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Query: UNIPROT:P06889 (
Mol
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630,302
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The initial step in the uptake of
iron
via ferric pseudobactin by the plant-growth-promoting Pseudomonas putida strain WCS358 is binding to a specific outer-membrane protein. The nucleotide sequence of the pupA structural gene, which codes for a ferric pseudobactin receptor, was determined. It contains a single open reading frame which potentially encodes a polypeptide of 819 amino acids, including a putative N-terminal signal sequence of 47 amino acids. Significant homology, concentrated in four boxes, was found with the TonB-dependent receptor proteins of Escherichia coli. The pupA mutant MH100 showed a residual efficiency of 30% in the uptake of 55Fe3+ complexed to pseudobactin 358, whereas the
iron
uptake of four other pseudobactins was not reduced at all. Cells of strain WCS374 supplemented with the pupA gene of strain WCS358 could transport ferric pseudobactin 358 but showed no affinity for three other pseudobactins. It is concluded that PupA is a specific receptor for ferric pseudobactin 358, and that strain WCS358 produces at least one other receptor for other pseudobactins.
Mol
Microbiol 1991 Mar
PMID:The ferric-pseudobactin receptor PupA of Pseudomonas putida WCS358: homology to TonB-dependent Escherichia coli receptors and specificity of the protein. 164 76
In an effort to develop a biologic marker of exposure to nitrogen dioxide (NO2), we investigated the in vivo formation of a complex between heme proteins and nitric oxide (NO). In aqueous solution, NO2 disproportionates to NO and nitrate. The NO binds to the
iron
of heme proteins to form an electron spin resonance (ESR)-detectable complex. We have shown that when rat liver, lung, or nasal microsomes are exposed to 20 ppm NO2 in vitro, an ESR signal attributable to an NO/heme protein complex is detected. After inhalation exposure of rats to 20 ppm NO2 for 6 h, this same ESR signal was detected in microsomes prepared from the exposed rats' lungs or liver; microsomes prepared from the nasal tissue failed to yield any detectable signal. When we lavaged the lungs of rats exposed for 6 h to 0, 5, 10, 20, or 30 ppm NO2 and isolated the bronchoalveolar cell pellets, the NO/heme protein complex was detected in the cell pellets. We were able to demonstrate a dose-dependent relationship between the ESR signal intensity of the NO/heme protein complex and the NO2 exposure concentration. Finally, we used ESR to examine bronchoalveolar lavage cell pellets obtained from human volunteers exposed to either 1.5 or 4 ppm NO2, for 20 min every other day, for six exposures. No signal was found in any of the samples taken 3 wk prior to NO2 exposure, but an ESR signal attributable to the NO/heme protein complex was detected in every sample obtained after the 4 ppm NO2 exposure and in five of eight samples obtained after the 1.5 ppm NO2 exposure.(ABSTRACT TRUNCATED AT 250 WORDS)
Am J Respir Cell
Mol
Biol 1991 Jun
PMID:The nitric oxide/heme protein complex as a biologic marker of exposure to nitrogen dioxide in humans, rats, and in vitro models. 164 79
Mini-myoglobin, obtained by limited proteolysis of horse heart myoglobin (residues 32 to 139), represents a good model for testing the correlation between an exon and a protein domain. We have shown that ligand binding kinetics, spectral and folding features of mini-myoglobin are very similar to those of native myoglobin. In order to develop further the analysis of the structure-function relationship in this mini-protein, mini-globin was reconstituted with the heme moiety in which
iron
is replaced by cobalt. The Soret absorption spectra of oxy and deoxy cobaltous mini-myoglobin are very similar to those of cobaltous myoglobin derivatives; in addition. Co-mini-myoglobin binds oxygen reversibly with an n value approximately 1 and a p50 value of 45 to 50 mm Hg (the same as Co-myoglobin). Oxy Co-mini-myoglobin shows a well-resolved electron paramagnetic resonance (e.p.r.) spectrum typical of an oxygenated hemoprotein, while the spectrum of the deoxy derivative, although similar to that of deoxy Co-myoglobin, displays a lower resolution of the complex hyperfine structure. Moreover, photodissociation experiments on oxy Co-mini-myoglobin allow e.p.r. detection of an intermediate state, already observed in most hemoproteins and diagnostic for the interaction of bound oxygen with the distal histidine residue. Thus, reconstitution of mini-globin with cobalt protoprophyrin IX has provided, for the first time, a stable oxygenated complex that reflects a correct folding of the protein surrounding the heme pocket and possesses the functional behaviour typical of a hemoprotein.
J
Mol
Biol 1991 Dec 05
PMID:Mini-myoglobin. Electron paramagnetic resonance and reversible oxygenation of the cobalt derivative. 166 Sep 28
It is proposed that the energy-transducing system of the first cellular organism and its precursor was fueled by the oxidation of hydrogen sulfide and ferric sulfide to
iron
pyrites and two [H+] on the outside surface of a vesicle (the cell membrane), with the concomitant reduction of CO or CO2 on the interior. The resulting proton gradient across the cell membrane provides a proton-motive force, so that a variety of kinds of work can be done. It is envisioned as providing a selective advantage for cells capable of harvesting this potential. The proposed reactants for these reactions are consistent with the predicted composition of the Earth's early environment. Modern-day homologs of the ancestral components of the energy-transducing system are thought to be membrane-associated ferredoxins for the extracellular redox reaction, carbon monoxide dehydrogenase for the carbon fixation reaction, and ATPase for the harvesting of the proton gradient. With a source of consumable energy, the cell could drive chemical reactions and transport events in such a way as to be exploited by Darwinian evolution.
J
Mol
Evol 1991 Oct
PMID:The first cellular bioenergetic process: primitive generation of a proton-motive force. 166 58
An
iron
-regulated promoter was cloned on a 2.1 kb Bg/II fragment from Pseudomonas sp. strain M114 and fused to the lacZ reporter gene.
Iron
-regulated lacZ expression from the resulting construct (pSP1) in strain M114 was mediated via the Fur-like repressor which also regulates siderophore production in this strain. A 390 bp StuI-PstI internal fragment contained the necessary information for
iron
-regulated promoter expression. This fragment was sequenced and the initiation point for transcription was determined by primer extension analysis. The region directly upstream of the transcription start point contained no significant homology to known promoter consensus sequences. However the -16 to -25 bp region contained homology to four other
iron
-regulated pseudomonad promoters. Deletion of bases downstream from the transcriptional start did not affect the
iron
-regulated expression of the promoter. The -37 and -43 bp regions exhibited some homology to the 19 bp Escherichia coli Fur-binding consensus sequence. When expressed in E. coli (via a cloned transacting factor from strain M114) lacZ expression from pSP1 was found to be regulated by
iron
. A region of greater than 77 bases but less than 131 upstream from the transcriptional start was found to be necessary for promoter activity, further suggesting that a transcriptional activator may be required for expression.
Mol
Gen Genet 1991 Aug
PMID:Regulation of iron assimilation: nucleotide sequence analysis of an iron-regulated promoter from a fluorescent pseudomonad. 167 22
The present study was designed to shed light on the extraordinary histochemical properties of the chromophobe cell renal carcinoma detected by Hale's colloidal
iron
reaction. Special emphasis was laid on the lectin histochemical analysis of cytoplasmic glycoconjugates. Binding of peanut agglutinin (PNA) and Erythrina cristagalli agglutinin (ECA) after enzymatic release of sialic acid and direct binding of Dolichos biflorus agglutinin (DBA) correlates well with the expression of binding sites for Sambucus nigra agglutinin (SNA) and Maackia amurensis agglutinin (MAA) revealing abundant sialylated carbohydrate moieties within the cytoplasm. This characteristic binding pattern differs considerably from the faint staining observed in the majority of other renal carcinomas, thus confirming that the chromophobe cell renal carcinoma is a distinct entity. However, the lectin binding pattern of renal oncocytoma obviously resembles that of chromophobe carcinoma indicating a close relationship between these renal tumors. Detailed analysis of adjacent renal parenchyma revealed a lectin binding pattern quite similar to that described in the chromophobe carcinomas exclusively in the intercalated cells lining the collecting duct. This finding suggests that the chromophobe cell renal carcinoma originates from the collecting duct epithelium. The detection of small complexes consisting of altered epithelia which display the morphological characteristics of chromophobe carcinoma and the histochemical properties of intercalated cells probably indicates the emergence of preneoplastic lesions preceding the development of chromophobe carcinoma. Even though further studies are clearly needed to elucidate the physiological role of the cellular glycoconjugates detected, the present results already provide valuable insight into the histogenesis and pathogenesis of the chromophobe cell renal carcinoma.
Virchows Arch B Cell Pathol Incl
Mol
Pathol 1991
PMID:Sialylated glycoconjugates in chromophobe cell renal carcinoma compared with other renal cell tumors. Indication of its development from the collecting duct epithelium. 168 20
Alveolar macrophages and their products are thought to be important mediators of the inflammatory lesions and consequent interstitial fibrosis caused by inhalation of inorganic particles. Identification of a homolog of platelet-derived growth factor (PDGF) produced by rat alveolar macrophages that were stimulated with carbonyl
iron
particles and asbestos fibers motivated our studies on the biologic activity of this potent cytokine. Macrophage-derived PDGF (MD-PDGF) competes for specific membrane receptors on rat lung fibroblasts, initiating DNA synthesis and cell replication. The present report demonstrates that purified human PDGF and the MD-PDGF are chemotactic for early passage rat lung fibroblasts, but not for lung macrophages. Rat lung fibroblasts exhibit a typical bell-shaped, dose-related curve and respond optimally between 2 and 4 ng/ml PDGF. We found that alveolar macrophage-conditioned medium (AMCM), fractionated by gel filtration in 1 M acetic acid, induced a clear chemotactic response in the same fractions (20 to 22 ml) where PDGF was identified by enzyme immunoassay. In contrast, AMCM fractionated by gel filtration in phosphate-buffered saline did not induce any chemotactic activity unless the fractions were treated further with 1 M acetic acid. In this case, chemotactic activity was observed in those fractions with molecular weights of 150 and greater than 200 kD. All chemotactic activity observed with fractionated AMCM was blocked greater than 90% by an anti-PDGF antibody. These observations demonstrate that MD-PDGF is chemotactic for rat lung fibroblasts if it first is released from its binding protein, alpha-macroglobulin (alpha-M), which is secreted into the medium along with PDGF.(ABSTRACT TRUNCATED AT 250 WORDS)
Am J Respir Cell
Mol
Biol 1990 Dec
PMID:Rat alveolar macrophage-derived platelet-derived growth factor is chemotactic for rat lung fibroblasts. 170 6
ADR-529 protects against anthracycline cardiotoxicity, possibly by preventing free radical induction. We hypothesize that this occurs by ADR-529 forming a ternary anthracycline-
iron
-ADR-529 complex. This study used 200-MHz Fourier-transformed NMR to demonstrate the ability of ADR-529 to do this. Peak assignments were by proton-correlated spectroscopy and proton-carbon heteronuclear-correlated spectroscopy. Ga3+ served as a probe for Fe3+, and D2O was the system solvent. Doxorubicin and epirubicin were the studied drugs. Proton spectra of multiple combinations (including pure standards as controls) were obtained. Both Ga3+ plus ADR-529 and Ga3+ plus doxorubicin showed evidence of complexation, as seen by appropriate peak shifts and changes in the associated coupling constants. Ga3+ plus ADR-529 plus epirubicin showed complexation different from that of Ga3+ plus ADR-529 or Ga3+ plus doxorubicin and consistent with the proposed structure. We conclude that ADR-529 would be able to form a ternary complex with an existing anthracycline-Fe3+ complex in an isolated aqueous environment.
Mol
Pharmacol 1992 Jan
PMID:In vitro evidence for direct complexation of ADR-529/ICRF-187 [(+)-1,2-bis-(3,5-dioxo-piperazin-1-yl)propane] onto an existing ferric-anthracycline complex. 173 25
The molecular dimensions of the extracellular, hexagonal bilayer chlorocruorin of the polychaete Eudistylia vancouverii, determined by scanning transmission electron microscopy (STEM) of negatively stained specimens, were diameter of 27.5 nm and height of 18.5 nm. STEM mass measurements of unstained, freeze-dried specimens provided a molecular mass (Mm) of 3480 +/- 225 kDa. The chlorocruorin had no carbohydrate and its
iron
content was 0.251 +/- 0.021 wt%, corresponding to a minimum Mm of 22.4 kDa. Mass spectra and nuclear magnetic resonance spectra of the prosthetic group confirmed it to be protoheme IX with a formyl group at position 3. SDS/polyacrylamide gel electrophoresis, reversed-phase chromatography and N-terminal sequencing suggested that the chlorocruorin consists of at least three chains of approximately 30 kDa and five chains of approximately 16 kDa; the two types of subunits occur in the ratio 0.26:0.74(+/- 0.08). Complete dissociation of the chlorocruorin at neutral pH in the presence of urea or guanidine hydrochloride, followed by gel filtration, produced elution profiles consisting of three peaks, B, C and D. Fractions B and C consisted of the approximately 16 kDa chains and fraction D consisted of the approximately 30 kDa subunits. Mass measurements of particles in STEM images of unstained, freeze-dried fractions B and C provided Mm of 208 +/- 23 kDa and 65 +/- 12 kDa, respectively, in agreement with 191 +/- 13 kDa and 67 +/- 5 kDa obtained by gel filtration. Particles with Mm = 221 +/- 21 kDa were also observed in STEM images of unstained, freeze-dried chlorocruorin. These results imply that the chlorocruorin structure, in addition to the approximately 30 kDa linker subunits that have 0.26 to 0.47 heme groups/chain, comprises approximately 65 kDa tetramers and approximately 200 kDa dodecamers (trimers of tetramers) of globin chains. The stoichiometry of the tetramer and linker subunits calculated from molar amino acid compositions was 34 +/- 4 and 43 +/- 9. The complete dissociation of the chlorocruorin was accompanied by a 50 to 75% loss of the 55 +/- 14 Ca2+/mol protein, and was decreased to approximately 35% by the presence of 10 to 25 mM-Ca2+. Reassociation of dissociated chlorocruorin was maximal in the presence of 2.5 to 5 mM-Ca2+. The dodecamer and/or tetramer subunits in the absence or presence of Ca2+ exhibited very limited (less than 10%) reassociation into hexagonal bilayer structures, only in the presence of the linker subunit.(ABSTRACT TRUNCATED AT 400 WORDS)
J
Mol
Biol 1991 Dec 20
PMID:Hierarchy of globin complexes. The quaternary structure of the extracellular chlorocruorin of Eudistylia vancouverii. 176 47
A 2 kb DNA fragment isolated from a cosmid library of Aquaspirillum magnetotacticum strain MS-1 complements the aromatic-metabolite requirements and
iron
-uptake deficiencies of Escherichia coli and Salmonella typhimurium strains that lack a functional aroD (biosynthetic dehydrodquinase) sequence. All recombinant cosmids selected for their aroD complementation property carry this sequence. No DNA sequence homology has, however, been detected by Southern hybridization between the cloned fragment and the aroD gene of E. coli or the qa2 (catabolic dehydroquinase) gene of Neurospora crassa.
Mol
Microbiol 1991 Sep
PMID:Cloning of a sequence of Aquaspirillum magnetotacticum that complements the aroD gene of Escherichia coli. 176 90
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