAld in the recipients from LRD without ARE (except 1 patient who showed high UKal values). However, the correlation was blurred inclusive of values in the patients who experienced ARE or other complications. There was no relationship between UKal, UPGE2, creatinine clearance, urine volume and urinary sodium. 5. Soybean trypsin inhibitor (STI) was used for the confirmation of specificity of the amidolytic method.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Urinary prostaglandin E2 and kallikrein-like activity excretion in renal transplant recipients]. 235 62

The uptake of nutrients and activities of membrane enzymes in the kidney were investigated using renal brush border membrane (BBM) vesicles in acute pyelonephritis in rats. A significant decrease (P less than 0.001) in the uptake of D-glucose and L-phenylalanine was observed in both the unobstructed right and obstructed left kidney, while there was a significant increase (P less than 0.001) in the uptake of L-alanine in the left kidney of pyelonephritic rats, demonstrating disturbances in the reabsorption of the glucose and aminoacids in the kidneys. Vmax of alkaline phosphatase, leucine-amino-peptidase and maltase was found to be decreased in the left kidney, suggesting that there was a reduction in the active enzyme molecule number. Km of alkaline phosphatase and leucine-aminopeptidase remained unchanged, while km of maltase decreased in both the right and left kidneys. An increase in the Vmax of alkaline phosphatase and leucine-aminopeptidase and substrate affinity of the maltase in the right kidney demonstrated a compensatory phenomenon for the malfunctioning of the left kidney. This is the first report demonstrating alterations in reabsorption of nutrients and BBM enzymes in experimental pyelonephritis.
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PMID:Pyelonephritis alters the reabsorption of nutrients and brush border membrane enzymes of rat kidney. 390 22

Chemotaxis is one of the most important functions of the polymorphonuclear leukocyte (PMN). In the host defense against pyelonephritis, the renal medulla is a site of interaction between bacteria and PMNs. At this site the osmotic pressure is elevated due to a high concentration of NaCl and urea. We evaluated the in vitro chemotactic activity of PMNs under the hyperosmolar conditions created by high concentrations of NaCl and urea. This activity was suppressed by the stimulation of opsonized zymosan and formyl-methionyl-leucyl-phenylalanine. The inhibition of chemotaxis was partially preserved by phosphoenolpyruvic acid (PEP), a precursor of adenosine triphosphate (ATP), in hyperosmolar NaCl but not in urea. The intracellular content of ATP was increased by supplementing the hyperosmolar NaCl with PEP. These observations suggest that inhibition of the chemotactic activity of PMNs is due to differing mechanisms for each NaCl and urea, and that PEP may protect the PMNs against hyperosmolar NaCl by maintaining ATP content.
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PMID:Suppression of chemotactic activity of neutrophils in hyperosmotic conditions comparable to the renal medulla: partial preservation by phosphoenolpyruvate. 843 19

Recent work has demonstrated that expression of type 1 fimbriae is repressed by PapB, a regulator of pyelonephritis-associated pili (P-pili). PapB belongs to family of related adhesin regulators, for which consensus residues required for DNA binding and oligomerization have been identified. Of the regulators tested in this study, PapB, SfaB (S-fimbriae) and PefB (Salmonella enterica serovar Typhimurium--plasmid-encoded fimbriae) repressed FimB-promoted off-to-on inversion of the fim switch, although complete repression was only demonstrated by PapB. DaaA, FaeB, FanA, FanB and ClpB had no effect on fim switching. In addition, only PapB stimulated FimE-promoted on-to-off inversion. Deletion analysis demonstrated that this specificity resides in the carboxy terminal of the protein, and not the amino terminal, with the central region being homologous among the family members. Exchange of Leu(82) and Ile(83) of PapB for the equivalent residues from the DaaA protein (Phe and Gln) within the carboxy terminal virtually abolished cross-talk activity. Whereas PapB can bind to a region around the left inverted repeat of the fim switch, DaaA and the PapB double mutant were effectively unable to bind this region. A previously characterized PapB DNA binding mutant also failed to bind to this region and failed to inhibit FimB activity at the fim switch. Thus, repression of fim expression appears unique to PapB and SfaB within E. coli and requires DNA binding involving amino acid residues located both within the homologous core and in the heterogeneous carboxy terminus. The variation in the carboxy terminus between the PapB family members explains their differential effects on fim. This mechanism of cross-talk seems restricted to the P and S family adhesins with type 1 fimbriae and may ensure variable and sequential expression of adhesins during urinary tract infections.
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PMID:PapB paralogues and their effect on the phase variation of type 1 fimbriae in Escherichia coli. 1170 57