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

Photosystem II, the photosynthetic water-oxidizing complex, can be isolated from both plants and cyanobacteria. A variety of methods have been developed for purification of this enzyme, which can be isolated in several functional and structural forms. Knowledge of the pigment content of photosystem II preparations is important for precise spectroscopic, biochemical, and functional analysis. We have determined pigment stoichiometries in oxygen-evolving photosystem II preparations from plants and cyanobacteria. We have employed a solvent system for the isocratic elution of a reverse phase HPLC column in which we have determined the extinction coefficients of the relevant pigments. Pigments were extracted from four photosystem II preparations. These preparations included spinach photosystem II membranes [Berthold, D. A., Babcock, G. T., & Yocum, C. F. (1981) FEBS Lett. 134, 231-234], spinach photosystem II reaction center complexes [Ghanotakis, D. F., & Yocum, C. F. (1986) FEBS Lett. 197, 244-248], spinach photosystem II complexes [MacDonald, G. M., & Barry, B. A. (1992) Biochemistry 31, 9848-9856], and photosystem II particles isolated from the cyanobacterium, Synechocystis sp. PCC 6803 [Noren, G. H., Boerner, R. J., & Barry, B. A. (1991) Biochemistry 30, 3943-3950]. Pigment stoichiometries were determined using two different methods of data analysis and were based on the assumption that there are two pheophytin a molecules per photosystem II reaction center. The pigment stoichiometries obtained were comparable for the two methods of data analysis and agreed with previous biophysical and biochemical characterizations of the preparations. The average pigment stoichiometries (chlorophyll:plastoquinone-9 per 2 pheophytin a) determined using the two data analysis methods were as follows: photosystem II membranes, 274:3.2; photosystem II reaction center complexes, 78:2.5; Synechocystis PS II particles, 55:2.4; photosystem II complexes, 121:2.0.
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PMID:Pigment quantitation and analysis by HPLC reverse phase chromatography: a characterization of antenna size in oxygen-evolving photosystem II preparations from cyanobacteria and plants. 867 81

A rat pheochromocytoma cell line (PC12) was encapsulated in a water-insoluble hydroxyethyl methacrylate-methyl methacrylate copolymer by interfacial precipitation from a polyethylene glycol 200 solution into phosphate-buffered saline. The resulting capsules (660 +/- 44 microns in diameter; 84 +/- 27 microns wall thickness) contained viable PC12 cells in a spheroidal arrangement, much like tumour spheroids, the latter grown on surfaces unsuitable for cell attachment. In these spheroids, the viable cells formed a band approximately 100 microns thick, surrounding an inner core of necrotic cells. A similar arrangement was seen 14, 28 and 42 days after encapsulation, with capsules maintained in an in vitro tissue culture environment; the annular ring was roughly constant in size, although the packing density appeared to increase over the 6 week observation period. During the first 4 weeks, when measurements were made the encapsulated cells converted a tetrazolium dye (MTT) into an insoluble formazan product, in a time-after-encapsulation-dependent manner. This indicated that PC12 cells retained viability despite encapsulation and an ability to increase (at least in part) their metabolic capacity, presumably by a combination of proliferation and altered cellular activity. The encapsulated PC12 cells also secreted dopamine when incubated in a high potassium release medium but not in a low potassium, conventional tissue culture medium (RPMI 1640). Consistent with the MTT results, the amount of dopamine released was also dependent on the time after encapsulation, as well as the cell density at the time of encapsulation.
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PMID:Dopamine secretion by PC12 cells microencapsulated in a hydroxyethyl methacrylate--methyl methacrylate copolymer. 874 23

The crystal structure of the ferredoxin:NADP+ reductase (FNR) from the cyanobacterium Anabaena PCC 7119 has been determined at 2.6 A resolution by multiple isomorphous replacement and refined using 15.0 A to 1.8 A data, collected at 4 degrees C, to an R-factor of 0.172. The model includes 303 residues, the flavin adenine dinucleotide cofactor (FAD), one sulfate ion located at the putative NADP+ binding site and 328 water molecule sites. The structure of Anabaena FNR, including FAD, a network of intrinsic water molecules and a large hydrophobic cavity in the C-terminal domain, resembles that of the spinach enzyme. The major differences concern the additional short alpha-helix (residues 172 to 177 in Anabaena FNR) and residues Arg 100 and Arg 233 which binds NADP+ instead of Lys 116 and Lys 244 in the spinach enzyme. Crystals of a complex of Anabaena FNR with NADP+ were obtained. The model of the complex has been refined using 15 A to 2.25 A X-ray data, collected at -170 degrees C, to an R-factor of 0.186. This model includes 295 residues, FAD, the full NADP+ (with an occupancy of 0.8) and 444 water molecules. The 2'-5' adenine moiety of NADP+ binds to the protein as 2'-phospho-5'-AMP to the spinach FNR. The nicotinamide moiety is turned towards the surface of the protein instead of stacking onto the FAD isoalloxazine ring as would be required for hydride transfer. The model of the complex agrees with previous biochemical studies as residues Arg 100 and Arg 233 are involved in NADP+ binding and residues Arg77, Lys 53 and Lys 294, located on the FAD side of the enzyme, remain free to interact with ferredoxin and flavodoxin, the physiological partners of ferredoxin: NADP reductase.
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PMID:X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8 A resolution, and crystallographic studies of NADP+ binding at 2.25 A resolution. 889 Sep 10

We have discovered a neuronal system that fires bursting exocytotic events. In the giant dopamine neuron of the fresh water snail Planorbis corneus, bursting exocytotic events are evoked following in situ stimulation with elevated potassium. Amperometric detection using carbon fiber microelectrodes, which provides high temporal resolution, has been used to record exocytotic events released from the neuron. Evaluation of the time interval between consecutive exocytotic events (inter-spike interval) recorded from about 80% of the neurons reveals the occurrence of distinct bursting patterns defined by transients having an equal interval among them. Statistical analysis of these bursting exocytotic events shows three distinct distributions of inter-spike intervals with mid points occurring at 5, 22 and 45 ms. This bursting release behavior is not observed from cultured pheochromocytoma cells although they show calcium-dependent exocytosis following in situ stimulation with elevated potassium. Our data appear to indicate that the Planorbis dopamine neuron in vivo is actively involved in specific modes of neural communication and may represent an important phenomenon in understanding single cell activities.
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PMID:Electrochemical monitoring of bursting exocytotic events from the giant dopamine neuron of Planorbis corneus. 889 Dec 56

A three-dimensional model of the photosystem II (PSII) reaction center from the cyanobacterium Synechocystis sp. PCC 6803 was generated based on homology with the anoxygenic purple bacterial photosynthetic reaction centers of Rhodobacter sphaeroides and Rhodopseudomonas viridis, for which the X-ray crystallographic structures are available. The model was constructed with an alignment of D1 and D2 sequences with the L and M subunits of the bacterial reaction center, respectively, and by using as a scaffold the structurally conserved regions (SCRs) from bacterial templates. The structurally variant regions were built using a novel sequence-specific approach of searching for the best-matched protein segments in the Protein Data Bank with the "basic local alignment search tool" (Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ, 1990, J Mol Biol 215:403-410), and imposing the matching conformational preference on the corresponding D1 and D2 regions. The structure thus obtained was refined by energy minimization. The modeled D1 and D2 proteins contain five transmembrane alpha-helices each, with cofactors (4 chlorophylls, 2 pheophytins, 2 plastoquinones, and a non-heme iron) essential for PSII primary photochemistry embedded in them. A beta-carotene, considered important for PSII photoprotection, was also included in the model. Four different possible conformations of the primary electron donor P680 chlorophylls were proposed, one based on the homology with the bacterial template and the other three on existing experimental suggestions in literature. The P680 conformation based on homology was preferred because it has the lowest energy. Redox active tyrosine residues important for P680+ reduction as well as residues important for PSII cofactor binding were analyzed. Residues involved in interprotein interactions in the model were also identified. Herbicide 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) was also modeled in the plastoquinone QB binding niche using the structural information available from a DCMU-binding bacterial reaction center. A bicarbonate anion, known to play a role in PSII, but not in anoxygenic photosynthetic bacteria, was modeled in the non-heme iron site, providing a bidentate ligand to the iron. By modifying the previous hypothesis of Blubaugh and Govindjee (1988, Photosyn Res 19:85-128), we modeled a second bicarbonate and a water molecule in the QB site and we proposed a hypothesis to explain the mechanism of QB protonation mediated by bicarbonate and water. The bicarbonate, stabilized by D1-R257, donates a proton to QB2- through the intermediate of D1-H252; and a water molecule donates another proton to QB2-. Based on the discovery of a "water transport channel" in the bacterial reaction center, an analogous channel for transporting water and bicarbonate is proposed in our PSII model. The putative channel appears to be primarily positively charged near QB and the non-heme iron, in contrast to the polarity distribution in the bacterial water transport channel. The constructed model has been found to be consistent with most existing data.
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PMID:Modeling of the D1/D2 proteins and cofactors of the photosystem II reaction center: implications for herbicide and bicarbonate binding. 889 6

Tyr161 of the D1 protein (Yz) is a redox component closely associated with the water-oxidizing complex of photosystem II. Yz reduces the primary donor P680+, and Yzox is then rereduced by the manganese cluster that oxidizes water. We aimed to investigate whether water oxidation by P680+ could occur through an alternative pathway in the absence of Tyr161. For this purpose, combinatorial mutagenesis was performed in residues presumed to be in the environment of Tyr161. Full sequence degeneracy was introduced in two regions of the D1 protein: at codons 157, 158, 160, 162, 163, 164, and 165, which are close to Yz by sequence, and at codons 186-191 which are assumed to be close to Yz in the tertiary structure; at position 161, the nucleotide combinations were designed to not give rise to a Tyr codon. The combinatorial DNA mixture was used to transform an obligate photoheterotrophic mutant (Y161W) of the cyanobacterium Synechocystis sp. PCC 6803, in which Trp at position 161 impairs photosynthetic activity. Transformants were selected in which photoautotrophic growth was restored, resulting in 11 viable mutants. In all of these mutants, however, a Tyr codon was found at position 161, introduced either by complex repair processes or as a result of PCR-induced mutations. Additional mutations found in residues neighboring Tyr161 mostly retained photosystem II properties similar to those of wild type. However, in two of these mutants, FVEYPI and FLVYNI, photoautotrophic growth was impaired and the relative variable fluorescence was reduced. Computer simulations of the environment of Yz suggest that the position of Tyr161 varies with respect to some neighboring residues without major functional consequences. We conclude that Tyr161 fulfills a critical role through its chemical nature and positioning and that this function cannot be substituted by another residue at a nearby position.
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PMID:Combinatorial mutagenesis and structural simulations in the environment of the redox-active tyrosine YZ of photosystem II. 898 78

The effects of ultraviolet-B radiation (280-320 nm) on photosystem II of Synechocystis sp. PCC 6303 were investigated at the functional and structural levels. Loss of oxygen-evolving and electron-transport activity, measured by various techniques including Clark electrode polarography, fluorescence induction and fluorescence relaxation after a single turnover flash, are discussed in terms of two types of damage caused by ultraviolet-B radiation: (a) depletion of the plastoquinone pool; (b) perturbation and degradation of the D1 protein, with cleavage in the second transmembrane segment. These findings are in full agreement with those obtained, both in vivo and in vitro for higher plants for which a donor-side mechanism involving the water-splitting Mn cluster has been proposed for the main cleavage of the D1 protein. At the structural level, complete disruption of the photosystem II core is documented as a consequence of (or in parallel with) degradation of the D1 protein. From this point of view, ultraviolet-B-induced photoinhibition is unlike the visible-induced type and less susceptible to repair by synthesis and reinsertion of new D1 protein.
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PMID:Effects of ultraviolet-B radiation on photosystem II of the cyanobacterium Synechocystis sp. PCC 6083. 902 12

The purpose of the study is to evaluate the ability of Gd-enhancement and fat-suppressed MR imaging operating at midfield strength to characterize incidentally discovered adrenal masses. Sixty patients with 72 adrenal masses incidentally discovered during US or CT exams were studied with a 0.51 MR unit following clinical and laboratory evaluation. After Gd-DTPA intravenous administration a modified three-point Dixon technique was performed in all patients. This technique provided three images sets: conventional T1-weighted SE images, fat-suppressed T1-weighted images and water-suppressed T1-weighted images. Diagnosis was established by means of surgery (11 lesions), fine-needle biopsy (21 lesions) and stability on ultrasonographic follow-up for at least 1 year (range, 12-87 months) from adrenal lesion discovery (40 masses). In most of adenomas (n = 55) an homogeneous enhancement was observed on postcontrast T1WI; however, 15 out of these lesions showed a small focal spot of high intensity in Gd-enhanced fat-suppressed images. On the contrary, malignant conditions (n = 6) and pheochromocytoma (n = 1), all had inhomogeneous signal intensities which were relatively higher after Gadolinium injection as compared with the liver. The fat suppression technique demonstrated areas of bright signal intensity related to high vascularity. The performance of three observers in order to differentiate malignant from benign conditions showed sensitivity, specificity, diagnostic accuracy, positive and negative predictive values of 100, 88.5, 90, 50 and 100% on the basis of gadolinium enhancement only, by utilizing the Dixon technique. In conclusion, although Gd-enhancement and fat-suppressed sequence helped correctly differentiate among the groups of incidentally discovered adrenal masses, the degree of overlap suggests that it is still difficult to characterize individual patients. However, the modified three-point Dixon technique after contrast material administration appears to be a further capability of midfield MRI in the characterization of adrenal tissue.
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PMID:Incidentally discovered adrenal masses: evaluation with gadolinium enhancement and fat-suppressed MR imaging at 0.5 T. 923 97

Photosystem II is a reaction center protein complex located in photosynthetic membranes of plants, algae, and cyanobacteria. Using light energy, photosystem II catalyzes the oxidation of water and the reduction of plastoquinone, resulting in the release of molecular oxygen. A key component of photosystem II is cytochrome b559, a membrane-embedded heme protein with an unknown function. The cytochrome is unusual in that a heme links two separate polypeptide subunits, alpha and beta, either as a heterodimer (alphabeta) or as two homodimers (alpha2 and beta2). To determine the structural organization of cytochrome b559 in the membrane, we used site-directed mutagenesis to fuse the coding regions of the two respective genes in the cyanobacterium Synechocystis sp. PCC 6803. In this construction, the C terminus of the alpha subunit (9 kDa) is attached to the N terminus of the beta subunit (5 kDa) to form a 14-kDa alphabeta fusion protein that is predicted to have two membrane-spanning alpha-helices with antiparallel orientations. Cells containing the alphabeta fusion protein grow photoautotrophically and assemble functional photosystem II complexes. Optical spectroscopy shows that the alphabeta fusion protein binds heme and is incorporated into photosystem II. These data support a structural model of cytochrome b559 in which one heme is coordinated to an alpha2 homodimer and a second heme is coordinated to a beta2 homodimer. In this model, each photosystem II complex contains two cytochrome b559 hemes, with the alpha2 heme located near the stromal side of the membrane and the beta2 heme located near the lumenal side.
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PMID:Structural model of cytochrome b559 in photosystem II based on a mutant with genetically fused subunits. 939 Nov 72

A water soluble protein with the carotenoid 3'-hydroxyequinenone bound to it has been purified from the cyanobacterium Synechocystis PCC 6803. Based on partial amino acid sequencing of the protein, oligonucleotides were synthesized and used as primers for PCR to obtain a substantial fragment of the gene. This DNA was sequenced and the sequence data and the size of the protein indicate that the protein is encoded by gene slr 1963 in the Kazusa DNA sequence data bank containing the Synechocystis 6803 genome. This protein is very similar to 3'-hydroxyechinenone proteins found in several other cyanobacteria but it shows very little resemblance in its amino acid or gene sequence to other carotenoid binding proteins. The protein binds 1-2 molecules of 3'-hydroxyechinenone and is slowly cleaved by proteases in the cell extract to give a molecule of approximately half the original mass which retains the carotenoid and which shows a striking change in color.
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PMID:The orange carotenoid protein of Synechocystis PCC 6803. 939 74


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