| 词条 | Macrophage migration inhibitory factor domain |
| 释义 |
| Symbol = MIF | Name = MIF | image = PDB 1dpt EBI.jpg | width = | caption = d-dopachrome tautomerase | Pfam = PF01187 | Pfam_clan = CL0082 | InterPro = IPR001398 | SMART = MIF4G | PROSITE = PDOC00892 | MEROPS = | SCOP = 1mif | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} Macrophage migration inhibitory factor domain is an evolutionary conserved protein domain. Macrophage migration inhibitory factor (MIF) is a key regulatory cytokine within innate and adaptive immune responses, capable of promoting and modulating the magnitude of the response.[1] MIF is released from T-cells and macrophages, and acts within the neuroendocrine system. MIF is capable of tautomerase activity, although its biological function has not been fully characterised. It is induced by glucocorticoid and is capable of overriding the anti-inflammatory actions of glucocorticoid.[2] MIF regulates cytokine secretion and the expression of receptors involved in the immune response. It can be taken up into target cells in order to interact with intracellular signalling molecules, inhibiting p53 function, and/or activating components of the mitogen-activated protein kinase and Jun-activation domain-binding protein-1 (Jab-1).[1] MIF has been linked to various inflammatory diseases, such as rheumatoid arthritis and atherosclerosis.[3]The MIF homologue D-dopachrome tautomerase (EC 4.1.1.84) is involved in detoxification through the conversion of dopaminechrome (and possibly norepinephrinechrome), the toxic quinine product of the neurotransmitter dopamine (and norepinephrine), to an indole derivative that can serve as a precursor to neuromelanin.[4][5] ExamplesHuman genes encoding proteins that contain this domain include DDT and MIF. References1. ^1 {{cite journal |vauthors=Donn RP, Ray DW | title = Macrophage migration inhibitory factor: molecular, cellular and genetic aspects of a key neuroendocrine molecule | journal = J. Endocrinol. | volume = 182 | issue = 1 | pages = 1–9 |date=July 2004 | pmid = 15225126 | doi = 10.1677/joe.0.1820001| url = }} {{InterPro content|IPR001398}}2. ^{{cite journal |vauthors=Van Molle W, Libert C | title = How glucocorticoids control their own strength and the balance between pro- and anti-inflammatory mediators | journal = Eur. J. Immunol. | volume = 35 | issue = 12 | pages = 3396–9 |date=December 2005 | pmid = 16331703 | doi = 10.1002/eji.200535556 | url = }} 3. ^{{cite journal |vauthors=Morand EF, Leech M, Bernhagen J | title = MIF: a new cytokine link between rheumatoid arthritis and atherosclerosis | journal = Nat Rev Drug Discov | volume = 5 | issue = 5 | pages = 399–410 |date=May 2006 | pmid = 16628200 | doi = 10.1038/nrd2029 | url = }} 4. ^{{cite journal |vauthors=Matsunaga J, Sinha D, Solano F, Santis C, Wistow G, Hearing V | title = Macrophage migration inhibitory factor (MIF)--its role in catecholamine metabolism | journal = Cell. Mol. Biol. (Noisy-le-grand) | volume = 45 | issue = 7 | pages = 1035–40 |date=November 1999 | pmid = 10644007 | doi = | url = }} 5. ^{{cite journal |vauthors=Sugimoto H, Taniguchi M, Nakagawa A, Tanaka I, Suzuki M, Nishihira J | title = Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 A resolution | journal = Biochemistry | volume = 38 | issue = 11 | pages = 3268–79 |date=March 1999 | pmid = 10079069 | doi = 10.1021/bi982184o | url = }} 1 : Protein domains |
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