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MIF (macrophage migration inhibitory factor (glycosylation-inhibiting factor))

Identity

Other namesGIF
GLIF
MMIF
HGNC (Hugo) MIF
LocusID (NCBI) 4282
Location 22q11.23
Location_base_pair Starts at 24236565 and ends at 24237409 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

Note [Annexed document]
 
Description 0,84 kb; mRNA: 561 bp; 3 Exons.
Transcription The promoter region contains no TATA box.
Pseudogene There are no MIF pseudogenes in the human genome. In contrast 5 pseudogenes have been described in the murine genome.

Protein

Description MIF is comprised of 115 amino acids with a molecular weight of 12,5 kDa (Weiser et al., 1989). In addition, research on the secondary structure revealed the existence of two antiparallel alpha-helices and six beta-pleated sheets with a high degree of similarity to MHC molecules (Suzuki et al., 1996). MIF acts as a pro-inflammatory protein, exists as a homo-trimer and displays enzymatic action (Rosengren et al., 1996).
Expression Widely.
Localisation Intracellular, cytoplasm, cytosolic, near the plasma membrane, perinuclear.
Function MIF monomers are able to align in order to form a homotrimeric molecule that is homologous to the enzyme D-Dopachrome-tautomerase (Sun et al., 1996). >From this structural analysis, some researches suggested that MIF may also display enzymatic activity (Rosengren et al., 1996). To date, the physiological importance of this enzymatic activity has not yet been revealed. Interestingly, using ISO-1, a known inhibitor of the enzyme D-Dopachrome-tautomerase led to reduced activity of MIF (Lubetsky et al., 2002). Therefore, it was hypothesized that this enzymatic activity may be related to its proper functioning. The protein MIF is involved in inducing angiogenesis, promoting cell cycle progression, inhibiting apoptosis and inhibiting lysing of tumor cells by NK cells (Takahashi et al., 1998; Shimizu et al., 1999; Mitchell and Bucala, 2000; Morrison et al., 2001; Fingerle-Rowson et al., 2003). Recently, the CD74 molecule has been suggested to act as a potential receptor for MIF (Leng et al., 2003).
Homology MIF shows homology to the enzyme D-Dopachrome tautomerase.

Mutations

Note Not known.

Implicated in

Entity Colon cancer
Disease MIF is upregulated in tumors as well as precancerous lesions (Wilson et al., 2005). They examined patients suffering from adenomas. In addition, an animal model of adenomatous polyposis coli was used. In both settings, the authors describe an increase in MIF mRNA levels in the diseases group when this was compared to healthy controls. Interestingly, in a mouse model of intestinal tumorigenesis, MIF deletion leads to a significant decrease in tumor size. In addition, reduced angiogenesis was taking place. The involvement of MIF in angiogenesis was also shown by Ogawa et al., using a mouse model of colon cancer (Ogawa et al., 2000). The application of MIF antibodies leads to suppression of angiogenesis in this disease model. Further work by Sun et al. demonstrated an involvement of MIF in tumor cell migration (Sun et al., 2005). They used siRNA technique and were able to show inhibition of cell migration after addition of siRNA directed against MIF. In an animal model, they injected colon cancer cells into mice portal vein after pretreatment with siRNA. The number of liver metastases was significantly reduced in the pretreated model. In summary, there is sufficient evidence to assume a role of MIF in both angiogenesis and tumor cell migration in colon cancer (Bach et al., 2009).
Prognosis MIF expression is correlated with outcome (Legendre et al., 2003). Legendre et al. (2003) examined MIF distribution in 99 specimens of colorectal cancer. Primarily, they applied immunohistochemistry. They describe that the expression of MIF (and also galectin-3) were increased in tumor tissue compared to normal tissue. For MIF, they could provide evidence that in Dukes C or D tumors with high concentration of MIF, this was associated with significantly better prognosis than in tumors with low MIF concentrations. They suggest that MIF could be used to identify patients at risk needing more aggressive treatment strategies.
  
Entity Melanoma
Disease MIF inhibits lysis of melanoma cells by NK cells (Repp et al., 2000). This was shown by Apte et al., who demonstrated that NK cells are prevented from cell lysis of melanoma cells (Apte et al., 1998). This underlines the influence of MIF on the immune system. In addition, it enhances tumor cell proliferation.
Prognosis To date, there is no clear association between MIF concentration and prognosis in melanoma cells.
  
Entity Prostate cancer
Disease MIF was shown to be abundant in prostate cancer (Meyer-Siegler et al., 1998). In addition, MIF was shown to influence cell viability and invasiveness. Specifically in prostate cancer, androgen independent cancer cells relied on MIF activated pathways in order to grow and for their invasiveness. Androgen dependent tumor cells did not require these signal transduction pathways. Meyer-Siegler et al. were able to show that CD74, a potential MIF surface receptor, was abundant in androgen-independent tumor cells (Meyer-Siegler et al., 2006). Receptor blockage as well as strategies to reduce MIF resulted in decreased cell proliferation, MIF secretion and invasion of tumor cells.
Prognosis MIF expression clearly correlates with disease progression (Meyer-Siegler et al., 2002). In androgen independent prostate cancer, cells require MIF activated signal transduction pathways for invasion and growth, in contrast to androgen dependent tumor cells. In a study by Meyer-Siegler, serum MIF concentration was measured in dependence of Gleason score in patients with prostate cancer (Meyer-Siegler et al., 2002). They were able to show that increased MIF concentration is positively associated with a Gleason Score greater than 5. In addition, even in patients with normal prostate-specific antigen, MIF concentration was increased. From their data, they conclude that MIF may be a suitable biomarker for prostate cancer.
  
Entity Lung adenocarcinoma
Note Treatment with siRNA leads to a significant reduction in cell invasiveness and cell migration (Rendon et al., 2007), paralled by a reduction of a Rho GTPase. MIF overexpression led to adverse effects.
Prognosis Kamimura and colleagues analysed the role of MIF with respect to prognosis in lung cancer (Kamimura et al., 2000). They used immunofluorescence staining in primary lung tissue that had been obtained surgically. They were able to demonstrate a diffuse staining pattern within the cytoplasm. Furthermore, sometimes, a nuclear staining was also observed. Interestingly, the authors were able to demonstrate a correlation between a lack of nuclear staining and a poorer prognosis. From this observation, they concluded that MIF might play different roles with respect to subcellular localization. It needs to be mentioned however, that only thirty-eight cases were reviewed.
  
Entity Glioblastoma
Note MIF is involved in angiogenesis and cell cycle regulation. It was demonstrated that MIF expression is induced following hypoxia and hypoglycemia (Bacher et al., 2003), which are both considered activators of angiogenesis. Using immunofluorescence techniques, MIF could be demonstrated around necrotic tissue and in blood vessels surrounding tumor cells. Therefore it was concluded that neovascularization is enhanced by MIF. In line with this observation is the work published by Munaut et al. (2002). They demonstrated that there is a correlation between MIF expression and the expression of vascular endothelial growth factor (VEGF). They analysed primary glioblastoma tissue using RT-PCR and immmunohistochemistry and they were able to show a strong correlation between MIF expression and VEGF mRNA concentration. >From these data, it was suggested that there may be a common triggering factor. Inactivation of p53 may be of central importance, as it is a common event in glioblastoma progression (Bach et al., 2009). In addition, p53 inactivation is also involved in increased VEGF expression (Kieser et al., 1994). Since the angiogenic potential of a tumor is vital for formation of metastases, it may be a potential target for antitumor therapy.
  
Entity Hepatocellular carcinoma
Note MIF expression and increased angiogenesis were also demonstrated in hepatocellular carcinoma following hypoxia (Hira et al., 2005).
Prognosis MIF overexpression correlates with negative prognosis (Hira et al., 2005). 56 samples of hepatocellular carcinoma were analysed using Western blot and correlated these values with clinical parameters. In addition, they used immunohistochemistry. They showed that MIF expression was correlated with high alpha fetoprotein level and the recurrence of hepatic tumor. In addition, tumor free survival was reduced when MIF expression was increased. In addition, increased mRNA concentrations can be seen (Ren et al., 2003).
  

External links

Nomenclature
HGNC (Hugo)MIF   7097
Cards
AtlasMIFID41365ch22q11
Entrez_Gene (NCBI)MIF  4282  macrophage migration inhibitory factor (glycosylation-inhibiting factor)
GeneCards (Weizmann)MIF
Ensembl (Hinxton) [Gene_View]  chr22:24236565-24237409 [Contig_View]  MIF [Vega]
AceView (NCBI)MIF
Genatlas (Paris)MIF
WikiGenes4282
SOURCE (Princeton)NM_002415
Genomic and cartography
GoldenPath (UCSC)MIF  -  22q11.23   chr22:24236565-24237409 +  22q11.23   [Description]    (hg19-Feb_2009)
EnsemblMIF - 22q11.23 [CytoView]
Mapping of homologs : NCBIMIF [Mapview]
OMIM153620   604302   
Gene and transcription
Genbank (Entrez)AF469046 AK311929 BC000447 BC007376 BC007676
RefSeq transcript (Entrez)NM_002415
RefSeq genomic (Entrez)AC_000154 NC_000022 NC_018933 NG_012099 NT_011520 NW_001838745 NW_004929430
Consensus coding sequences : CCDS (NCBI)MIF
Cluster EST : UnigeneHs.407995 [ NCBI ]
CGAP (NCI)Hs.407995
Alternative Splicing : Fast-db (Paris)GSHG0019883
Gene ExpressionMIF [ NCBI-GEO ]     MIF [ SEEK ]   MIF [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP14174 (Uniprot)
NextProtP14174  [Medical]
With graphics : InterProP14174
Splice isoforms : SwissVarP14174 (Swissvar)
Catalytic activity : Enzyme5.3.2.1 [ Enzyme-Expasy ]   5.3.2.15.3.2.1 [ IntEnz-EBI ]   5.3.2.1 [ BRENDA ]   5.3.2.1 [ KEGG ]   
Domaine pattern : Prosite (Expaxy)MIF (PS01158)   
Domains : Interpro (EBI)Macrophage_inhib_fac    Macrophage_inhib_fac_CS    Tautomerase/MIF_sf   
Related proteins : CluSTrP14174
Domain families : Pfam (Sanger)MIF (PF01187)   
Domain families : Pfam (NCBI)pfam01187   
Domain structure : Prodom (Prabi Lyon)Macrophage_inhib_fac (PD004816)   
DMDM Disease mutations4282
Blocks (Seattle)P14174
PDB (SRS)1CA7    1CGQ    1GCZ    1GD0    1GIF    1LJT    1MIF    1P1G    2OOH    2OOW    2OOZ    3B9S    3CE4    3DJH    3DJI    3HOF    3IJG    3IJJ    3JSF    3JSG    3JTU    3L5P    3L5R    3L5S    3L5T    3L5U    3L5V    3SMB    3SMC    3U18    4ETG    4EUI    4EVG    4F2K   
PDB (PDBSum)1CA7    1CGQ    1GCZ    1GD0    1GIF    1LJT    1MIF    1P1G    2OOH    2OOW    2OOZ    3B9S    3CE4    3DJH    3DJI    3HOF    3IJG    3IJJ    3JSF    3JSG    3JTU    3L5P    3L5R    3L5S    3L5T    3L5U    3L5V    3SMB    3SMC    3U18    4ETG    4EUI    4EVG    4F2K   
PDB (IMB)1CA7    1CGQ    1GCZ    1GD0    1GIF    1LJT    1MIF    1P1G    2OOH    2OOW    2OOZ    3B9S    3CE4    3DJH    3DJI    3HOF    3IJG    3IJJ    3JSF    3JSG    3JTU    3L5P    3L5R    3L5S    3L5T    3L5U    3L5V    3SMB    3SMC    3U18    4ETG    4EUI    4EVG    4F2K   
PDB (RSDB)1CA7    1CGQ    1GCZ    1GD0    1GIF    1LJT    1MIF    1P1G    2OOH    2OOW    2OOZ    3B9S    3CE4    3DJH    3DJI    3HOF    3IJG    3IJJ    3JSF    3JSG    3JTU    3L5P    3L5R    3L5S    3L5T    3L5U    3L5V    3SMB    3SMC    3U18    4ETG    4EUI    4EVG    4F2K   
Peptide AtlasP14174
HPRD01091
IPIIPI00293276   
Protein Interaction databases
DIP (DOE-UCLA)P14174
IntAct (EBI)P14174
BioGRIDMIF
InParanoidP14174
Interologous Interaction database P14174
IntegromeDBMIF
STRING (EMBL)MIF
Ontologies - Pathways
Ontology : AmiGOprostaglandin biosynthetic process  negative regulation of mature B cell apoptotic process  dopachrome isomerase activity  receptor binding  cytokine activity  cytokine receptor binding  protein binding  extracellular region  extracellular space  cytoplasm  inflammatory response  cell surface receptor signaling pathway  cell aging  cell proliferation  cell surface  negative regulation of gene expression  positive regulation of protein kinase A signaling cascade  carboxylic acid metabolic process  DNA damage response, signal transduction by p53 class mediator  positive regulation of B cell proliferation  positive regulation of lipopolysaccharide-mediated signaling pathway  negative regulation of cellular protein metabolic process  negative regulation of myeloid cell apoptotic process  positive regulation of peptidyl-serine phosphorylation  chemoattractant activity  positive regulation of phosphorylation  regulation of macrophage activation  negative regulation of apoptotic process  positive regulation of MAP kinase activity  negative regulation of DNA damage response, signal transduction by p53 class mediator  innate immune response  positive regulation of fibroblast proliferation  phenylpyruvate tautomerase activity  positive regulation of cytokine secretion  positive regulation of peptidyl-tyrosine phosphorylation  positive chemotaxis  positive regulation of prostaglandin secretion involved in immune response  positive regulation of myeloid leukocyte cytokine production involved in immune response  protein homotrimerization  positive regulation of ERK1 and ERK2 cascade  negative regulation of cell cycle arrest  positive regulation of arachidonic acid secretion  negative regulation of cell aging  negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator  positive regulation of chemokine (C-X-C motif) ligand 2 production  
Ontology : EGO-EBIprostaglandin biosynthetic process  negative regulation of mature B cell apoptotic process  dopachrome isomerase activity  receptor binding  cytokine activity  cytokine receptor binding  protein binding  extracellular region  extracellular space  cytoplasm  inflammatory response  cell surface receptor signaling pathway  cell aging  cell proliferation  cell surface  negative regulation of gene expression  positive regulation of protein kinase A signaling cascade  carboxylic acid metabolic process  DNA damage response, signal transduction by p53 class mediator  positive regulation of B cell proliferation  positive regulation of lipopolysaccharide-mediated signaling pathway  negative regulation of cellular protein metabolic process  negative regulation of myeloid cell apoptotic process  positive regulation of peptidyl-serine phosphorylation  chemoattractant activity  positive regulation of phosphorylation  regulation of macrophage activation  negative regulation of apoptotic process  positive regulation of MAP kinase activity  negative regulation of DNA damage response, signal transduction by p53 class mediator  innate immune response  positive regulation of fibroblast proliferation  phenylpyruvate tautomerase activity  positive regulation of cytokine secretion  positive regulation of peptidyl-tyrosine phosphorylation  positive chemotaxis  positive regulation of prostaglandin secretion involved in immune response  positive regulation of myeloid leukocyte cytokine production involved in immune response  protein homotrimerization  positive regulation of ERK1 and ERK2 cascade  negative regulation of cell cycle arrest  positive regulation of arachidonic acid secretion  negative regulation of cell aging  negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator  positive regulation of chemokine (C-X-C motif) ligand 2 production  
Pathways : KEGGTyrosine metabolism    Phenylalanine metabolism   
REACTOMEMIF
Protein Interaction DatabaseMIF
Wikipedia pathwaysMIF
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)MIF
SNP (GeneSNP Utah)MIF
SNP : HGBaseMIF
Genetic variants : HAPMAPMIF
1000_GenomesMIF 
Somatic Mutations in Cancer : COSMICMIF 
CONAN: Copy Number AnalysisMIF 
Mutations and Diseases : HGMDMIF
OMIM153620    604302   
GENETestsMIF
Disease Genetic AssociationMIF
Huge Navigator MIF [HugePedia]  MIF [HugeCancerGEM]
Genomic VariantsMIF  MIF [DGVbeta]
Exome VariantMIF
dbVarMIF
ClinVarMIF
snp3D : Map Gene to Disease4282
General knowledge
Homologs : HomoloGeneMIF
Homology/Alignments : Family Browser (UCSC)MIF
Phylogenetic Trees/Animal Genes : TreeFamMIF
Chemical/Protein Interactions : CTD4282
Chemical/Pharm GKB GenePA30819
Clinical trialMIF
Other databases
Probes
Litterature
PubMed415 Pubmed reference(s) in Entrez
CoreMineMIF
iHOPMIF

Bibliography

Molecular cloning of a cDNA encoding a human macrophage migration inhibitory factor.
Weiser WY, Temple PA, Witek-Giannotti JS, Remold HG, Clark SC, David JR.
Proc Natl Acad Sci U S A. 1989 Oct;86(19):7522-6.
PMID 2552447
 
Mutant p53 potentiates protein kinase C induction of vascular endothelial growth factor expression.
Kieser A, Weich HA, Brandner G, Marme D, Kolch W.
Oncogene. 1994 Mar;9(3):963-9.
PMID 8108142
 
The immunoregulatory mediator macrophage migration inhibitory factor (MIF) catalyzes a tautomerization reaction.
Rosengren E, Bucala R, Aman P, Jacobsson L, Odh G, Metz CN, Rorsman H.
Mol Med. 1996 Jan;2(1):143-9.
PMID 8900542
 
The subunit structure of human macrophage migration inhibitory factor: evidence for a trimer.
Sun HW, Swope M, Cinquina C, Bedarkar S, Bernhagen J, Bucala R, Lolis E.
Protein Eng. 1996 Aug;9(8):631-5.
PMID 8875640
 
Crystal structure of the macrophage migration inhibitory factor from rat liver.
Suzuki M, Sugimoto H, Nakagawa A, Tanaka I, Nishihira J, Sakai M.
Nat Struct Biol. 1996 Mar;3(3):259-66.
PMID 8605628
 
Cutting edge: role of macrophage migration inhibitory factor in inhibiting NK cell activity and preserving immune privilege.
Apte RS, Sinha D, Mayhew E, Wistow GJ, Niederkorn JY.
J Immunol. 1998 Jun 15;160(12):5693-6.
PMID 9637476
 
Expression of macrophage migration inhibitory factor in the human prostate.
Meyer-Siegler K, Fattor RA, Hudson PB.
Diagn Mol Pathol. 1998 Feb;7(1):44-50.
PMID 9646034
 
Involvement of macrophage migration inhibitory factor (MIF) in the mechanism of tumor cell growth.
Takahashi N, Nishihira J, Sato Y, Kondo M, Ogawa H, Ohshima T, Une Y, Todo S.
Mol Med. 1998 Nov;4(11):707-14.
PMID 9932108
 
High expression of macrophage migration inhibitory factor in human melanoma cells and its role in tumor cell growth and angiogenesis.
Shimizu T, Abe R, Nakamura H, Ohkawara A, Suzuki M, Nishihira J.
Biochem Biophys Res Commun. 1999 Nov 2;264(3):751-8.
PMID 10544003
 
Intracellular distribution of macrophage migration inhibitory factor predicts the prognosis of patients with adenocarcinoma of the lung.
Kamimura A, Kamachi M, Nishihira J, Ogura S, Isobe H, Dosaka-Akita H, Ogata A, Shindoh M, Ohbuchi T, Kawakami Y.
Cancer. 2000 Jul 15;89(2):334-41.
PMID 10918163
 
Tumor growth-promoting properties of macrophage migration inhibitory factor (MIF).
Mitchell RA, Bucala R.
Semin Cancer Biol. 2000 Oct;10(5):359-66. (REVIEW)
PMID 11100884
 
An antibody for macrophage migration inhibitory factor suppresses tumour growth and inhibits tumour-associated angiogenesis.
Ogawa H, Nishihira J, Sato Y, Kondo M, Takahashi N, Oshima T, Todo S.
Cytokine. 2000 Apr;12(4):309-14.
PMID 10805210
 
Human uveal melanoma cells produce macrophage migration-inhibitory factor to prevent lysis by NK cells.
Repp AC, Mayhew ES, Apte S, Niederkorn JY.
J Immunol. 2000 Jul 15;165(2):710-5.
PMID 10878343
 
The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44.
Morrison H, Sherman LS, Legg J, Banine F, Isacke C, Haipek CA, Gutmann DH, Ponta H, Herrlich P.
Genes Dev. 2001 Apr 15;15(8):968-80.
PMID 11316791
 
The tautomerase active site of macrophage migration inhibitory factor is a potential target for discovery of novel anti-inflammatory agents.
Lubetsky JB, Dios A, Han J, Aljabari B, Ruzsicska B, Mitchell R, Lolis E, Al-Abed Y.
J Biol Chem. 2002 Jul 12;277(28):24976-82. Epub 2002 May 7.
PMID 11997397
 
Macrophage migration inhibitory factor evaluation compared with prostate specific antigen as a biomarker in patients with prostate carcinoma.
Meyer-Siegler KL, Bellino MA, Tannenbaum M.
Cancer. 2002 Mar 1;94(5):1449-56.
PMID 11920501
 
Macrophage migration inhibitory factor (MIF) expression in human glioblastomas correlates with vascular endothelial growth factor (VEGF) expression.
Munaut C, Boniver J, Foidart JM, Deprez M.
Neuropathol Appl Neurobiol. 2002 Dec;28(6):452-60.
PMID 12445161
 
Up-regulation of macrophage migration inhibitory factor gene and protein expression in glial tumor cells during hypoxic and hypoglycemic stress indicates a critical role for angiogenesis in glioblastoma multiforme.
Bacher M, Schrader J, Thompson N, Kuschela K, Gemsa D, Waeber G, Schlegel J.
Am J Pathol. 2003 Jan;162(1):11-7.
PMID 12507885
 
The p53-dependent effects of macrophage migration inhibitory factor revealed by gene targeting.
Fingerle-Rowson G, Petrenko O, Metz CN, Forsthuber TG, Mitchell R, Huss R, Moll U, Muller W, Bucala R.
Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9354-9. Epub 2003 Jul 23.
PMID 12878730
 
Prognostic values of galectin-3 and the macrophage migration inhibitory factor (MIF) in human colorectal cancers.
Legendre H, Decaestecker C, Nagy N, Hendlisz A, Schuring MP, Salmon I, Gabius HJ, Pector JC, Kiss R.
Mod Pathol. 2003 May;16(5):491-504.
PMID 12748256
 
MIF signal transduction initiated by binding to CD74.
Leng L, Metz CN, Fang Y, Xu J, Donnelly S, Baugh J, Delohery T, Chen Y, Mitchell RA, Bucala R.
J Exp Med. 2003 Jun 2;197(11):1467-76.
PMID 12782713
 
Macrophage migration inhibitory factor: roles in regulating tumor cell migration and expression of angiogenic factors in hepatocellular carcinoma.
Ren Y, Tsui HT, Poon RT, Ng IO, Li Z, Chen Y, Jiang G, Lau C, Yu WC, Bacher M, Fan ST.
Int J Cancer. 2003 Oct 20;107(1):22-9.
PMID 12925952
 
Overexpression of macrophage migration inhibitory factor induces angiogenesis and deteriorates prognosis after radical resection for hepatocellular carcinoma.
Hira E, Ono T, Dhar DK, El-Assal ON, Hishikawa Y, Yamanoi A, Nagasue N.
Cancer. 2005 Feb 1;103(3):588-98.
PMID 15612021
 
Macrophage migration inhibitory factor promotes tumor invasion and metastasis via the Rho-dependent pathway.
Sun B, Nishihira J, Yoshiki T, Kondo M, Sato Y, Sasaki F, Todo S.
Clin Cancer Res. 2005 Feb 1;11(3):1050-8.
PMID 15709171
 
Macrophage migration inhibitory factor promotes intestinal tumorigenesis.
Wilson JM, Coletta PL, Cuthbert RJ, Scott N, MacLennan K, Hawcroft G, Leng L, Lubetsky JB, Jin KK, Lolis E, Medina F, Brieva JA, Poulsom R, Markham AF, Bucala R, Hull MA.
Gastroenterology. 2005 Nov;129(5):1485-503.
PMID 16285950
 
Inhibition of macrophage migration inhibitory factor or its receptor (CD74) attenuates growth and invasion of DU-145 prostate cancer cells.
Meyer-Siegler KL, Iczkowski KA, Leng L, Bucala R, Vera PL.
J Immunol. 2006 Dec 15;177(12):8730-9.
PMID 17142775
 
Regulation of human lung adenocarcinoma cell migration and invasion by macrophage migration inhibitory factor.
Rendon BE, Roger T, Teneng I, Zhao M, Al-Abed Y, Calandra T, Mitchell RA.
J Biol Chem. 2007 Oct 12;282(41):29910-8. Epub 2007 Aug 20.
PMID 17709373
 
The role of macrophage inhibitory factor in tumorigenesis and central nervous system tumors.
Bach JP, Deuster O, Balzer-Geldsetzer M, Meyer B, Dodel R, Bacher M.
Cancer. 2009 May 15;115(10):2031-40. (REVIEW)
PMID 19326434
 
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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Contributor(s)

Written06-2010Jan-Philipp Bach, Michael Bacher, Richard Dodel
Department of Neurology, Philipps-University Marburg, Rudolf-Bultmann-Strasse 8, 35039 Marburg, Germany

Citation

This paper should be referenced as such :
Bach JP, Bacher M, Dodel R . MIF (macrophage migration inhibitory factor (glycosylation-inhibiting factor)). Atlas Genet Cytogenet Oncol Haematol. June 2010 .
URL : http://AtlasGeneticsOncology.org/Genes/MIFID41365ch22q11.html

The various updated versions of this paper are referenced and archived by INIST as such :
http://documents.irevues.inist.fr/bitstream/2042/44983/1/06-2010-MIFID41365ch22q11.pdf   [ Bibliographic record ]

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indexed on : Fri Apr 18 17:17:34 CEST 2014

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