UNIPROT:Q86TM3 - FACTA Search

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Query: UNIPROT:Q86TM3 (cage)
29,987 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Recoverin is a member of the EF-hand family of calcium-binding proteins involved in the transduction of light by vertebrate photoreceptors. Recoverin also was identified as an autoantigen in the degenerative disease of the retina known as cancer-associated retinopathy (CAR), a paraneoplastic syndrome whereby immunological events lead to the degeneration of photoreceptors in some individuals with cancer. In this study, we demonstrate that recoverin is expressed in the lung tumor of a CAR patient but not in similar tumors obtained from individuals without the associated retinopathy. Recoverin was identified intially by Western blot analysis of the CAR patient's biopsy tissue by using anti-recoverin antibodies generated against different regions of the recoverin molecule. In addition, cultured cells from the biopsy tissue expressed recoverin, as demonstrated by reverse transcription-PCR using RNA extracted from the cells. The immunodominant region of recoverin also was determined in this study by a solid-phase immunoassay employing overlapping heptapeptides encompassing the entire recoverin sequence. Two linear stretches of amino acids (residues 64-70, Lys-Ala-Tyr-Ala-Gln-His-Val; and 48-52, Gln-Phe-Gln-Ser-Ile) made up the major determinants. One of the same regions of the recoverin molecule (residues 64-70) also was uniquely immunopathogenic, causing photoreceptor degeneration upon immunization of Lewis rats with the corresponding peptide. These data demonstrate that the neural antigen recoverin more than likely is responsible for the immunological events associated with vision loss in some patients with cancer. These data also establish CAR as one of the few autoimmune-mediated diseases for which the specific self-antigen is known.
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PMID:Recoverin, a photoreceptor-specific calcium-binding protein, is expressed by the tumor of a patient with cancer-associated retinopathy. 756 96

Phospholipase A2 [EC 3.1.1.4] treatment of pig kidney Na+,K(+)-ATPase [EC 3.6.1.3] labeled with fluorescence probes at the alpha-chain reduced the extent of the fluorescence intensity change of an N-[p-(2-benzimidazolyl)phenyl]maleimide (BIPM) probe at Cys-964 to below one-third of the control level accompanying the accumulation of phosphoenzymes. However, it only induced a slight decrease in that of a fluorescence isothiocyanate (FITC) probe at Lys-501 with a large decrease in the rate of change. The addition of phosphatidylserine (PS) or phosphatidylinositol (PI) to the phospholipase-treated BIPM-FITC-labeled enzyme increased the rate of the FITC fluorescence change. Phospholipase treatment of the BIPM-enzyme greatly reduced the Na+,K(+)-ATPase activity. The addition of PS or PI to the treated enzyme induced reactivation. These data and others suggest that Cys-964 and Glu-953 (Rb+ protectable dicyclohexyl carbodiimide binding site) are located in the vicinity of the surface area of the enzyme where hydrocarbon chains of phospholipids are present, and conserved H-bonding amino acids, Thr-955 and Ser-962, are located rather near the center of a domain forming a cation binding route or cage with other hydrophobic transmembrane segments. These data may indicate that the interaction between the BIPM probe and the hydrocarbon chains of phospholipids changes in such a way as to sense the change in the binding state of various ligands accompanying the sequential appearance of reaction intermediates of the enzyme.
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PMID:Different susceptibility to phospholipase A2 treatment of the fluorescence intensity changes in the vicinity of Cys-964 and Lys-501 in the alpha-chain of probe-labeled Na+,K(+)-ATPase. 805 57

B72.3 monoclonal antibody has been successfully boronated using mercaptoundecahydro-closo-dodecaborate (boron cage compound). The reagent was incorporated by first reacting the lysine residues of the antibody with m-maleimidobenzoyl succinimide ester (MBS), followed by Michael addition to the maleimido group by the mercapto boron cage compound to form a physiologically stable thioether linkage. Boron content of the antibody was determined by atomic absorption spectroscopy. For biodistribution studies, boronated antibody was radioiodinated with idogen. 125I-labeled and boronated B72.3 monoclonal antibody demonstrated clear tumor localization when administered via tail vein injections to athymic nude mice bearing LS174-T tumor xenografts. Boronated antibody was calculated to deliver 10(6) boron atoms per tumor cell. Although this falls short of the specific boron content originally proposed as necessary for boron neutron capture therapy (BNCT), recent calculations suggest that far fewer atoms of 10B per tumor cell would be necessary to effect successful BNCT when the boron is targeted to the tumor cell membrane.
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PMID:A technique to prepare boronated B72.3 monoclonal antibody for boron neutron capture therapy. 846 73

The dynamics of proton binding to the extracellular and the cytoplasmic surfaces of the purple membrane were measured by laser-induced proton pulses. Purple membranes, selectively labeled by fluorescein at Lys-129 of bacteriorhodopsin, were pulsed by protons released in the aqueous bulk from excited pyranine (8-hydroxy-1,3,6-pyrenetrisulfonate) and the reaction of protons with the indicators was measured. Kinetic analysis of the data imply that the two faces of the membrane differ in their buffer capacities and in their rates of interaction with bulk protons. The extracellular surface of the purple membrane contains one anionic proton binding site per protein molecule with pK = 5.1. This site is within a Coulomb cage radius (approximately 15 A) from Lys-129. The cytoplasmic surface of the purple membrane bears 4-5 protonable moieties (pK = 5.1) that, due to close proximity, function as a common proton binding site. The reaction of the proton with this cluster is at a very fast rate (3.10(10) M-1.s-1). The proximity between the elements is sufficiently high that even in 100 mM NaCl they still function as a cluster. Extraction of the chromophore retinal from the protein has a marked effect on the carboxylates of the cytoplasmic surface, and two to three of them assume positions that almost bar their reaction with bulk protons. The protonation dynamics determined at the surface of the purple membrane is of relevance both for the vectorial proton transport mechanism of bacteriorhodopsin and for energy coupling, not only in halobacteria, but also in complex chemiosmotic systems such as mitochondrial and thylakoid membranes.
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PMID:Protonation dynamics of the extracellular and cytoplasmic surface of bacteriorhodopsin in the purple membrane. 885 51

In the accompanying paper (Chung, J.-K., Sekiya, F., Kang, H.-S., Lee, C., Han, J.-S., Kim, S. R., Bae, Y. S., Morris, A. J., and Rhee, S. G. (1997) J. Biol. Chem. 272, 15980-15985), synaptojanin is identified as a protein that inhibits phospholipase D (PLD) activity stimulated by ADP-ribosylation factor and phosphatidylinositol 4, 5-bisphosphate (PI(4,5)P2). Here, the purification from rat brain cytosol of another PLD-inhibitory protein that is immunologically distinct from synaptojanin is described, and this protein is identified as clathrin assembly protein 3 (AP3) by peptide sequencing and immunoblot analysis. AP3 binds both inositol hexakisphosphate and preassembled clathrin cages with high affinity. However, neither inositol hexakisphosphate binding nor clathrin cage binding affected the ability of AP3 to inhibit PLD. AP3 also binds to PI(4,5)P2 with low affinity. But the PI(4,5)P2 binding was not responsible for PLD inhibition, because the potency and efficacy of AP3 as an inhibitor of PLD were similar in the absence and presence of PI(4,5)P2. A bacterially expressed fusion protein, glutathione S-transferase-AP3 (GST-AP3), also inhibited PLD with a potency equal to that of brain AP3. The inhibitory effect of AP3 appeared to be the result of direct interaction between AP3 and PLD because PLD bound GST-AP3 in an in vitro binding assay. Using GST fusion proteins containing various AP3 sequences, we found that the sequence extending from residues Pro-290 to Lys-320 of AP3 is critical for both inhibition of and binding to PLD. The fact that AP3 is a synapse-specific protein indicates that the AP3-dependent inhibition of PLD might play a regulatory role that is restricted to the rapid cycling of synaptic vesicles.
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PMID:Inhibition of phospholipase D by clathrin assembly protein 3 (AP3). 918 1

Three experiments were conducted with cage-reared broilers to 21 d following nutrient restriction from 6 to 12 d age. In Experiment 1, birds were full-fed from 6 to 11 or given 50% of ad libitum intake on a daily basis, or 100% of ad libitum intake on a daily basis when the diet was diluted 50% with oat hulls. Birds were not able to fully recover body weight depression by 21 d, although birds previously restricted, by whatever method, were more efficient (P < 0.01) in overall energy intake:body weight gain. Prior feed restriction had no effect on ability to metabolize diet energy (P > 0.05), although these birds did exhibit increased nitrogen retention compared to birds full-fed from 6 to 11 d. In a second experiment, birds were fed diets with 1.25, 1.38, 1.51, 1.63, 1.76, or 1.88% lysine in the realimentation diet from 12 to 21 d. Lysine level had no effect on growth rate or feed efficiency (P > 0.05) for full-fed birds; however there was a linear (P < 0.05) decline in growth rate from 12 to 21 d in response to extra dietary lysine for the birds previously feed restricted from 6 to 12 d. In a third experiment, birds were fed diets varying in energy (3,000 to 3,300 kcal/kg) or protein (22 to 29% CP) from 12 to 21 d following ad libitum vs 50% feed restriction from 6 to 11 d age. Protein level of the diet had little effect on performance traits to 21 d, although there was an indication of improved growth in response to the higher energy concentration. Birds full-fed from 6 to 11 d showed increased liver size at 21 d when fed more protein, although the converse was true for the restricted birds (P < 0.05). The growth response to diet energy was associated with increased carcass fatness. In general, there does not seem to be any advantage to manipulating diet formulation during realimentation of birds previously nutrient-restricted.
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PMID:Nutrition of the broiler chicken around the period of compensatory growth. 920 Feb 35

To further understand the six-electron reductions of sulfite and nitrite catalyzed by the Escherichia coli sulfite reductase hemoprotein (SiRHP), we have determined crystallographic structures of the enzyme in complex with the inhibitors phosphate, carbon monoxide, and cyanide, the substrates sulfite and nitrite, the intermediate nitric oxide, the product sulfide (or, most likely, an oxidized derivative thereof), and an oxidized nitrogen species (probably nitrate). A hydrogen-bonded cage of ligand-binding arginine and lysine side chains, ordered water molecules, and siroheme carboxylates provides preferred locations for recognizing the common functional groups of these ligands and accommodates their varied sizes, shapes, and charged without requiring substantial structural changes. The coordination geometries presented here suggest that the successively deoxygenated sulfur and nitrogen species produced during catalysis need not alter their orientation in the active site to adopt new stable coordination states. Strong pi-acid ligands decrease the bond length between the siroheme and the proximal cysteine thiolate shared with the iron-sulfur cluster, emphasizing the ability of the coupled cofactors to promote electron tranfer into substrate. On binding the siroheme, the substrate sulfite provides an oxygen atom in a unique location of the binding site compared to all other ligands studied, induces a spin transition in the siroheme iron, flips an active-site arginine, and orders surrounding active-center loops. The loop that coalesces over the active center shields the positively charged ligand-coordinating residues from solvent, enhancing their ability to polarize the substrate. Hydrogen bonds supplied by active-site arginine and lysine residues facilitate charge transfer into the substrate from the electron-rich cofactors, activate S-O bonds for reductive cleavage, and provide potential proton sources for the formation of favorable aquo leaving groups on the substrate. Strong interactions between sulfite and ordered water molecules also implicate solvent as a source of protons for generating product water. From the structures reported here, we propose a series of key structural states of ligated SiRHP in the catalytic reduction of sulfite to sulfide.
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PMID:Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products. 931 49

Palm kernel meal (PKM), a by-product from the African Palm oil industry that is extensively cultivated in tropical countries, is an interesting feed ingredient for poultry due to its availability and low cost. The objective of this study was to evaluate the use of different levels of PKM in layer diets. This particular PKM contained 9.70% crude protein, 0.20% methionine, 0.36% lysine, and a TMEn value of 2,254 kcal/kg. A control diet based on corn and soybean meal and five different levels of PKM added to it were fed to Single Comb White Leghorn hens from 18 to 38 wk of age. The PKM levels were 0, 10, 20, 30, 40, and 50%. The hens were housed three per cage (30.5 cm wide x 45.7 cm deep). The six treatments were assigned randomly to three contiguous cages in each of eight rows in a randomized complete block design. Egg production was recorded daily, and feed consumption for an entire week was recorded every 21 d. Egg weight and specific gravity were recorded for 3 consecutive d every 21 d. Mortality was recorded daily. Results show that egg production was significantly decreased (P < 0.05) only with 50% PKM in the diet. Feed conversion was not affected by any level of PKM. Specific gravity was slightly but significantly (P < 0.05) decreased by all levels of added PKM. Feed consumption, mortality, and egg weight did not differ significantly among the treatments. We concluded that this particular PKM may be used up to 40% in the diet, taking into account that specific gravity may be slightly decreased.
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PMID:Research notes: The effect of different levels of palm kernel meal in layer diets. 1068 92

The product of the cyanobacterium Synechocystis sp. PCC 6803 gene slr2097 is a 123 amino acid polypeptide chain belonging to the truncated hemoglobin family. Recombinant, ferric heme-reconstituted Synechocystis sp. PCC 6803 hemoglobin is a low-spin complex whose endogenous hexacoordination gives rise to optical and NMR characteristics reminiscent of cytochrome b(5) [Scott, N. L., and Lecomte, J. T. J. (2000) Protein Sci. 9, 587-597]. In this work, the sequential assignments using (15)N-(13)C-labeled protein, (1)H nuclear Overhauser effects, and longitudinal relaxation data identified His70 as the proximal histidine and His46 as the sixth ligand to the iron ion. It was also found that one of two possible heme orientations within the protein matrix is highly preferred (>90%) and that this orientation is the same as in vertebrate myoglobins. The rate constant for the 180 degrees rotation of the heme within a protein cage to produce the favored isomer was 0.5 h(-1) at 25 degrees C, approximately 35 times faster than in sperm whale myoglobin. Variable temperature studies revealed an activation energy of 132 +/- 4 kJ mol(-1), similar to the value in metaquomyoglobin at the same pH. The rate constant for heme loss from the major isomer was estimated to be 0.01 h(-1) by optical spectroscopy, close to the value for myoglobin and decades slower than in the related Nostoc commune cyanoglobin. The slow heme loss was attributed in part to the additional coordination bond to His46, whereas the relatively fast rate of heme reorientation suggested that this bond was weaker than the proximal His70-Fe bond. The standard reduction potential of the hexacoordinated protein was measured with and without poly-L-lysine as a mediator and found to be approximately -150 mV vs SHE, indicating a stabilization of the ferric state compared to most hemoglobins and b(5) cytochromes.
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PMID:Binding of ferric heme by the recombinant globin from the cyanobacterium Synechocystis sp. PCC 6803. 1137 Dec 18

Dekalb Delta hens were randomly assigned to one of eight dietary treatment groups. Two intakes of lysine (860 and 959 mg/hen per day) and 4 intakes of TSAA (635, 689, 811, 877 mg/hen per day) were combined in a 2 x 4 factorial treatment arrangement and fed from 20 to 43 wks of age. A phase feeding regimen was implemented at 43 wk with lysine intake lowered to 715 or 816 mg/hen per day and TSAA to 578, 607, 699, or 779 mg/hen per day. Cage was the experimental unit (5 hens/cage), and dietary treatments were replicated 8 times. Egg production (EP) and feed consumption were not affected by dietary treatments. Feed efficiency improved linearly by increasing TSAA intake during phase I only. Hen weight gain was improved (P < or = 0.03) by increased dietary lysine (94.2 vs. 135.2 g weight gain/hen). During phase I, hen weight gain was affected quadratically (P < or = 0.02) by TSAA. Increasing TSAA intake up to 689 mg/hen per day increased hen weight gain, but gain decreased at the highest intake. Egg weights (EW) increased (P < or = 0.02) from 59.02 to 60.21 g with increased lysine intake. Increasing lysine intake increased wet and dry albumen percentage, whereas dry yolk percentage decreased with increasing lysine. Total sulfur amino acid intake affected wet yolk, dry yolk, and solids in a quadratic trend, with hens fed 811 and 699 mg/d producing eggs with the greatest yolk solids. Wet and dry shell percentages were not affected by lysine or TSAA, and specific gravity decreased linearly during phase II and overall, with increased dietary TSAA. In conclusion, the dietary lysine at 959 and 816 mg/hen per day for phases I and II, respectively, optimized EW and feed efficiency. Because EP was not affected by dietary lysine, the dietary level for optimizing EP is closer to 860 and 715 mg/hen per day for phases I and II, respectively. Dietary TSAA level for maximum EP and feed efficiency was near 811 and 699 mg/hen per day but for EW may be closer to 877 and 779 mg/hen per day for phases I and II, respectively.
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PMID:The combined effects of dietary lysine and total sulfur amino acid level on egg production parameters and egg components in Dekalb Delta laying hens. 1520 25

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