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Query: UMLS:C0240066 (iron deficiency)
7,156 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

On a field trip toSaudi Arabia (M.A.F.E.H.) in which the relationship between alpha-thalassemia and iron deficiency was studied, a fast moving hemoglobin variant was noted in a 30 year old Saudi Arabian woman. Analysis of the hemoglobin variant showed that the amino acid substitution was beta120 Lys replaced by Asn. This variant had not been described previously and has been named Hb Riyadh. There was also present an alpha-thalassemia and details are given of the imbalance of globin chain synthesis. It was possible to improve considerably the balance in vitro by the addition of hemin.
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PMID:Hemoglobin Riyadh--alpha2beta2 (120(GH3)Lys replaced by Asn). A new variant found in association with alpha-thalassemia and iron deficiency. 105 71

Iron is regarded as one of the most important nutriments, and many diseases are related to iron deficiency or its overload. Approximately 70% of iron in the body is located in heme, functioning as hemoglobin, myoglobin, and cytochrome P450. Iron itself also has many catalytic functions through the iron-sulfa cluster. It is believed that iron and/or heme plays significant roles in regulation of genes, however, little about the mechanism has been elucidated. Recently, not only iron but also heme has been identified as important regulators of gene activation via oxygen sensing. For example, iron controls the oxygen response of HIF-1 activity by two mechanisms; in cytosol, the half life of HIF-1 alpha is determined by hydroxylation of Pro, and transcriptional activity of HIF1 alpha in nuclei is disturbed by hydroxylation of Asn. Hemoproteins in prokaryotes such as FixL, Dos, and HemAT were found to be oxygen sensors, however, little has been reported in eukaryotes. Our finding on Bach1 seems to be the first report of heme and oxygen-mediated regulation of genes in vertebrates. Understanding of these newly identified mechanisms in iron- and heme-controlled genes is essential in the field of nutritional science. We therefore summarize here the recent findings indicating mechanisms of iron as transcriptional regulators.
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PMID:[Molecular biology of iron in nutritional science]. 1280 62

Here, we report a rare coincidence of heterozygous hemoglobinopathy (Hb) Stanleyville II and severe pernicious anemia due to autoimmune gastritis. Hb Stanleyville II is characterized by a single base exchange (AAC-->AAA) resulting in a substitution Asn --> Lys at position 78 of hemoglobin alpha2-chain. Under normal conditions this hemoglobinopathy does not cause any symptoms even if present as homozygous variant. However, in our case diagnosis of pernicious anemia was hampered by the absence of typical erythrocytic macrocytosis and hyperchromasia. In addition, interpretation of bone marrow smears was difficult as characteristic findings for pernicious anemia were little pronounced. All known reasons for the absence of typical cytomorphologic signs in pernicious anemia as underlying iron deficiency and thalassemia could be excluded.
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PMID:Cytomorphologic signs of severe pernicious anemia obscured in a patient with heterozygous hemoglobin Stanleyville II. 1768 Aug 15

Iron deficiency is a common nutritional disorder worldwide. Peptides derived from protein hydrolysates have recently attracted interest as novel iron chelators due to their superiority in terms of increasing solubility, bioavailability, absorption and stability. The aim of this study was to isolate and identify iron-chelating peptides from casein hydrolysates. Casein was hydrolyzed (trypsin, 3 h) and subsequently isolated using ultrafiltration and RP-HPLC. Four iron-chelating casein hydrolysate peptides, named CHP-1, CHP-2, CHP-3 and CHP-4, were identified by LC-MS/MS, and their amino acid sequences were Glu-Asp-Val-Pro-Ser-Glu-Arg (EDVPSER), His-Lys-Glu-Met-Pro-Phe-Pro-Lys (HKEMPFPK), Asn-Met-Ala-Ile-Asn-Pro-Ser-Lys (NMAINPSK) and Ala-Val-Pro-Tyr-Pro-Gln-Arg (AVPYPQR), with molecular weights of 830.6120 Da, 1012.5280 Da, 873.4440 Da and 829.4570 Da, respectively. The artificially synthesized peptides of CHP-1, CHP-2, CHP-3 and CHP-4 were verified, and their iron-chelating rates were 11.14%, 8.02%, 7.57% and 59.76%, respectively. These results suggested that the isolated iron-chelating peptides might serve as potential iron supplements and be used as food additives and functional foods.
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PMID:Isolation and identification of iron-chelating peptides from casein hydrolysates. 3099 79