Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q86TM3 (cage)
 29,987 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An increased risk of cancer associated with nickel refining and with chromate production has been known for some decades. The occupational exposure pattern of both nickel and chromium is very complex. Even though nickel carbonyl is an experimental carcinogen, there are no data supporting its carcinogenicity in humans. Nickel subsulfide may be the most potent carcinogen among the different nickel compounds. A correlation between lung cancer and exposure to chromates has been shown in several studies. As yet, there are no epidemiologic data indicating carcinogenicity of chromium(III) salts. Hexavalent chromium, however, has been suggested as the causative carcinogen among platers and ferrochromium workers. There is an urgent need for careful dose registration before a quantitative cancer risk analysis can be performed for the nickel and chromium industry.
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PMID:Cancer hazards caused by nickel and chromium exposure. 746 13

The role of 5-HT1, 5-HT2 and 5-HT3 receptors in the genesis of colonic motor alterations induced by emotional stress was evaluated in rats equipped with implanted nickel/chrome electrodes on the proximal colon and a catheter into the lateral ventricle of the brain. In control rats the frequency of colonic spike bursts increased from 7.6 +/- 1.3 to 16.8 +/- 1.3 per 10 min when the rats were placed in a test cage in which they had previously received electric footshocks. I.p. injection of methysergide (0.1 mg/kg) reduced by 54% the emotional stress-induced increase of colonic spike burst frequency, while a higher dosage (1 mg/kg) of methysergide had no effect. The i.p. injection of ketanserin (a 5-HT2 receptor antagonist, 0.1 and 1 mg/kg) or granisetron (a 5-HT3 receptor antagonist, 0.1 and 1 mg/kg) had no effect on emotional stress-induced colonic hyperkinesia. The i.p. injection of the 5-HT1A receptor agonists, buspirone (1 mg/kg) or 8-OH-DPAT (8-hydroxy-2-(di-n-propylamino(tetralin) (0.05 and 0.1 mg/kg) or benzodiazepine (clonazepam, 1 mg/kg) significantly reduced or suppressed the emotional stress-induced increase of colonic spike bursts. Injected i.c.v., buspirone, but not 8-OH-DPAT, also reduced the emotional stress-induced hyperkinesia. Pretreatment with devazepide receptor (1 microgram/kg) antagonized the inhibitory effects of buspirone and 8-OH-DPAT injected i.p. on emotional stress-induced colonic hyperkinesia but did not alter the effects of clonazepam (1 mg/kg).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Comparative involvement of 5-HT1, 5-HT2 and 5-HT3 receptors in stress-induced colonic motor alterations in rats. 838 21

We have developed a system for analysis of histidine-tagged (His-tagged) retrovirus core (Gag) proteins, assembled in vitro on lipid monolayers consisting of egg phosphatidylcholine (PC) plus the novel lipid DHGN. DHGN was shown to chelate nickel by atomic absorption spectrometry, and DHGN-containing monolayers specifically bound gold conjugates of His-tagged proteins. Using PC + DHGN monolayers, we examined membrane-bound arrays of an N-terminal His-tagged Moloney murine leukemia virus (M-MuLV) capsid (CA) protein, His-MoCA, and in vivo studies suggest that in vitro-derived His-MoCA arrays reflect some of the Gag protein interactions which occur in assembling virus particles. The His-MoCA proteins formed extensive two-dimensional (2D) protein crystals, with reflections out to 9.5 A resolution. The image-analyzed 2D projection of His-MoCA arrays revealed a distinct cage-like network. The asymmetry of the individual building blocks of the network led to the formation of two types of hexamer rings, surrounding protein-free cage holes. These results predict that Gag hexamers constitute a retrovirus core substructure, and that cage hole sizes define an exclusion limit for entry of retrovirus envelope proteins, or other plasma membrane proteins, into virus particles. We believe that the 2D crystallization method will permit the detailed analysis of retroviral Gag proteins and other His-tagged proteins.
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PMID:Structural analysis of membrane-bound retrovirus capsid proteins. 913 37

To evaluate the effect of green nickel oxide (NiO) on the production of tumor necrosis factor (TNF) by alveolar macrophages, alveolar macrophages were exposed to NiO in vitro and in vivo. For the in vitro study, rats alveolar macrophages were incubated with NiO on a microplate for 24 h. TNF activity in the culture supernatant was determined by the L929 bioassay. Rats alveolar macrophages cultured with 100 and 200 micrograms/mL of NiO in vitro induced the production of TNF, however, it was not statistically significant compared with the control that was free from NiO exposure. For exposure in vivo, rats were divided into two groups. Five were exposed to a daily concentration of 11.7 +/- 2.0 mg/m3 of NiO for an 8-hr/d, 5 d/wk, for 4 wk, and five rats (control) were kept in a cage and not exposed to NiO. Bronchoalveolar lavage was performed and the recovered alveolar macrophages were incubated on a microplate for 24 h. TNF production by exposed alveolar macrophages was significantly higher than that of controls.
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PMID:Effects of nickel oxide on the production of tumor necrosis factor by alveolar macrophages of rats. 939 48

In an in vitro system that mimics the assembly of immature human immunodeficiency virus (HIV) particles, ordered arrays of HIV-1 capsid (CA) proteins encoded by the viral gag gene have been obtained by incubation of histidine-tagged capsid proteins (His-HIVCA) beneath lipid monolayers containing the nickel-chelating lipid, 1,2-di-O-hexadecyl-sn-glycero-3-(1'-2"-R-hydroxy-3'-N-(5-amino-1- carboxypentyl)iminodiacetic acid)propyl ether. The membrane-bound His-HIVCA proteins formed small crystalline arrays of primitive (p1) unit cells with dimensions of a = 74.2 A, b = 126.2 A, gamma = 89.3 degrees. The image-analyzed two-dimensional projection of His-HIVCA assemblies shows a cage-like lattice, consisting of hexamer and trimer units, surrounding protein-free cage holes. The hexamer-coordinated cage holes of 26.3-A diameter are spaced at 74. 2-A intervals: these distances, and the hexamer-trimer arrangement, are consistent with previous, lower resolution studies on immature HIV-1 virus particles produced in vivo. Additionally, HIV-1 matrix protein trimer unit structures align to the His-HIVCA trimer units such that residues previously shown to interact with the HIV-1 gp120/gp41 envelope protein complex are oriented toward the hexamer cage holes. Our results form a bridge between results from conventional methods for the analysis of HIV particle structure.
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PMID:Organization of HIV-1 capsid proteins on a lipid monolayer. 951 5

We have used an in vitro system that mimics the assembly of immature Moloney murine leukemia virus (M-MuLV) particles to examine how viral structural (Gag) proteins oligomerize at membrane interfaces. Ordered arrays of histidine-tagged Moloney capsid protein (his-MoCA) were obtained on membrane bilayers composed of phosphatidylcholine (PC) and the nickel-chelating lipid 1, 2-di-O-hexadecyl-sn-glycero-3-(1'-2"-R-hydroxy-3'N-(5-amino-1-carboxy pentyl)iminodiacetic acid)propyl ether (DHGN). The membrane-bound arrays were analyzed by electron microscopy (EM) and atomic force microscopy (AFM). Two-dimensional projection images obtained by EM showed that bilayer-bound his-MoCA proteins formed cages surrounding different types of protein-free cage holes with similar cage holes spaced at 81.5-A distances and distances between dissimilar cage holes of 45.5 A. AFM images, showing topological features viewed near the membrane-proximal domain of the his-MoCA protein, revealed a cage network of only symmetrical hexamers spaced at 79-A distances. These results are consistent with a model in which dimers constitute structural building blocks and where membrane-proximal and distal his-MoCA regions interact with different partners in membrane-bound arrays.
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PMID:Atomic force microscopy and electron microscopy analysis of retrovirus Gag proteins assembled in vitro on lipid bilayers. 1062 Mar 1

The synthesis and structural characterisation of a series of cobalt and nickel cages are reported. Eight of these structures contain a [M10(mu3-OH)6(eta2, mu3-xhp),(eta2, mu2-O2CR)6]2+ core (where M = Co or Ni; xhp = 6-chloro- or 6-methyl-2-pyridonate: R = Me, Ph, CHMe2, CH2Cl, CHPh2 or CMe3), where the ten metal atoms describe a centred-tricapped-trigonal prism (ttp). The cage contains six hydroxide ligands around the central metal, and the exterior is coated with pyridonate and carboxylate ligands. For four of the cages additional metal centres are found attached to the upper and/or lower triangular faces of the trigonal prism, generating dodeca- and undecanuclear cages. Three further cages are reported that contain a metal core based on an incomplete centred-tetraicosahedron. These cages involve trimethylacetate as a ligand in company with either 6-methyl-2-pyridonate or 6-chloro-2-pyridonate. Comparison of these latter structures with the trigonal prisms reveal that they can be described as a pentacapped-trigonal prism missing one edge. Magnetic studies of three of the nickel cages with trigonal prismatic cores show spin ground states of S = 8, 4 and 2 for Ni12, Ni11 and Ni10 cages, respectively.
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PMID:A family of polynuclear cobalt and nickel complexes stabilised by 2-pyridonate and carboxylate ligands 1082 11

Retrovirus Gag precursor (PrGag) proteins direct the assembly of roughly spherical immature virus particles, while after proteolytic processing events, the Gag capsid (CA) and nucleocapsid (NC) domains condense on viral RNAs to form mature retrovirus core structures. To investigate the process of retroviral morphogenesis, we examined the properties of histidine-tagged (His-tagged) Moloney murine leukemia (M-MuLV) capsid plus nucleocapsid (CANC) (His-MoCANC) proteins in vitro. The His-MoCANC proteins bound RNA, possessed nucleic acid-annealing activities, and assembled into strand, circle (or sphere), and tube forms in the presence of RNA. Image analysis of electron micrographs revealed that tubes were formed by cage-like lattices of CANC proteins surrounding at least two different types of protein-free cage holes. By virtue of a His tag association with nickel-chelating lipids, His-MoCANC proteins also assembled into planar sheets on lipid monolayers, mimicking the membrane-associated immature PrGag protein forms. Membrane-bound His-MoCANC proteins organized into two-dimensional (2D) cage-like lattices that were closely related to the tube forms, and in the presence of both nickel-chelating lipids and RNAs, 2D lattice forms appeared similar to lattices assembled in the absence of RNA. Our observations are consistent with a M-MuLV morphogenesis model in which proteolytic processing of membrane-bound Gag proteins permits CA and NC domains to rearrange from an immature spherical structure to a condensed mature form while maintaining local protein-protein contacts.
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PMID:Assembly of retrovirus capsid-nucleocapsid proteins in the presence of membranes or RNA. 1090 96

A centered icosahedral 12-coordinate samarium cluster formed by six bis(L-prolinato)nickel(II) ([Ni(pro)2]) ligands, [Sm(Ni(pro)2)6]3+, was prepared. The reaction of Sm with [Ni(pro)2] in a small excess (a 2-fold excess) and also in a large excess (even a 10-fold excess) of the latter produced the cluster. Therefore, this system is a self-assembly. In the cluster, each nickel atom is surrounded by six atoms: two amino nitrogens, two carboxylate oxygens which form chelate rings with the nitrogen atoms, and two carboxylate oxygen atoms which link the neighboring nickel atoms. The samarium atom is coordinated by six [Ni(pro)2] ligands, and the metal is in an icosahedral environment formed by 12 oxygen atoms. The icosahedral geometry is almost ideal. Crystals of [Sm(Ni(pro)2)6](ClO4)3.6MeOH, which were prepared from a methanol solution, immediately decompose after filtration because of loosely trapped MeOH molecules in the crystal lattice. Therefore, crystals without MeOH molecules, which must be stable, were prepared by recrystallization from acetonitrile with tetramethylammonium perchlorate (TMAP). According to the X-ray crystal analysis, the cluster is TMA[Sm(Ni(pro)2)6](ClO4)4, cubic of space group F23, with a = 21.273(9) A, V = 9626(1) A3, and Z = 4; R = 0.053 (Rw = 0.049) for 1296 reflections. In addition, several crystals of cluster salts that have different counteranions, i.e., tetrafluoroborate (BF4-), hexafluorophosphate (PF6-), iodide (I-), and nitrate (NO3-), were prepared. The order of increasing ease of crystallization of the cluster salts was I- > PF6- approximately ClO4- > BF4- >> NO3-. The cluster structure is retained in alcohol and acetonitrile solutions; the UV-vis spectra of the solutions are perfectly consistent with the powder diffuse reflection spectrum. Cyclic voltammograms of [Sm(Ni(pro)2)6]3+ in acetonitrile proved that the structure of [Sm(Ni(pro)2)6]3+ is retained in the redox process and that the nickel atoms electrochemically interact with one another. Thermal analysis of the cluster salts with different counteranions was investigated. The results imply that the cluster is very stable until bis(L-prolinato)nickel(II) ligands, which form the cage structure, disintegrate and that the thermal decomposition processes of the cluster salts depend on their counteranions.
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PMID:Synthesis of stable crystals of a self-assembled centered icosahedral samarium cluster formed by bis(L-prolinato)nickel(II) ligands. 1119 3

A pyrazolate-based dinucleating ligand of the bis(alpha-diimine) type forms an unusual hexanucler nickel(II) cage complex incorporating an interstitial mu 6-Cl atom.
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PMID:An unusual hexanickel cage complex with mu- and mu 3-chloro bridges and an interstitial mu 6-chloride. 1224 99


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