Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Marrow-iron stores were absent or reduced in twenty-three of thirty-nine patients studied within 52 months of starting maintenance haemodialysis. 2. Oral iron was given to twelve patients (group I) with absent or reduced, and to eleven patients (group II) with normal or increased marrow-iron stores. 3. A significant increase in mean haemoglobin concentration and marrow iron was observed in group I. No significant change in mean haemoglobin concentration or marrow iron occurred in group II. Mean haemoglogin concentration after treatment was significantly higher in group I than in group II. 4. The four patients who had normal or increased marrow iron and who received no oral iron all suffered a fall in haemoglobin concentration, and three of them showed a reduction in marrow iron. 5. These findings indicate that continuous oral iron therapy should be given to all patients on maintenance dialysis to correct or prevent iron deficiency.
Clin Sci Mol Med Suppl 1975 Jun
PMID:Iron therapy in maintenance haemodialysis. 105 83

A purified polyclonal antiserum directed against the isolated main 80 kD IROMP (iron-regulated outer-membrane protein) from Pseudomonas aeruginosa PAO1 detected only the 80 kD polypeptide of outer-membrane proteins from PAO1 cells grown in iron deficiency in Western blots. It was also shown to inhibit the uptake of 59Fe pyoverdin by PAO1 cells as well as its binding to purified outer membranes. Immunofluorescence experiments with intact PAO1 cells confirmed that the receptor is present only at the surface of cells grown under conditions of iron deficiency. All these data allow us to conclude that the 80 kD main IROMP of P. aeruginosa is indeed the receptor for the siderophore ferripyoverdin.
Mol Microbiol 1990 Aug
PMID:Pyoverdin-facilitated iron uptake in Pseudomonas aeruginosa: immunological characterization of the ferripyoverdin receptor. 212 27

Previous studies have documented decreased activities of certain enzymes and altered function in polymorphonuclear leukocytes (PMN) during iron deficiency. The present study was undertaken to determine if the enzymatic abnormalities could be correlated with morphologic or quantitative change in PMN granules. Ultrastructural examination of primary and secondary granules and assessment of the secondary granule components alkaline phosphatase and vicinal glycol-containing glycoconjugates was performed in rabbit bone marrow, peripheral blood, and peritoneal heterophils. In addition, biochemical quantifications of the secondary granule component alkaline phosphatase and the primary granule marker beta-glucuronidase were performed. The results confirmed that a marked, significant decrease in alkaline phosphatase occurs in iron-deficient animals; however, no biochemical decrease in beta-glucuronidase activity was observed. Ultrastructurally, PMN secondary granules of iron-deficient rabbits tended to be more numerous than in controls when examined with morphometric and glycoconjugate staining methods, but lacked staining in alkaline phosphatase preparations. These results demonstrate that iron-deficient rabbits produce normal to increased quantities of primary and secondary granules, despite a uniform deficiency of alkaline phosphatase, a secondary granule marker.
Exp Mol Pathol 1986 Feb
PMID:Ultrastructural morphology and cytochemistry of iron-deficient polymorphonuclear leukocytes. 394 78

In 1991, we postulated that carbon monoxide, which is formed endogenously from heme catabolism catalyzed by heme oxygenase and shares some of the chemical and biological properties of nitric oxide, may play a role similar to that of nitric oxide as a widespread signal transduction mechanism for the regulation of cell function and communication. We review the experimental evidence that tests this postulate. Carbon monoxide appears to be involved in the neurophysiological phenomenon of long-term potentiation, which appears to play a key role in memory and learning. Zinc protoporphyrin, an inhibitor of heme oxygenase, prevents induction of long-term potentiation. Zinc protoporphyrin is an endogenous substance, the levels of which are increased in iron deficiency states and in lead poisoning, and by inhibiting heme oxygenase may modulate long-term potentiation and memory. It has been shown that, when cobalt protoporphyrin is injected into the medial nuclei of the rat hypothalamus, weight loss occurs. These nuclei contain heme oxygenase, and we postulate that weight loss is due to cobalt protoporphyrin induction of heme oxygenase and increased formation of carbon monoxide, which serves as a signal transduction mechanism in the medial hypothalamus to suppress appetite.
Cell Mol Biol (Noisy-le-grand) 1994 Nov
PMID:Heme oxygenase: the physiological role of one of its metabolites, carbon monoxide and interactions with zinc protoporphyrin, cobalt protoporphyrin and other metalloporphyrins. 784 53

Male Fischer rats were maintained for a period of 17 weeks on an iron-deficient diet along with suitable controls. The effect of long term deprivation of iron on xenobiotic metabolism was studied by the activities of various drug metabolising enzymes in both liver as well as extra-hepatic tissues like lungs, kidneys and intestinal mucosa (I.M.). The results show that among the Phase I (activating) enzymes, the hepatic activities of benzo(a)pyrene hydroxylase (AHH) and microsomal epoxide hydrolase (mEH) are significantly reduced in iron deficiency. The other parameters of the activating system, namely cytochrome P450, aminopyrene demethylase (ADM) and aniline hydroxylase (AH), are not altered. Of the two Phase II (conjugating) enzymes studied, only uridine diphospho glucuronyl transferase (UDPGT) is found to be depressed, but not glutathione S-transferase (GST) in liver in iron deficiency. Activities of Phase I enzymes are markedly lowered in extra-hepatic tissues compared to liver; such depression is not observed in conjugating enzymes. Iron deficiency does not seem to make much impact on the enzyme activities of extra-hepatic tissues. Overall, the hepatic results suggest a defect in detoxification mechanisms in iron deficiency. Such impairment may very well predispose an iron-deficient host to an increased risk of carcinogenesis.
Comp Biochem Physiol B Biochem Mol Biol 1995 Jan
PMID:Effect of long term iron deficiency on the activities of hepatic and extra-hepatic drug metabolising enzymes in Fischer rats. 785 40

A lambda zapII cDNA library was constructed from mRNA isolated from Fe-deficient barley roots and screened with cDNA probes made from mRNA of Fe-deficient and Fe-sufficient (control) barley roots. Seven clones were selected. Among them a clone having the putative full-length mRNA of dioxygenase as judged by northern hybridization was selected and named Ids2 (iron deficiency-specific clone 2). Using a cDNA fragment as probe, two clones from the genomic library (lambda EMBL-III) were isolated and one was sequenced. The predicted amino acid sequence of Ids2 resembled that of 2-oxoglutarate-dependent dioxygenase. Ids2 is expressed in the Fe-deficient barley roots but is not in the leaves. The expression is repressed by the availability of Fe. Ids2 was also strongly expressed under Mn deficiency and weakly under Zn deficiency or excess NaCl (0.5%). The upstream 5'-flanking region of Ids2 has a root-specific cis element of the CaMV 35S promoter and a nodule-specific element of leghemoglobin, a metal regulatory element (MRE) and several Cu regulatory elements (UAS) of yeast metallothionein (CUP1).
Plant Mol Biol 1994 Jul
PMID:A dioxygenase gene (Ids2) expressed under iron deficiency conditions in the roots of Hordeum vulgare. 806 21

The photosynthetic apparatus is rich in iron-containing cofactors and iron deficiency causes severe impairment of photosynthesis in plants, algae, and cyanobacteria. Synechocystis sp. PCC 6803 serves as a model system to investigate the complex assembly and integration of the multi-subunit protein complexes of oxygenic photosynthetic electron transport; particularly when coupled to developmental cues due to nutrient limitation or requirements. We study Fe(3+)-deficient and Fe(3+)-supplemented cultures of Synechocystis sp. PCC 6803. The autotrophic growth rate of Fe(3+)-deficient cultures is slower than Fe(3+)-supplemented cultures. Whole cell spectral analysis reveals differences in both the quantity and the peak absorbance of chlorophyll. Fe3+ deficiency decreases rates of photosynthetic electron transport and the mRNA and corresponding protein levels as observed using specific probes. mRNA levels of psaB increased 20-fold during recovery from Fe3+ deficiency, as compared to the control. psaD transcript levels increased to 160% during recovery as compared to the control. PsaA/B heterodimer formation and turnover is dependent on Fe3+ and the complete assembly on the reducing side of photosystem I (PS I) is PsaD-dependent. Recovery from Fe3+ deficiency suggests that regulation occurs at both the mRNA and protein level.
Plant Mol Biol 1993 Dec
PMID:Characterization of Synechocystis sp. PCC 6803 in iron-supplied and iron-deficient media. 829 89

Several cellular mRNAs are regulated posttranscriptionally by iron-responsive elements (IREs) and the cytosolic IRE-binding proteins IRP-1 and IRP-2. Three different signals are known to elicit IRP-1 activity and thus regulate IRE-containing mRNAs: iron deficiency, nitric oxide (NO), and the reactive oxygen intermediate hydrogen peroxide (H2O2). In this report, we characterize the pathways for IRP-1 regulation by NO and H2O2 and examine their effects on IRP-2. We show that the responses of IRP-1 and IRP-2 to NO remarkably resemble those elicited by iron deficiency: IRP-1 induction by NO and by iron deficiency is slow and posttranslational, while IRP-2 induction by these inductive signals is slow and requires de novo protein synthesis. In contrast, H2O2 induces a rapid posttranslational activation which is limited to IRP-1. Removal of the inductive signal H2O2 after < or = 15 min of treatment (induction phase) permits a complete IRP-1 activation within 60 min (execution phase) which is sustained for several hours. This contrasts with the IRP-1 activation pathway by NO and iron depletion, in which NO-releasing drugs or iron chelators need to be present during the entire activation phase. Finally, we demonstrate that biologically synthesized NO regulates the expression of IRE-containing mRNAs in target cells by passive diffusion and that oxidative stress endogenously generated by pharmacological modulation of the mitochondrial respiratory chain activates IRP-1, underscoring the physiological significance of NO and reactive oxygen intermediates as regulators of cellular iron metabolism. We discuss models to explain the activation pathways of IRP-1 and IRP-2. In particular, we suggest the possibility that NO affects iron availability rather than the iron-sulfur cluster of IRP-1.
Mol Cell Biol 1996 Jul
PMID:Nitric oxide and oxidative stress (H2O2) control mammalian iron metabolism by different pathways. 866 95

Few data exist on the iron status and metabolism in macaques, which are considered optimal models for the study of reproductive biology and anemia. The delivery influence on the hematological parameters of iron metabolism was investigated in adult Macaca fascicularis females during late pregnancy and at 6 weeks postpartum follow-up. No significant differences were detected for each parameter by one-way analysis of variance. A decrease of all parameters was observed at delivery. During the following weeks, however, the hematological values progressively came back to normal. In conclusion, notwithstanding the increased need of iron faced during pregnancy, a balanced diet, including iron, does not allow the development of either iron deficiency or sideropenic anemia.
Comp Biochem Physiol B Biochem Mol Biol 1996 Jun
PMID:Role of delivery on serum iron-related parameters in Macaca fascicularis females. 875 90

Iron is one of the most important micronutrients for plants. Like other organisms, plants have developed active mechanisms for the acquisition of sufficient iron from the soil. Nevertheless, very little is known about the genetic mechanisms that control the active uptake. In tomato, two spontaneously derived mutants are available, which are defective in key steps that control this process. The recessive mutation chloronerva (chln) affects a gene which controls the synthesis of the non-protein amino acid nicotianamine (NA), a key component in the iron physiology of plants. The root system of the recessive mutant fer is unable to induce any of the characteristic responses to iron deficiency and iron uptake is thus completely blocked. We present a characterization of the double mutant, showing that the fer gene is epistatic over the chln gene and thus very likely to be one of the major genetic elements controlling iron physiology in tomato. In order to gain access to these two genes at the molecular level, both mutants were precisely mapped onto the high density RFLP map of tomato. The chln gene is located on chromosome 1 and the fer gene is on chromosome 6 of tomato. Using this high-resolution map, a chromosome walk has been started to isolate the fer gene by map-based cloning. The isolation of the fer gene will provide new insights into the molecular mechanisms of iron uptake control in plants.
Mol Gen Genet 1996 Aug 27
PMID:Genetic analysis of two tomato mutants affected in the regulation of iron metabolism. 880 7


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