Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The heme-heme oxygenase system has recently been recognized to possess important regulatory properties. It is tightly involved in both physiological as well as pathophysiological processes, such as cytoprotection, apoptosis, and inflammation. Heme functions as a double-edged sword. In moderate quantities and bound to protein, it forms an essential element for various biological processes, but when unleashed in large amounts, it can become toxic by mediating oxidative stress and inflammation. The effect of this free heme on the vascular system is determined by extracellular factors, such as hemoglobin/heme-binding proteins, haptoglobin, albumin, and hemopexin, and intracellular factors, including heme oxygenases and ferritin. Heme oxygenase (HO) enzyme activity results in the degradation of heme and the production of iron, carbon monoxide, and biliverdin. All these heme-degradation products are potentially toxic, but may also provide strong cytoprotection, depending on the generated amounts and the microenvironment. Pre-induction of HO activity has been demonstrated to ameliorate inflammation and mediate potent resistance to oxidative injury. A better understanding of the complex heme-heme
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PMID:Different faces of the heme-heme oxygenase system in inflammation. 1286 63

The development of an enhanced chemiluminescence detection method for the rapid detection of haptoglobin phenotyping after polyacrylamide gel electrophoresis is described in this paper. The enhanced chemiluminescence detection is based upon chemiluminescent reaction between luminol and hydrogen peroxide. Increased sensitivity and dynamic range are achieved by employing ammonium persulfate to enhance the chemiluminescence signal. Detection of haptoglobin phenotypes in human blood serum was easily achieved even without the addition of hemoglobin. Different polyacrylamide gel electrophoresis results were found between pure serum and hemoglobin-supplemented serum. Applying the suggested enhanced chemiluminescence detection, the original combining forms of haptoglobin and hemoglobin can be detected. The linear range of haptoglobin is 0.1-13.3 microg/mL, with a detection limit of 1.21 ng (sample loading volume 15 microL). Other proteins, such as catalase and ferritin, can also be detected using enhanced chemiluminescence detection. All detections after polyacrylamide gel electrophoresis were completed within 15 min. The proposed detection is very fast, compared to traditional methods using staining detection (minutes versus hours).
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PMID:Chemiluminescent image detection of haptoglobin phenotyping after polyacrylamide gel electrophoresis. 1516 74

Erythropoiesis was studied in 11 subjects submitted to a 4-h hypoxia (HH) in a hypobaric chamber (4,500 m, barometric pressure 58.9 kPa) both before and after a 3-week sojourn in the Andes. On return to sea level, increased red blood cells (+3.27%), packed cell volume (+4.76%), haemoglobin (+6.55%) ( P<0.05), and increased arterial partial pressure of oxygen (+8.56%), arterial oxygen saturation (+7.40%) and arterial oxygen blood content ( C(a)O(2)) (+12.93%) at the end of HH ( P<0.05) attested high altitude acclimatization. Reticulocytes increased during HH after the sojourn only (+36.8% vs +17.9%, P<0.01) indicating a probable higher reticulocyte release and/or production despite decreased serum erythropoietin (EPO) concentrations (-46%, P<0.01). Hormones (thyroid, catecholamines and cortisol), iron status (serum iron, ferritin, transferrin and haptoglobin) and renal function (creatinine, renal, osmolar and free-water clearances) did not significantly vary (except for lower thyroid stimulating hormone at sea level, P<0.01). Levels of 2,3-diphosphoglycerate (2,3-DPG) increased throughout HH on return (+14.7%, P<0.05) and an inverse linear relationship was found between 2,3-DPG and EPO at the end of HH after the sojourn only ( r=-0.66, P<0.03). Inverse linear relationships were also found between C(a)O(2) and EPO at the end of HH before ( r=-0.63, P<0.05) and after the sojourn ( r=-0.60, P=0.05) with identical slopes but different ordinates at the origin, suggesting that the sensitivity but not the gain of the EPO response to hypoxia was modified by altitude acclimatization. Higher 2,3-DPG levels could partly explain this decreased sensitivity of the EPO response to hypoxia. In conclusion, we show that altitude acclimatization modifies the control of erythropoiesis not only at sea level, but also during a subsequent hypoxia.
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PMID:Control of erythropoiesis after high altitude acclimatization. 1524 67

Recent researches focused on the study of the role of the inflammation in the atherothrombotic pathogenesis of the acute cerebral ischemia. The aim of the study was to identify some acute phase proteins with possible role in the pathogenesis of the ischemic stroke. Some acute phase proteins were prospectively investigated by standard methods in sera of 78 patients with ischemic stroke in the first admission day. There were two groups according to neurological deficit one month after the ischemic stroke: good outcome and poor outcome. In the second group mean value of C-reactive protein (CRP) was 0.122 +/- 0.06 g/l (p < 0.01), mean value of C3 was 2.61 +/- 0.36 g/l (p < 0.01), mean value of C4 was 0.73 +/- 0.07 g/l (p < 0.05), mean value of alpha 1-antitrypsin (AAT) was 4.9 +/- 0.46 g/l (p < 0.01), mean value of alpha 1-antichymotrypsin (ACT) was 0.33 +/- 0.04 g/l (p < 0.01), mean value of alpha 1-acid glycoprotein (AGA) was 1.12 +/- 0.15 g/l, (p < 0.05), mean value of fibrinogen was 2.6 +/- 0.22 g/l (p < 0.01), mean value of haptoglobin was 2.8 +/- 0.33 g/l, (p < 0.05), mean value of transferrin was 2.8 +/- 0.26 g/l (p < 0.05), mean value of ferritin was 238 +/- 22.42 microg/l (p < 0.001), mean value of fibronectin was 2.14 +/- 0.17 g/l (p < 0.05), mean value of ceruloplasmin was 1.23 +/- 0.24 g/l (p < 0.01). High significant values of ferritine and significant values of CRP, C3, AAT, ACT and fibrinogen were observed in patients with poor outcome. The presented data suggest that the studied markers are useful to appreciate the role of the inflammatory reaction in the atherothrombotic pathogenesis of the ischemic stroke.
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PMID:Study of some markers of inflammation in atherothrombotic pathogenesis of acute ischemic stroke. 1552 46

Serum levels of acute phase reactants (APR) were measured in patients with rheumatoid arthritis (RA) and the correlations of these parameters with the disease activity score (DAS28) were investigated. The study included 47 patients with RA and 50 healthy controls. Laboratory tests included erythrocyte sedimentation rate (ESR), serum C-reactive protein (CRP), haptoglobin (Hp), ferritin, and plasma fibrinogen. Disease activity was assessed using the DAS28 score. The means (+/- SD) of ESR, CRP, Hp, ferritin, and fibrinogen levels were respectively 36.0 +/- 23.5 mm/hr, 2.4 +/- 1.9 mg/dl, 121.3 +/- 34.2 mg/dl, 67.7 +/- 36.2 ng/ml, and 371.2 +/- 96.0 mg/dl in the patients with RA, vs 16.4 +/- 11.3 mm/hr, 0.4 +/- 0.3 mg/dl, 104.0 +/- 35.3 mg/dl, 50.9 +/- 23 ng/ml, and 332.2 +/- 58.5 mg/dl in the controls. All of the APR levels were significantly higher in patients vs controls (p < 0.001 for ESR and CRP; p < 0.05 for Hp, ferritin, and fibrinogen). There were significant correlations between serum APR levels and disease activity based on DAS28 score in RA patients (for CRP, r = 0.650, p <0.01; for Hp, r = 0.331, p < 0.05; for ferritin, r = 0.299, p < 0.05; for fibrinogen, r = 0.373, p < 0.01). This study indicates that serum CRP, among the various ARP tests, is the most useful biochemical marker for evaluating the disease activity of patients with RA.
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PMID:Associations between acute phase reactant levels and disease activity score (DAS28) in patients with rheumatoid arthritis. 1564 84

A reduction in haemoglobin concentration is consistently reported after deep saturation dives. This may be due to a downregulation of erythropoietin (EPO) concentration or to a toxic effect of the hyperoxia associated with the dives resulting in an increased destruction rate of erythrocytes. In this study haemoglobin concentration, blood cell counts, serum ferritin, bilirubin, haptoglobin and EPO concentrations were measured before, during and after a 19 day saturation dive to 240 m. The partial pressure of oxygen (PO(2)) was 35-70 kPa during the 7 day compression and bottom phase, and 30-50 kPa during the 12 day decompression phase. There was a reduction in EPO concentration from 8.4+/-1.4 (mean +/- 1SD) to 6.3 +/- 1.9 U.L(-1) on Dive day 2. On Dive days 7 and 17 EPO concentrations were not significantly different from baseline despite the continued exposure to hyperoxia. Immediately after the dive and return to a normoxic environment there was an increase in the EPO concencentration to 14.5 +/- 4.7 U.L(-1). Haemoglobin concentration, erythrocyte and reticulocyte counts were decreased at the end of the dive, and there was an increase in serum ferritin. There were no changes in bilirubin or haptoglobin concentrations indicative of haemolysis. It appears that the change in PO(2), rather than the sustained exposure to a hyperoxic environment, induces the changes in the EPO concentrations and erythropoietic activity.
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PMID:Changes in erythropoietin and haemoglobin concentrations in response to saturation diving. 1600 37

Many reports have stated that some of the pathogenic bacteria can obtain iron from ferroproteins, such as cytochrome C, ferritin, hemin, hemoglobin, and myoglobin. These reports prompted us to determine if an opportunistic pathogenic fungus, Candida albicans, can utilize ferroproteins to circumvent the iron-regulatory effect of transferrin. The following assays were carried out to measure in vitro growth stimulation by the ferroproteins: as an initial step, C. albicans was cultured in iron-free (pretreated with apotransferrin for 24 h) culture medium. Once Candida albicans yeast cell growth reached stasis from iron starvation, individual ferroproteins were added to the culture media. Results showed that hemin, hemoglobin, and myoglobin supported a partial growth recovery. Additional studies with haptoglobin, a serum protein that interacts with the globin moiety of certain ferroproteins, established that C. albicans could obtain iron from the haptoglobin-ferroprotein complexes. These data indicate that the heme part of the ferroproteins is the source of iron. This implies that heme oxygenase, CaHMX1 might be involved in bringing about dissociation of heme-containing protein for iron-acquisition. In addition, anticandidal activity of transferrin takes place not only by the process of iron regulation, but also by direct interaction with the yeast cells.
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PMID:Utilization of ferroproteins by Candida albicans during candidastasis by apotransferrin. 1617 24

To characterize the mouse bone marrow tissue proteome and investigate the response to radiation damage we took bone marrow before and after 4-Gy gamma-irradiation from mouse strains (C57BL/6 and CBA/Ca) that differ in their short-term and long-term radiation responses and analyzed extracellular proteins by high-resolution 2-DE. Twenty proteins were identified from 71 protein spots in both C57BL/6 and CBA/Ca. We detected significant differences between control and irradiated bone marrow and between genotypes and identified many of the changed proteins by MS. In C57BL/6, 27 spots were significantly different between control and irradiated samples. In CBA/Ca, 18 spots showed significant changes following irradiation. Proteins such as serum albumin, apolipoprotein A-I, ferritin, haptoglobin (Hp) and alpha-1-antitrypsin were changed in irradiated bone marrow of both mouse strains, reflecting an ongoing acute-phase reaction. Several other proteins including serotransferrin, neutrophil collagenase, peroxiredoxin 2 and creatine kinase M chain were changed specifically in an individual mouse strain. The proteomic approach makes an important contribution to characterizing bone marrow proteome and investigating the tissue response of bone marrow to radiation, assists in identifying genotype-dependent responses and provides support for the importance of microenvironmental factors contributing to the overall response.
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PMID:A proteomic analysis of murine bone marrow and its response to ionizing radiation. 1619 97

The liver performs three main functions in iron homeostasis. It is the major site of iron storage, it regulates iron traffic into and around the body through its production of the peptide hepcidin, and it is the site of synthesis of major proteins of iron metabolism such as transferrin and ceruloplasmin. Most of the iron that enters the liver is derived from plasma transferrin under normal circumstances, and transferrin receptors 1 and 2 play important roles in this process. In pathological situations, non-transferrin-bound iron, ferritin, and hemoglobin/haptoglobin and heme/hemopexin complexes assume greater importance in iron delivery to the organ. Iron is stored in the liver as ferritin and, with heavy iron loading, as hemosiderin. The liver can divest itself of iron through the plasma membrane iron exporter ferroportin 1, a process that also requires ceruloplasmin. Hepcidin can regulate this iron release through its interaction with ferroportin.
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PMID:Hepatic iron metabolism. 1631 36

We have characterized a new abnormal hemoglobin (Hb) at position 32 of the alpha-globin chain. The proband, a 38-year-old woman of Surinamese Black ancestry, was referred to the Academic Hospital in Amsterdam, The Netherlands, after 3 years of Prednisone treatment in Surinam. Kidney failure was diagnosed at the Nephrology Department, Free University Medical Center, Amsterdam, The Netherlands; the cortisone treatment was interrupted and dialysis was started. At this stage, a microcytic hypochromic anemia was observed with high reticulocyte (40%) and ferritin (500 microg/L) levels, and hemoglobinopathy was suspected. No abnormal bands were visible on alkaline electrophoresis and high performance liquid chromatography (HPLC). The Hb A2 level was normal (2.7%) and the erythrocyte count was low (3.59 x 10(12)/L) with a normal haptoglobin level (68 mg/100 mL). None of the common alpha-thalassemia (thal) deletion defects were present. The beta-globin gene sequence was normal but the alpha2-globin gene sequence revealed an ATG-->ATA transition at codon 32, changing the methionine into an isoleucine residue. The mutation, called Hb Amsterdam, was observed in the mother of the proband, who was also heterozygous for the--alpha3.7-thal deletion and affected by a moderate microcytic hypochromic anemia. Both Hb Amsterdam and the--alpha(-3.7) allele were found in association with a new polymorphism, IVS-I-39 (C-->T), previously observed in our laboratory in seven patients of African origin, on both the alpha1 and alpha2 genes. In addition, Hb Amsterdam was also associated with the common African alpha2 polymorphism (G-->CTCGGCCC at position 7238 and T-->G at position 7174). Hb Amsterdam is the first mutation ever described at codon alpha32, a position involved in alpha1/beta1 interaction. The possibility of a contribution of this mutation to the nephropatic state of the proband is discussed.
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PMID:Hb Amsterdam [alpha32(B13)Met--Ile (alpha2)]: a new unstable variant associated with an alpha-thalassemia phenotype and a new African polymorphism. 1637 Apr 85


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