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PubMed2002

Serotypic and antibiotic susceptibility pattern of Salmonella species isolated from cases of gastroenteritis at Infectious Diseases Hospital (IDH), Delhi from 1997-2000.

A total number of 11,551 stool samples/rectal swabs obtained from acute gastroenteritis cases admitted at Infectious Diseases Hospital (IDH), Delhi during a period of four years from 1997-2000 were processed at National Institute of Communicable Diseases (NICD), Delhi to look for the presence of enteropathogens. One hundred twelve Salmonellae species belonging to different serotypes were isolated. The commonest species was S. typhimurium, accounting for 31% of isolates, followed by S. weltervreden (19%), S. litchfield (15%) and others. 61% of S. typhimurium isolates depicted multidrug resistance to Chloramphenicol, Tetracycline, Furazolidone and Co-trimoxazole. However, none showed resistance to quinolones and third generation cephalosporins. Estimation of minimum inhibitory concentration (MIC) for S. typhimurium against Ampicillin, Chloramphenicol and Cephalothin was carried out by E test. A good correlation between disc diffusion technique and E test was observed.

Adolescent↗
PubMed1994

Close linkage of the dominant cataract mutations (Cat-2) with Idh-1 and cryge on mouse chromosome 1.

The murine dominant gene Cat-2 was located on chromosome 1 between the loci of fuzzy and leaden. Subsequent linkage analysis revealed one recombinant between Cat-2t and isocitrate dehydrogenase-1, and one between Cat-2t and gamma E-crystallin among 338 offspring in three-point backcrosses. The resulting genetic distance between the loci is 0.3 +/- 0.3 cM. The very close linkage between the Cat-2 and the gamma-crystallin gene cluster together with the finding of reduced gamma-crystallin transcripts in mutant lenses suggest strongly that the gamma-crystallin genes may be candidate genes for the Cat-2 mutations.

Animals↗
PubMed1987

Mapping of the mouse fibronectin gene (Fn-1) to chromosome 1: conservation of the Idh-1-Cryg-Fn-1 synteny group in mammals.

Restriction fragment length polymorphisms (RFLPs) were observed in BamHI-digested mouse DNA probed with a cDNA for human fibronectin. Analysis of the inheritance of fibronectin RFLPs in AKXD and SWXJ recombinant inbred strains of mice mapped the locus, Fn-1, to the midregion of mouse chromosome 1 about 4 cM distal from the loci encoding gamma-crystallins (Cryg). Loci homologous to genes in the centromeric third of mouse chromosome 1 are also syntenic in rats, humans, and cattle and may, therefore, mark a large conserved chromosomal segment of the mammalian genome.

Animals↗
PubMed1972

Assignment of three human genes to chromosomes (LDH-A to 11, TK to 17, and IDH to 20) and evidence for translocation between human and mouse chromosomes in somatic cell hybrids (thymidine kinase-lactate dehydrogenase A-isocitrate dehydrogenase-C-11, E-17, and F-20 chromosomes).

Independently derived man-mouse somatic cell hybrids and their derivative subclones show a positive correlation between the expression of human lactate dehydrogenase A subunits and the occurrence of the human C-11 chromosome. Data are also presented that confirm the previously reported linkage of the thymidine kinase locus to the E-17 chromosome. A translocation of the E-17 chromosome provides presumptive evidence for the assignment of the thymidine kinase locus to the long arm segment of the E-17 chromosome. This translocation also provides evidence for translocation between man and mouse chromosomes in somatic cell hybrids. A presumptive association between the human phenotype for isocitrate dehydrogenase and the human F group is also described. Identification of specific human chromosomes was achieved by the application of several new cytological techniques: measurement of chromosome arm length, in situ annealing with mouse satellite complementary RNA, constitutive heterochromatin staining with Giemsa, and quinacrine mustard fluorochromatic staining.

Animals↗
PubMedDate not supplied

Linkage of an IDH locus with sex and two lethals in Aedes aegypti.

A previously unmapped isocitrate dehydrogenase (DH) locus has been mapped on chromosome 1 in Aedes aedes aegypti. No recombination between this and sex was observed in any of the several hundred instances where crossing over could have been detected. Within an isofemale line from Daker, two ldh-1 alleles are in linkage disequilibrium with two lethal loci. The two lethals complement one another, and show no recombination with sex or ldh-1. Recombination between bz and ldh-1 was demonstrated, placing ldh-1 very close to Me and sw. The results show that in two natural populations, ldh-1 and sex are in linkage disequilibrium with each other and most probably with the two lethal loci also. The distribution of ldh-1 variation world-wide and the implications of sex-linked lethals are discussed.

Aedes↗
PubMed2003

The effect of frequent or occasional dialysis-associated hypotension on survival of patients on maintenance haemodialysis.

BACKGROUND: While frequent or occasional symptomatic intradialytic hypotension (IDH) may influence patient well-being, its effects on survival-independent of comorbidities-has not previously been investigated. In this study, therefore, our objective was to assess the effect of frequent IDH (f-IDH) or occasional IDH (o-IDH) on survival. METHODS: During a 10 month run-in period in 1998, 77 patients with f-IDH (> or =10 hypotensive events/10 months, responding only to medical intervention) and 101 patients with o-IDH (1 or 2 events/10 months) were identified among all 958 patients of a dialysis network. Eighty-five patients who had no hypotensive episodes (no-IDH) during this run-in phase served as controls. Patients were followed for a median of 27 months (range: 0.3-37) and survival of patients in the three groups was compared by log-rank test. Independent association of f-IDH and o-IDH with survival, compared with no-IDH, was assessed by a proportional hazards model that included patient demographics, laboratory data and antihypertensive medication as well as comorbidity. RESULTS: Forty-five patients (58%) with f-IDH, 47 (47%) with o-IDH and 33 (39%) with no-IDH died during the follow-up. Mortality rates (deaths/100 patient years) were 37 (log-rank P = 0.013 vs no-IDH), 26 (log-rank P = 0.375 vs no-IDH) and 21 in the three groups, respectively. This indicates significantly decreased survival in patients with f-IDH as compared to those with no-IDH. In multivariate proportional hazards regression, however, where age, sex, time spent on dialysis, presence of coronary heart disease, diabetes, Kt/V, albumin level and use of beta-blockers, calcium-channel blockers and long-acting nitrates has been adjusted for, neither f-IDH nor o-IDH was associated with survival. CONCLUSIONS: Mortality in patients with f-IDH is significantly higher than in those without such events. After adjustments for covariates, however, there is no independent effect of frequent or occasional episodes of IDH on mortality.

Adult↗
PubMedDate not supplied

Isocitrate dehydrogenase kinase/phosphatase.

In Escherichia coli, isocitrate dehydrogenase (IDH) is regulated by phosphorylation. This phosphorylation cycle is catalyzed by an unusual, bifunctional protein:IDH kinase/phosphatase. IDH kinase/phosphatase is expressed from a single gene, aceK, and both activities are catalyzed by the same polypeptide. The amino acid sequence of IDH kinase/phosphatase does not exhibit the characteristics which are typical of other protein kinases, although it does contain a consensus ATP binding site. The available evidence suggests that the IDH kinase and IDH phosphatase reactions occur at the same active site and that the IDH phosphatase reaction results from the back reaction of IDH kinase tightly coupled to ATP hydrolysis. The function of the IDH phosphorylation cycle is to control the flux of isocitrate through the glyoxylate bypass. This pathway is essential for growth on acetate because it prevents the quantitative loss of the acetate carbons as CO2 in the Krebs' cycle. IDH kinase/phosphatase monitors general metabolism by responding to the levels of a wide variety of metabolites, many of which activate IDH phosphatase and inhibit IDH kinase. The ability of IDH kinase/phosphatase to monitor general metabolism allows. the IDH phosphorylation cycle to compensate for substantial perturbations of the system, such as a 15-fold overproduction of IDH. The significance of the cellular level of IDH kinase/phosphatase has also been evaluated. The level of this protein is in great excess of that required for steady-state growth on acetate. In contrast, IDH kinase/phosphatase is, in some cases, rate-limiting for the dephosphorylation of IDH which results when preferred carbon sources are added to cultures growing on acetate.

Amino Acid Sequence↗
PubMed2006

Two isocitrate dehydrogenases from a psychrophilic bacterium, Colwellia psychrerythraea.

Two structurally different monomeric and dimeric types of isocitrate dehydrogenase (IDH; EC 1.1.1.42) isozymes were confirmed to exist in a psychrophilic bacterium, Colwellia psychrerythraea, by Western blot analysis and the genes encoding them were cloned and sequenced. Open reading frames of the genes (icd-M and icd-D) encoding the monomeric and dimeric IDHs of this bacterium, IDH-M and IDH-D, were 2,232 and 1,251 bp in length and corresponded to polypeptides composed of 743 and 416 amino acids, respectively. The deduced amino acid sequences of the IDH-M and IDH-D showed high homology with those of monomeric and dimeric IDHs from other bacteria, respectively. Although the two genes were located in tandem, icd-M then icd-D, on the chromosomal DNA, a Northern blot analysis and primer extension experiment revealed that they are transcribed independent of each other. The expression of the monomeric and dimeric IDH isozyme genes in C. maris, a psychrophilic bacterium of the same genus as C. psychrerythraea, is known to be induced by low temperature and acetate, respectively, but no such induction in the expression of the C. psychrerythraea icd-M and icd-D genes was detected. IDH-M and IDH-D overexpressed in Escherichia coli were purified and characterized. In C. psychrerythraea, the IDH-M isozyme is cold-active whereas IDH-D is mesophilic, which is similar to C. maris that contains both cold-adapted and mesophilic isozymes of IDH. Experiments with chimeric enzymes between the cold-adapted monomeric IDHs of C. psychrerythraea and C. maris (IDH-M and ICD-II, respectively) suggested that the C-terminal region of the C. maris IDH-II is involved in its catalytic activity.

Alteromonadaceae↗
PubMed2000

Locations of the regulatory sites for isocitrate dehydrogenase kinase/phosphatase.

Isocitrate dehydrogenase (IDH)(1) of Escherichia coli is regulated by a bifunctional protein, IDH kinase/phosphatase. In this paper, we demonstrate that the effectors controlling these activities belong to two distinct classes that differ in mechanism and in the locations of their binding sites. NADPH and isocitrate are representative members of one of these effector classes. NADPH inhibits both IDH kinase and IDH phosphatase, whereas isocitrate inhibits only IDH kinase. Isocitrate can "activate" IDH phosphatase by reversing product inhibition by dephospho-IDH. Mutations in icd, which encodes IDH, had parallel effects on the binding of these ligands to the IDH active site and on their effects on IDH kinase and phosphatase, indicating that these ligands regulate IDH kinase/phosphatase through the IDH active site. Kinetic analyses suggested that isocitrate and NADPH prevent formation of the complex between IDH kinase/phosphatase and its protein substrate. AMP, 3-phosphoglycerate, and pyruvate represent a class of regulatory ligands that is distinct from that which includes isocitrate and NADPH. These ligands bind directly to IDH kinase/phosphatase, a conclusion which is supported by the observation that they inhibit the IDH-independent ATPase activity of this enzyme. These effector classes can also be distinguished by the observation that mutant derivatives of IDH kinase/phosphatase expressed from aceK3 and aceK4 exhibited dramatic changes in their responses to AMP, 3-phosphoglycerate, and pyruvate but not to NADPH and isocitrate.

Adenosine Monophosphate↗
PubMed2001

Clinical case-based approach to understanding intradialytic hypotension.

The approach to end-stage renal disease (ESRD) patients who develop intradialytic hypotension (IDH) encompasses an understanding of the pathophysiology, appropriate dialysis prescription modification, application of newer pharmacologic therapies, and development of strategies for prevention. Patients should have a "minimal data set" as part of their predialysis assessment. This information is critical to prescription modifications that may help decrease the risk for IDH. Individuals at "high risk" for IDH should be kept to a "safe zone" for dialysis ultrafiltration (</=3% of body weight). Specific maneuvers that may decrease the risk for IDH include adjustment of the dialysate sodium or calcium concentration and dialysate temperature. The first priority for patients developing IDH should be the stabilization of the blood pressure and improvement in the patient's symptomology. Pharmacologic intervention should be considered for patients who require repeat interventions for IDH. "At-risk" patients with a strong cardiac history should undergo an assessment of their cardiovascular status if IDH episodes occur. The use of pharmacologic therapy, ie, midodrine, alone or in combination with prescription modification, can be helpful in decreasing interventions required for IDH. Noncompliance and high interdialytic weight gain in the setting of left ventricular hypertrophy (LVH) and diastolic dysfunction can increase the risk of IDH. Assessment of antihypertensive medications should be performed on a regular basis to determine the correct dosing schedule for patients with hypertension who develop IDH. Coronary flow reserve may be compromised in patients with LVH, adding to the risk for perfusion injury with low blood pressure. Increasing the dialysate calcium concentration may decrease the incidence of arrhythmogenicity in certain patients. Patients with low body temperature may benefit most from cool dialysate. Unit personnel should be aware of the potential link between hypotension and the increased relative risk for death in ESRD patients. Clinical training sessions on IDH risk recognition and appropriate treatment should be implemented within the dialysis unit. Because repeated bouts of IDH can be disruptive to the smooth efficiency of unit operations, attention to prevention as well as acute intervention of IDH is important. Preventive strategies can be developed in each unit to decrease the number of future IDH events. Considering the importance of hypotension in overall patient survival, attention to identifying the percentage of patients in each unit who experience IDH and/or who present with low blood pressure (systolic <110 mm Hg) should be tracked as a quality assurance initiative.

Adult↗
PubMed1987

Isocitrate dehydrogenase kinase/phosphatase exhibits an intrinsic adenosine triphosphatase activity.

In Escherichia coli, isocitrate dehydrogenase (IDH) is regulated by reversible phosphorylation. The bifunctional enzyme which catalyzes this phosphorylation cycle, IDH kinase/phosphatase, also exhibits a specific ATPase activity. Mutant derivatives of this protein which are nearly devoid of IDH phosphatase activity retain both IDH kinase and ATPase activity, indicating that ATP hydrolysis does not result from the cyclic phosphorylation of IDH. However, the IDH kinase and ATPase activities of these mutant proteins differ significantly from those of the wild-type IDH kinase/phosphatase expressed from the parental allele. This observation suggest that IDH kinase and IDH phosphatase do not reside on structurally independent domains. In contrast to many enzymes which catalyze kinetically unfavorable side reactions, the maximum velocity of the ATPase substantially exceeded those of IDH kinase and IDH phosphatase. ATP hydrolysis was only partially inhibited by phospho- and dephospho-IDH, with saturating levels of phospho-IDH decreasing the rate of ATP hydrolysis by a factor of approximately 5. Even in the presence of near-saturating concentrations of phospho-IDH, the rate of ATP hydrolysis was 4-fold greater than the rate of the cyclic phosphorylation of IDH.

Adenosine Triphosphatases↗
PubMed2002

Characterization of isocitrate dehydrogenase from the green sulfur bacterium Chlorobium limicola. A carbon dioxide-fixing enzyme in the reductive tricarboxylic acid cycle.

Isocitrate dehydrogenase (IDH) catalyzes the reversible conversion between isocitrate and 2-oxoglutarate accompanied by decarboxylation/carboxylation and oxidoreduction of NAD(P)+ cofactor. While this enzyme has been well studied as a catabolic enzyme in the tricarboxylic acid (TCA) cycle, here we have characterized NADP-dependent IDH from Chlorobium limicola, a green sulfur bacterium that fixes CO2 through the reductive tricarboxylic acid (RTCA) cycle, focusing on the CO2-fixation ability of the enzyme. The gene encoding Cl-IDH consisted of 2226 bp, corresponding to a polypeptide of 742 amino acid residues. The primary structure and the size of the recombinant protein indicated that Cl-IDH was a monomeric enzyme of 80 kDa distinct from the dimeric NADP-dependent IDHs predominantly found in bacteria or eukaryotic mitochondria. Apparent Michaelis constants for isocitrate (45 +/- 13 microm) and NADP+ (27 +/- 10 microm) were much smaller than those for 2-oxoglutarate (1.1 +/- 0.5 mm) and CO2 (1.3 +/- 0.3 mm). No significant differences in kinetic properties were observed between Cl-IDH and the dimeric, NADP-dependent IDH from Saccharomyces cerevisiae (Sc-IDH) at the optimum pH of each enzyme. However, in contrast to the 20% activity of Sc-IDH toward carboxylation as compared with that toward decarboxylation at pH 7.0, the activities of Cl-IDH for both directions were almost equivalent at this pH, suggesting a more favorable property of Cl-IDH than Sc-IDH as a CO2-fixation enzyme under physiological pH. Furthermore, we found that among various intermediates, oxaloacetate was a competitive inhibitor (K(i) = 0.35 +/- 0.04 mm) for 2-oxoglutarate in the carboxylation reaction by Cl-IDH, a feature not found in Sc-IDH.

Base Sequence↗