Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0031511 (pheochromocytoma)
 14,622 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The region of the genome encoding the glucose-6-phosphate dehydrogenase gene zwf was analysed in a unicellular cyanobacterium, Synechococcus sp. PCC 7942, and a filamentous, heterocystous cyanobacterium, Anabaena sp. PCC 7120. Comparison of cyanobacterial zwf sequences revealed the presence of two absolutely conserved cysteine residues which may be implicated in the light/dark control of enzyme activity. The presence in both strains of a gene fbp, encoding fructose-1,6-bisphosphatase, upstream from zwf strongly suggests that the oxidative pentose phosphate pathway in these organisms may function to completely oxidize glucose 6-phosphate to CO2. The amino acid sequence of fructose-1,6-bisphosphatase does not support the idea of its light activation by a thiol/disulfide exchange mechanism. In the case of Anabaena sp. PCC 7120, the tal gene, encoding transaldolase, lies between zwf and fbp.
 ...
PMID:A comparison of gene organization in the zwf region of the genomes of the cyanobacteria Synechococcus sp. PCC 7942 and Anabaena sp. PCC 7120. 856 7

A mutant (M45) of the cyanobacterium Synechococcus sp. strain PCC 7942, which is defective in active transport of nitrate, was used for the studies of the nitrogen regulation of the genes involved in nitrate and CO2 assimilation. In a medium containing 30 mM nitrate as the nitrogen source, M45 grew under constant stress of nitrogen deficiency and accumulated a five-times-larger amount of the transcript of nirA, the gene for nitrite reductase, compared with nitrate-grown wild-type cells. By contrast, the level of the transcript of rbcL, the gene for the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase, was 40% of the wild-type level. Addition of ammonium to the culture of M45 abolished the accumulation of the nirA transcript and stimulated the accumulation of the rbcL transcript, showing that ammonium repressed and activated the transcription of nirA and rbcL, respectively. Glutamine, the initial product of ammonium fixation, also showed negative and positive effects on nirA and rbcL, respectively. One of the metabolites of glutamine, carbamoylphosphate, and its decomposition product, cyanate, were found to repress nirA and also to markedly activate rbcL. Cyanate negatively regulated another ammonium-repressible gene, glnA, but had no effect on the psbAI and rps1 genes. The effects of cyanate were not ascribable to the ammonium and CO, resulting from its decomposition. These findings suggested that cyanate may act as a regulator of the ammonium-responsive genes involved in carbon and nitrogen assimilation in the cyanobacterium.
 ...
PMID:Regulation by cyanate of the genes involved in carbon and nitrogen assimilation in the cyanobacterium Synechococcus sp. strain PCC 7942. 862 39

This study compares the outcome of laparoscopic adrenalectomy (LpA) in 23 patients using CO2 insufflation with the outcome of this procedure in another 8 patients with pheochromocytoma (7 unilateral, 1 bilateral) using helium for pneumoperitoneum. The adrenal lesions in the first group included nonfunctional adenoma (n = 3), aldosterone adenoma (n = 11), Cushing's adenoma (n = 6), and Cushing's disease (n = 3). The latter patients were compared with a third group of 8 patients with pheochromocytoma undergoing conventional transabdominal adrenalectomy (CTA). With both procedures, intraoperative changes in plasma catecholamine levels were studied during pheochromocytoma removal and the changes correlated with intraoperative cardiovascular derangements. LpA was successfully performed in 95% of patients with adrenal lesions and in 100% of patients with pheochromocytoma. There was no significant difference in laparoscopic adrenalectomy for pheochromocytoma compared to that for other adrenal lesions in terms of operative time, blood loss, hospital stay, analgesic requirements, and return to normal activity. The outcome was less favorable in pheochromocytoma patients undergoing CTA. The largest increase of catecholamine levels in pheochromocytoma patients occurred during tumor manipulation with both LpA (17.4-fold for epinephrine and 8.6-fold for norepinephrine) and CTA (34.2-fold for epinephrine and 13.7-fold for norepinephrine), but cardiovascular instability was associated only with CTA. LpA may become the technique of choice for surgical removal of adrenal lesions and may also become the preferred method for removing pheochromocytoma.
 ...
PMID:Laparoscopic approach to pheochromocytoma: hemodynamic changes and catecholamine secretion. 867 48

The Clp family consists of large, ubiquitous proteins that function as molecular chaperones and/or regulators of ATP-dependent proteolysis. A single copy gene coding for one of these proteins, ClpC, was cloned from the unicellular cyanobacterium Synechococcus sp. PCC 7942. The predicted polypeptide is most similar (ca. 88%) to the chloroplast-localized ClpC protein from higher plants. Using degenerate PCR primers specific for the two distinct ATP-binding domains characteristic of all ClpA-C proteins, partial sequences homologous to clpC from Synechococcus were also identified in five other cyanobacterial strains. The Synechococcus clpC gene is transcribed under standard growth conditions as a monocistronic message of around 2.7 kb. The level of this message, however, decreases slightly after a shift from 37 to 47.5 degrees C for 2 h, similar to expression previously observed for clpC mRNA from heat-shocked higher plants. At the protein level, the amount of ClpC remains relatively unchanged during the high temperature shift, while that of the known heat shock protein GroEL rises considerably. In contrast, the constitutive level of ClpC in Synechococcus increases considerably under conditions of rapid growth, both with increasing light intensities or CO2 concentrations. This, and the fact that attempts to inactivate clpC expression fail to produce a viable phenotype, suggest that ClpC activity is essential for growth in this obligate photoautotrophic cyanobacterium.
 ...
PMID:The cyanobacterium Synechococcus sp. PCC 7942 possesses a close homologue to the chloroplast ClpC protein of higher plants. 880 3

The authors utilized inhalation of 35% carbon dioxide and 65% oxygen as a diagnostic tool in the evaluation of suspected panic disorder. In two inpatients admitted for a medical evaluation for pheochromocytoma and carcinoid syndrome, respectively, a positive response to the double-blind administration of CO2/O2 or room air was consistent with a diagnosis of panic disorder by psychiatric history. In two additional patients in whom denial of mental illness was a psychological impediment to proper treatment, a positive CO2/O2 challenge resulted in therapeutic benefit.
 ...
PMID:The practical use of carbon dioxide-induced anxiety in the diagnosis and care of patients with panic disorder. 898 14

A gene (designated ecaA) encoding a vertebrate-like (alpha-type) carbonic anhydrase (CA) has been isolated from two disparate cyanobacteria, Anabaena sp. strain PCC 7120 and Synechococcus sp. strain PCC 7942. The deduced amino acid sequences correspond to proteins of 29 and 26 kDa, respectively, and revealed significant sequence similarity to human CAI and CAII, as well as Chlamydomonas CAHI, including conservation of most active-site residues identified in the animal enzymes. Structural similarities between the animal and cyanobacterial enzymes extend to the levels of antigenicity, as the Anabaena protein cross-reacts with antisera derived against chicken CAII. Expression of the cyanobacterial ecaA is regulated by CO2 concentration and is highest in cells grown at elevated levels of CO2. Immunogold localization using an antibody derived against the ecaA protein indicated an extracellular location. Preliminary analysis of Synechococcus mutants in which ecaA has been inactivated by insertion of a drug resistance cassette suggests that extracellular carbonic anhydrase plays a role in inorganic-carbon accumulation by maintaining equilibrium levels of CO2 and HCO3- in the periplasm.
 ...
PMID:Identification and characterization of a gene encoding a vertebrate-type carbonic anhydrase in cyanobacteria. 900 32

The large subunit core of ribulose-bisphosphate carboxylase from Synechococcus PCC 6301 expressed in Escherichia coli in the absence of its small subunits retains a trace of carboxylase activity (about 1% of the kcat of the holoenzyme) (Andrews, T. J (1988) J. Biol. Chem. 263, 12213-12219). During steady-state catalysis at substrate saturation, this residual activity diverted approximately 10% of the reaction flux to 1-deoxy-D-glycero-2,3-pentodiulose-5-phosphate as a result of beta elimination of inorganic phosphate from the first reaction intermediate, the 2,3-enediol form of ribulose bisphosphate. This indicates that the active site's ability to stabilize and/or retain this intermediate is compromised by the absence of small subunits. Epimerization and isomerization of the substrate resulting from misprotonation of the enediol intermediate were not significantly exacerbated by lack of small subunits. The residual carboxylating activity partitioned product between pyruvate and 3-phosphoglycerate in a ratio similar to that of the holoenzyme, indicating that stablization of the penultimate three-carbon aci-acid intermediate is not perturbed by lack of small subunits. The underlying instability of the five-carbon enediol intermediate was revealed, even with the holoenzyme, under conditions designed to lead to exhaustion of substrate CO2 (and O2). When carboxylation (and oxygenation) stalled upon exhaustion of gaseous substrate, both spinach and Synechococcus holoenzymes continued slowly to beta eliminate inorganic phosphate from and to misprotonate the enediol intermediate. With carboxylation and oxygenation blocked, the products of these side reactions of the enediol intermediate accumulated to readily detectable levels, illustrating the difficulties attendant upon ribulose-P2 carboxylase's use of this reactive species as a catalytic intermediate.
 ...
PMID:Side reactions catalyzed by ribulose-bisphosphate carboxylase in the presence and absence of small subunits. 903 45

Changes in photosystem stoichiometry in response to shift of environments for cell growth other than light regime were studied with the cyanophyte Synechocystis PCC 6714 in relation to the change induced by light-quality shift. Following two environment-shifts were examined: the shift of molecular form of inorganic carbon source for photosynthesis from CO2 to HCO3- (CO2 stress) and the increase in salinity of the medium with NaCl (0.5 M) (Na+ stress). Both CO2 and Na+ stresses induced the increase in PSI abundance resulting in a higher PSI/PSII stoichiometry. CO2 stress was found to elevate simultaneously Cyt c oxidase activity (Vmax). The feature was the same as that caused by light-quality shift from preferential excitation of PSI to PSII (light stress) though the enhancement by either stress was smaller than that by light stress. Under our experimental conditions, PSI/PSII stoichiometry appeared to increase at a fairly constant rate to the basal level even when the basal level had been differently determined by the light-quality. Enhancing rates for PSI/PSII stoichiometry and for Cyt c oxidase activity were also similar to each other. Since the two stresses affect the thylakoid electron transport similarly to the shift of light-quality, we interpreted our results as follows: three environmental stresses, CO2, Na+, and light stresses, cause changes in electron turnover capacity of PSI and Cyt c oxidase under a similar, probably a common, mechanism for monitoring redox state of thylakoid electron transport system.
 ...
PMID:Changes in photosystem stoichiometry in response to environmental conditions for cell growth observed with the cyanophyte Synechocystis PCC 6714. 917 26

Cyanobacterial genomes harbour two separate highly divergent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) genes, gap1 and gap2, which are closely related at the sequence level to the nuclear genes encoding cytosolic and chloroplast GAPDH of higher plants, respectively. Genes gap1 and gap2 of the unicellular cyanobacterium Synechocystis sp. PCC 6803 were cloned and sequenced and subsequently inactivated by insertional mutagenesis to understand their metabolic functions. We obtained homozygous gap1- mutants which have lost the capacity to grow on glucose under dim light while growth on organic acids as well as photosynthetic growth under CO2 and high light is not impaired. Homozygous gap2- mutants show the reciprocal phenotype. Under dim light they only grow on glucose but not on organic acids nor do they survive under photosynthetic conditions. Measurements of the anabolic activities (reduction of 1,3-bisphosphoglycerate) in extracts from wild type and mutant cells show that Gap2 is a major enzyme with dual cosubstrate specificity for NAD and NADP, while Gap1 displays a minor NAD-specific GAPDH activity. However, if measured in the catabolic direction (oxidation of glyceraldehyde-3-phosphate) Gap2 activity is very low and increases three- to fivefold after gel filtration of extracts over Sephadex G25. Our results suggest that enzymes Gap1 and Gap2, although coexpressed in cyanobacterial wild-type cells, play distinct key roles in catabolic and anabolic carbon flow, respectively. While Gap2 operates in the photosynthetic Calvin cycle and in non-photosynthetic gluconeogenesis, Gap1 seems to be essential only for glycolytic glucose breakdown, conditions under which the catabolic activity of Gap2 seems to be repressed by a specific low-molecular-weight inhibitor.
 ...
PMID:Genetic and biochemical evidence for distinct key functions of two highly divergent GAPDH genes in catabolic and anabolic carbon flow of the cyanobacterium Synechocystis sp. PCC 6803. 948 73

An inactivation library was used to isolate high-CO2-requiring mutants of Synechococcus PCC 7942. One of them, mutant IL-7, is composed of elongated cells, some 5-15 times longer than the wild-type. IL-7 is impaired in the ability to accumulate inorganic carbon within the cells due to a lesion in HCO3- transport. Consequently, the apparent photosynthetic affinity for external inorganic carbon was about 50-100-fold lower than in the wild-type. Analysis of the genomic region modified in IL-7 demonstrated that the inactivating fragment was composed of two genomically unrelated fragments which were ligated together during the formation of the inactivation library. One of the fragments originated from a known genomic region, rbcLS, encoding ribulose 1,5-bisphosphate carboxylase/oxygenase and the other showed high homology to mutS encoding a DNA mismatch repair protein. We suggest that the primary lesion in IL-7 was in mutS and not in rbcLS, and that the phenotype of IL-7 resulted from secondary random mutations. We were unable to identify the spontaneous mutation(s) due to low transformability of IL-7. Our finding that two unrelated fragments ligated together points to possible mistakes in the identification of the function of putative genes with the aid of an inactivation library.
 ...
PMID:A mutant of Synechococcus PCC 7942 impaired in HCO3- uptake. 950 27


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>