9325434

Source:http://linkedlifedata.com/resource/pubmed/id/9325434

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0005528, umls-concept:C0025519, umls-concept:C0205307, umls-concept:C0302583, umls-concept:C0441712, umls-concept:C0597032, umls-concept:C1521991
pubmed:issue	1
pubmed:dateCreated	1997-10-28
pubmed:abstractText	Iron uptake by mammalian cells is mediated by the binding of serum Tf to the TfR. Transferrin is then internalized within an endocytotic vesicle by receptor-mediated endocytosis and the Fe released from the protein by a decrease in endosomal pH. Apart from this process, several cell types also have other efficient mechanisms of Fe uptake from Tf that includes a process consistent with non-specific adsorptive pinocytosis and a mechanism that is stimulated by small-Mr Fe complexes. This latter mechanism appears to be initiated by hydroxyl radicals generated by the Fe complexes, and may play a role in Fe overload disease where a significant amount of serum non-Tf-bound Fe exists. Apart from Tf-bound Fe uptake, mammalian cells also possess a number of mechanisms that can transport Fe from small-Mr Fe complexes into the cell. In fact, recent studies have demonstrated that the membrane-bound Tf homologue, MTf, can bind and internalize Fe from 59Fe-citrate. However, the significance of this Fe uptake process and its pathophysiological relevance remain uncertain. Iron derived from Tf or small-Mr complexes is probably transported into mammalian cells in the Fe(II) state. Once Fe passes through the membrane, it then becomes part of the poorly characterized intracellular labile Fe pool. Iron in the labile Fe pool that is not used for immediate requirements is stored within the Fe-storage protein, ferritin. Cellular Fe uptake and storage are coordinately regulated through a feedback control mechanism mediated at the post-transcriptional level by cytoplasmic factors known as IRP1 and IRP2. These proteins bind to stem-loop structures known as IREs on the 3 UTR of the TfR mRNA and 5 UTR of ferritin and erythroid delta-aminolevulinic acid synthase mRNAs. Interestingly, recent work has suggested that the short-lived messenger molecule, NO (or its by-product, peroxynitrite), can affect cellular Fe metabolism via its interaction with IRP1. Moreover, NO can decrease Fe uptake from Tf by a mechanism separate to its effects on IRP1, and NO may also be responsible for activated macrophage-mediated Fe release from target cells. On the other hand, the expression of inducible NOS which produces NO, can be stimulated by Fe chelators and decreased by the addition of Fe salts, suggesting that Fe is involved in the control of NOS expression.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0217513
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm, http://linkedlifedata.com/resource/pubmed/chemical/Ferritins, http://linkedlifedata.com/resource/pubmed/chemical/Iron, http://linkedlifedata.com/resource/pubmed/chemical/Iron Regulatory Protein 1, http://linkedlifedata.com/resource/pubmed/chemical/Iron Regulatory Protein 2, http://linkedlifedata.com/resource/pubmed/chemical/Iron-Regulatory Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Iron-Sulfur Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Melanoma-Specific Antigens, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transferrin, http://linkedlifedata.com/resource/pubmed/chemical/Transferrin
pubmed:status	MEDLINE
pubmed:month	Mar
pubmed:issn	0006-3002
pubmed:author	pubmed-author:PonkaPP, pubmed-author:RichardsonD RDR
pubmed:issnType	Print
pubmed:day	14
pubmed:volume	1331
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1-40
pubmed:dateRevised	2011-11-17
pubmed:meshHeading	pubmed-meshheading:9325434-Antigens, Neoplasm, pubmed-meshheading:9325434-Biological Transport, pubmed-meshheading:9325434-Ferritins, pubmed-meshheading:9325434-Humans, pubmed-meshheading:9325434-Iron, pubmed-meshheading:9325434-Iron Regulatory Protein 1, pubmed-meshheading:9325434-Iron Regulatory Protein 2, pubmed-meshheading:9325434-Iron-Regulatory Proteins, pubmed-meshheading:9325434-Iron-Sulfur Proteins, pubmed-meshheading:9325434-Melanoma, pubmed-meshheading:9325434-Melanoma-Specific Antigens, pubmed-meshheading:9325434-Models, Biological, pubmed-meshheading:9325434-Neoplasm Proteins, pubmed-meshheading:9325434-Neoplasms, pubmed-meshheading:9325434-Nitric Oxide, pubmed-meshheading:9325434-RNA-Binding Proteins, pubmed-meshheading:9325434-Receptors, Transferrin, pubmed-meshheading:9325434-Transferrin
pubmed:year	1997
pubmed:articleTitle	The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells.
pubmed:affiliation	Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital, McGill University, Montréal, Québec, Canada. des.richardson@jcu.edu.au
pubmed:publicationType	Journal Article, Review, Research Support, Non-U.S. Gov't