Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.16.3.1 (ceruloplasmin)
 5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mRNAs of proteins involved in iron metabolism were measured in isolated hepatocytes, Kupffer cells, sinusoidal endothelial cells (SECs), and hepatic stellate cells (HSCs). Levels of type I hereditary hemochromatosis gene (HFE), transferrin, hepcidin, transferrin receptors 1 and 2 (TfR1, TfR2), ferroportin 1 (FPN1), divalent metal transporter 1 (DMT1), natural resistance-associated macrophage protein 1 (Nramp1), ceruloplasmin, hephaestin, and glyceraldehyde 3-phosphate dehydrogenase (GAPDH), were measured by quantitative reverse-transriptase polyerase chain reaction (qRT-PCR). We show that hepatocytes express almost all the iron-related genes tested, in keeping with their central role in iron metabolism. In addition, hepatocytes had 10-fold lower TfR1 mRNA levels than TfR2 and the lowest levels of TfR1 of the 4 cell types isolated. Kupffer cells, which process senescent red blood cells and recycle the iron, had high levels of ferroportin 1, ceruloplasmin, and hephaestin mRNA. Most important, of all the cell types tested, hepatocytes had the highest level of HFE mRNA, a factor of 10 higher than Kupffer cells. In situ hybridization analysis was conducted with rat liver sections. Consistent with the qRT-PCR analysis, HFE gene expression was localized mainly in hepatocytes. Western blot analysis confirmed this finding. Unexpectedly, HSCs also had high levels of DMT1 and ferroportin, implicating them in either iron sensing or iron cycling.
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PMID:Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes. 1456 38

Iron, the major trace element in the body, is an essential component of many proteins and enzymes. As low-molecular-weight iron is potentially toxic to cells, higher organisms express a number of proteins for the transport and storage of iron. We review our current understanding of the intestinal absorption of iron in the light of recently identified membrane proteins, namely the ferrric reductase, Dcytb, the two iron(II) transport proteins, DMT1 and ferroportin/Ireg1, and hephaestin, the membrane-bound homologue of the ferroxidase ceruloplasmin. Two types of mammalian transferrin receptor, TfR1 and TfR2, are now known to exist. The structure of TfR1 and its role in the process of receptor-mediated cellular uptake of iron are presented together with structural information on the iron storage protein ferritin. Mechanisms for the regulation of levels of TfR1 and ferritin, as well as other proteins involved in iron homeostasis, are discussed. Our current knowledge and understanding of the structure of members of the transferrin family of iron-binding proteins and the nature of the iron-binding centres in transferrins is presented, together with information on the processes of iron-uptake and iron-release by transferrin and a summary of the elements that have been found to bind to transferrins.
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PMID:Structure/function overview of proteins involved in iron storage and transport. 1630 65

Smoking is associated with oxidative stress and increased risks of many chronic diseases that both shorten life and impair its quality. Low concentrations of several micronutrients, especially the antioxidants vitamin C and beta-carotene, are also associated with smoking, and there has been much interest in determining whether deficiencies in micronutrients are involved etiologically in smoking-related diseases. The objective of this review was to bring together reports on dietary intakes, biochemical indicators of micronutrient status, and results of some intervention studies on micronutrients where authors had compared outcomes in smokers and non-smokers. The micronutrients discussed are vitamins A, E, and C; the carotenoids; some of the B-vitamin group; and the minerals selenium, zinc, copper, and iron. The data were then examined to determine whether effects on the biochemical markers of micronutrient status were due to differences in dietary intakes between smokers and non-smokers or to the consequences of inflammatory changes caused by the oxidative stress of smoking. It was concluded that although smoking is associated with reduced dietary intake of vitamin C and carotenoid-containing foods, inflammatory changes increase turnover of these micronutrients so that blood concentrations are still lower in smokers than non-smokers even when there is control for dietary differences. In the case of vitamin E, there is some evidence for increased turnover of this nutrient in smokers, but this has little to no influence on blood concentrations, and there are no differences in dietary intake of vitamin E between smokers and non-smokers. Serum concentrations of vitamin A, folate, and vitamin B12 and B6 markers do not appear to be influenced by smoking, although there is some influence of dietary intake on concentrations of these nutrients in the body. In the case of the minerals examined, the main effects on biochemical markers of mineral status were attributed to inflammation and were therefore greater in heavy or long-term smokers. Serum concentrations of selenium and erythrocyte GPx activity were lower in smokers. Erythrocyte CuZn-SOD activity and serum ceruloplasmin concentrations were elevated, while serum zinc concentrations were depressed only in heavy smokers. Lastly, smoking appears to affect iron homeostasis mainly by changing hemoglobin concentrations, which were in general increased. Serum iron, TfR, and ferritin were mostly unaffected by smoking, except in pregnancy where there is evidence of increased erythropoiesis causing lower saturation of plasma transferrin and some evidence of lowering of iron stores.
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PMID:Monitoring micronutrients in cigarette smokers. 1704 81