Macrophage migration inhibitory factor

Last updated
MIF
Protein MIF PDB 1ca7.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases MIF , GIF, GLIF, Mmacrophage migration inhibitory factor (glycosylation-inhibiting factor), macrophage migration inhibitory factor
External IDs OMIM: 153620 MGI: 96982 HomoloGene: 55655 GeneCards: MIF
EC number 5.3.3.12
Orthologs
SpeciesHumanMouse
Entrez

4282

17319

Ensembl

ENSG00000276701
ENSG00000240972

ENSMUSG00000033307

UniProt

P14174

P34884

RefSeq (mRNA)

NM_002415

NM_010798

RefSeq (protein)

NP_002406
NP_002406.1

NP_034928

Location (UCSC) Chr 22: 23.89 – 23.9 Mb Chr 10: 75.7 – 75.7 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse
Macrophage migration inhibitory factor (MIF)
Identifiers
SymbolMIF
Pfam PF01187
InterPro IPR001398
PROSITE PDOC00892
SCOP2 1mif / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Macrophage migration inhibitory factor (MIF), also known as glycosylation-inhibiting factor (GIF), L-dopachrome isomerase, or phenylpyruvate tautomerase is a protein that in humans is encoded by the MIF gene. [5] [6] MIF is an important regulator of innate immunity. [7] The MIF protein superfamily also includes a second member with functionally related properties, the D-dopachrome tautomerase (D-DT). [8] CD74 is a surface receptor for MIF. [9]

Bacterial antigens stimulate white blood cells to release MIF into the blood stream. [10] The circulating MIF binds to CD74 on other immune cells to trigger an acute immune response. Hence, MIF is classified as an inflammatory cytokine. Furthermore, glucocorticoids also stimulate white blood cells to release MIF and hence MIF partially counteracts the inhibitory effects that glucocorticoids have on the immune system. Finally trauma activates the anterior pituitary gland to release MIF. [11]

Structure

Macrophage migration inhibitory factor assembles into a trimer composed of three identical subunits. Each of these monomers contain two antiparallel alpha helices and a four-stranded beta sheet. The monomers surround a central channel with 3-fold rotational symmetry. [12] [13]

Response to injury

Cytokines play an important role in promoting wound healing and tissue repair. Cell injury results in MIF release which then interacts with CD74. MIF-CD74 signaling activates pro-survival and proliferative pathways that protects the host during injury. [14]

Enzymatic activity

MIF contains two motifs with catalytic activity. The first is a 27 amino acid motif located at the N-terminus functions as a phenylpyruvate tautomerase that can catalyze the conversion of 2-carboxy-2,3-dihydroindole-5,6-quinone (dopachrome) into 5,6-dihydroxyindole-2-carboxylic acid (DHICA). [15] [16] MIF also contains a Cys-Ala-Leu-Cys catalytic site between residues 57 and 60 that appears to function as a disulfide reductase. [17]

Function

This gene encodes a lymphokine involved in cell-mediated immunity, immunoregulation, and inflammation. [18] [19] [20] MIF plays a role in the regulation of macrophage function in host defense through the suppression of anti-inflammatory effects of glucocorticoids. [20] [21] [22] This lymphokine and the JAB1 protein form a complex in the cytosol near the peripheral plasma membrane, which may indicate a role in integrin signaling pathways. [23]

Mechanism of action

MIF binds to CD74, [24] inducing its phosphorylation and the recruitment of CD44 which then activates non-receptor tyrosine kinases, leading ultimately to extracellular signal-regulated kinase phosphorylation. [25] In addition to ERK, stimulation of CD74 activates other signaling pathways such PI3K-Akt, NF-κB, and AMP-activated protein kinase (AMPK) pathways. [26]

Interactions

Macrophage migration inhibitory factor has been reported to interact with:

Clinical significance

MIF is a potential drug target for sepsis, rheumatoid arthritis, and cancer. [40] [41]

Parasite-produced MIF homologs

Parasite-Produced MIF Cytokine in Immune Evasion, Invasion, and Pathogenesis Parasite-Produced MIF Cytokine in Immune Evasion, Invasion, and Pathogenesis.jpg
Parasite-Produced MIF Cytokine in Immune Evasion, Invasion, and Pathogenesis

Multiple protozoan parasites produce homologs MIF that have similar inflammatory functions to human MIF, and play a role in their pathogenesis, invasion and immune evasion. [42] [43] A preclinical study showed that blocking parasite MIF improves outcome in severe protozoan infections. [44] Examples of protozoans with MIF homologs that have been reported:

Related Research Articles

<span class="mw-page-title-main">Inflammation</span> Physical effects resulting from activation of the immune system

Inflammation is part of the biological response of body tissues to harmful stimuli, such as pathogens, damaged cells, or irritants. The five cardinal signs are heat, pain, redness, swelling, and loss of function.

<span class="mw-page-title-main">Cytokine</span> Broad and loose category of small proteins important in cell signaling

Cytokines are a broad and loose category of small proteins important in cell signaling. Due to their size, cytokines cannot cross the lipid bilayer of cells to enter the cytoplasm and therefore typically exert their functions by interacting with specific cytokine receptors on the target cell surface. Cytokines have been shown to be involved in autocrine, paracrine and endocrine signaling as immunomodulating agents.

<span class="mw-page-title-main">Tumor necrosis factor</span> Protein

Tumor necrosis factor is an adipokine and a cytokine. TNF is a member of the TNF superfamily, which consists of various transmembrane proteins with a homologous TNF domain.

<span class="mw-page-title-main">Chemokine</span> Small cytokines or signaling proteins secreted by cells

Chemokines, or chemotactic cytokines, are a family of small cytokines or signaling proteins secreted by cells that induce directional movement of leukocytes, as well as other cell types, including endothelial and epithelial cells. In addition to playing a major role in the activation of host immune responses, chemokines are important for biological processes, including morphogenesis and wound healing, as well as in the pathogenesis of diseases like cancers.

Pattern recognition receptors (PRRs) play a crucial role in the proper function of the innate immune system. PRRs are germline-encoded host sensors, which detect molecules typical for the pathogens. They are proteins expressed mainly by cells of the innate immune system, such as dendritic cells, macrophages, monocytes, neutrophils, as well as by epithelial cells, to identify two classes of molecules: pathogen-associated molecular patterns (PAMPs), which are associated with microbial pathogens, and damage-associated molecular patterns (DAMPs), which are associated with components of host's cells that are released during cell damage or death. They are also called primitive pattern recognition receptors because they evolved before other parts of the immune system, particularly before adaptive immunity. PRRs also mediate the initiation of antigen-specific adaptive immune response and release of inflammatory cytokines.

<span class="mw-page-title-main">Interferon gamma</span> InterPro Family

Interferon gamma (IFN-γ) is a dimerized soluble cytokine that is the only member of the type II class of interferons. The existence of this interferon, which early in its history was known as immune interferon, was described by E. F. Wheelock as a product of human leukocytes stimulated with phytohemagglutinin, and by others as a product of antigen-stimulated lymphocytes. It was also shown to be produced in human lymphocytes. or tuberculin-sensitized mouse peritoneal lymphocytes challenged with Mantoux test (PPD); the resulting supernatants were shown to inhibit growth of vesicular stomatitis virus. Those reports also contained the basic observation underlying the now widely employed IFN-γ release assay used to test for tuberculosis. In humans, the IFN-γ protein is encoded by the IFNG gene.

<span class="mw-page-title-main">Interleukin 8</span> Mammalian protein found in Homo sapiens

Interleukin 8 is a chemokine produced by macrophages and other cell types such as epithelial cells, airway smooth muscle cells and endothelial cells. Endothelial cells store IL-8 in their storage vesicles, the Weibel-Palade bodies. In humans, the interleukin-8 protein is encoded by the CXCL8 gene. IL-8 is initially produced as a precursor peptide of 99 amino acids which then undergoes cleavage to create several active IL-8 isoforms. In culture, a 72 amino acid peptide is the major form secreted by macrophages.

<span class="mw-page-title-main">Macrophage inflammatory protein</span> Protein family

Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1α and MIP-1β, renamed CCL3 and CCL4 respectively, since 2000. However, other names are sometimes encountered in older literature, such as LD78α, AT 464.1 and GOS19-1 for human CCL3 and AT 744, Act-2, LAG-1, HC21 and G-26 for human CCL4. Other macrophage inflammatory proteins include MIP-2, MIP-3 and MIP-5.

<span class="mw-page-title-main">Interleukin 22</span> Protein, encoded in humans by IL22 gene

Interleukin-22 (IL-22) is protein that in humans is encoded by the IL22 gene.

<span class="mw-page-title-main">Interleukin 19</span> Protein-coding gene in the species Homo sapiens

Interleukin 19 (IL-19) is an immunosuppressive protein that belongs to the IL-10 cytokine subfamily.

Chemokine ligands 4 previously known as macrophage inflammatory protein (MIP-1β), is a protein which in humans is encoded by the CCL4 gene. CCL4 belongs to a cluster of genes located on 17q11-q21 of the chromosomal region. Identification and localization of the gene on the chromosome 17 was in 1990 although the discovery of MIP-1 was initiated in 1988 with the purification of a protein doublet corresponding to inflammatory activity from supernatant of endotoxin-stimulated murine macrophages. At that time, it was also named as "macrophage inflammatory protein-1" (MIP-1) due to its inflammatory properties.

<span class="mw-page-title-main">CXCL1</span> Mammalian protein found in Homo sapiens

The chemokine ligand 1 (CXCL1) is a small peptide belonging to the CXC chemokine family that acts as a chemoattractant for several immune cells, especially neutrophils or other non-hematopoietic cells to the site of injury or infection and plays an important role in regulation of immune and inflammatory responses. It was previously called GRO1 oncogene, GROα, neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MGSA-α). CXCL1 was first cloned from a cDNA library of genes induced by platelet-derived growth factor (PDGF) stimulation of BALB/c-3T3 murine embryonic fibroblasts and named "KC" for its location in the nitrocellulose colony hybridization assay. This designation is sometimes erroneously believed to be an acronym and defined as "keratinocytes-derived chemokine". Rat CXCL1 was first reported when NRK-52E cells were stimulated with interleukin-1β (IL-1β) and lipopolysaccharide (LPS) to generate a cytokine that was chemotactic for rat neutrophils, cytokine-induced neutrophil chemoattractant (CINC). In humans, this protein is encoded by the gene Cxcl1 and is located on human chromosome 4 among genes for other CXC chemokines.

<span class="mw-page-title-main">Toll-like receptor 4</span> Protein-coding gene in the species Homo sapiens

Toll-like receptor 4 (TLR4), also designated as CD284, is a key activator of the innate immune response and plays a central role in the fight against bacterial infections. TLR4 is a transmembrane protein of approximately 95 kDa that is encoded by the TLR4 gene.

<span class="mw-page-title-main">CD74</span> Mammalian protein found in Homo sapiens

HLA class II histocompatibility antigen gamma chain also known as HLA-DR antigens-associated invariant chain or CD74, is a protein that in humans is encoded by the CD74 gene. The invariant chain is a polypeptide which plays a critical role in antigen presentation. It is involved in the formation and transport of MHC class II peptide complexes for the generation of CD4+ T cell responses. The cell surface form of the invariant chain is known as CD74. CD74 is a cell surface receptor for the cytokine macrophage migration inhibitory factor (MIF).

<span class="mw-page-title-main">COP9 constitutive photomorphogenic homolog subunit 5</span> Protein-coding gene in the species Homo sapiens

COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis), also known as COPS5 or Csn5, is a gene conserved from humans to Saccharomyces cerevisiae.

<span class="mw-page-title-main">Peptidoglycan recognition protein 1</span> Protein-coding gene in the species Homo sapiens

Peptidoglycan recognition protein 1, PGLYRP1, also known as TAG7, is an antibacterial and pro-inflammatory innate immunity protein that in humans is encoded by the PGLYRP1 gene.

An inflammatory cytokine or proinflammatory cytokine is a type of signaling molecule that is secreted from immune cells like helper T cells (Th) and macrophages, and certain other cell types that promote inflammation. They include interleukin-1 (IL-1), IL-6, IL-12, and IL-18, tumor necrosis factor alpha (TNF-α), interferon gamma (IFNγ), and granulocyte-macrophage colony stimulating factor (GM-CSF) and play an important role in mediating the innate immune response. Inflammatory cytokines are predominantly produced by and involved in the upregulation of inflammatory reactions.

<span class="mw-page-title-main">Interleukin-1 family</span> Group of cytokines playing a key role in the regulation of immune and inflammatory responses

The Interleukin-1 family is a group of 11 cytokines that plays a central role in the regulation of immune and inflammatory responses to infections or sterile insults.

Chemorepulsion is the directional movement of a cell away from a substance. Of the two directional varieties of chemotaxis, chemoattraction has been studied to a much greater extent. Only recently have the key components of the chemorepulsive pathway been elucidated. The exact mechanism is still being investigated, and its constituents are currently being explored as likely candidates for immunotherapies.

<span class="mw-page-title-main">Macrophage migration inhibitory factor domain</span>

Macrophage migration inhibitory factor domain is an evolutionary conserved protein domain.

References

  1. 1 2 3 ENSG00000240972 GRCh38: Ensembl release 89: ENSG00000276701, ENSG00000240972 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033307 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Weiser WY, Temple PA, Witek-Giannotti JS, Remold HG, Clark SC, David JR (October 1989). "Molecular cloning of a cDNA encoding a human macrophage migration inhibitory factor". Proceedings of the National Academy of Sciences of the United States of America. 86 (19): 7522–6. Bibcode:1989PNAS...86.7522W. doi: 10.1073/pnas.86.19.7522 . PMC   298097 . PMID   2552447.
  6. ↑ Kozak CA, Adamson MC, Buckler CE, Segovia L, Paralkar V, Wistow G (June 1995). "Genomic cloning of mouse MIF (macrophage inhibitory factor) and genetic mapping of the human and mouse expressed gene and nine mouse pseudogenes". Genomics. 27 (3): 405–11. doi:10.1006/geno.1995.1070. PMID   7558020.
  7. ↑ Calandra T, Roger T (October 2003). "Macrophage migration inhibitory factor: a regulator of innate immunity". Nature Reviews. Immunology. 3 (10): 791–800. doi:10.1038/nri1200. PMC   7097468 . PMID   14502271.
  8. ↑ Günther S, Fagone P, Jalce G, Atanasov AG, Guignabert C, Nicoletti F (February 2019). "Role of MIF and D-DT in immune-inflammatory, autoimmune, and chronic respiratory diseases: from pathogenic factors to therapeutic targets". Drug Discovery Today. 24 (2): 428–439. doi:10.1016/j.drudis.2018.11.003. PMID   30439447. S2CID   53562815.
  9. ↑ Farr L, Ghosh S, Moonah S (2020). "Role of MIF Cytokine/CD74 Receptor Pathway in Protecting Against Injury and Promoting Repair". Frontiers in Immunology. 11: 1273. doi: 10.3389/fimmu.2020.01273 . PMC   7325688 . PMID   32655566.
  10. ↑ Barret, James (1980). Basic Immunology and its Medical Application (2 ed.). St.Louis: The C.V. Mosby Company. ISBN   978-0-8016-0495-9.
  11. ↑ Larson DF, Horak K (2006). "Macrophage migration inhibitory factor: controller of systemic inflammation". Critical Care. 10 (2): 138. doi: 10.1186/cc4899 . PMC   1550887 . PMID   16677407.
  12. ↑ Sun HW, Bernhagen J, Bucala R, Lolis E (May 1996). "Crystal structure at 2.6-A resolution of human macrophage migration inhibitory factor". Proceedings of the National Academy of Sciences of the United States of America. 93 (11): 5191–6. doi: 10.1073/pnas.93.11.5191 . PMC   39220 . PMID   8643551.
  13. ↑ Al-Abed Y, VanPatten S (January 2011). "MIF as a disease target: ISO-1 as a proof-of-concept therapeutic". Future Medicinal Chemistry. 3 (1): 45–63. doi:10.4155/fmc.10.281. PMID   21428825.
  14. ↑ Farr L, Ghosh S, Moonah S (2020). "Role of MIF Cytokine/CD74 Receptor Pathway in Protecting Against Injury and Promoting Repair". Frontiers in Immunology. 11: 1273. doi: 10.3389/fimmu.2020.01273 . PMC   7325688 . PMID   32655566.
  15. ↑ Rosengren E, Bucala R, Aman P, Jacobsson L, Odh G, Metz CN, Rorsman H (January 1996). "The immunoregulatory mediator macrophage migration inhibitory factor (MIF) catalyzes a tautomerization reaction". Molecular Medicine. 2 (1): 143–9. doi:10.1007/BF03402210. PMC   2230029 . PMID   8900542.
  16. ↑ Veillat V, Carli C, Metz CN, Al-Abed Y, Naccache PH, Akoum A (December 2010). "Macrophage migration inhibitory factor elicits an angiogenic phenotype in human ectopic endometrial cells and triggers the production of major angiogenic factors via CD44, CD74, and MAPK signaling pathways". The Journal of Clinical Endocrinology and Metabolism. 95 (12): E403-12. doi: 10.1210/jc.2010-0417 . PMID   20829186.
  17. ↑ Thiele M, Bernhagen J (2005). "Link between macrophage migration inhibitory factor and cellular redox regulation". Antioxidants & Redox Signaling. 7 (9–10): 1234–48. doi:10.1089/ars.2005.7.1234. PMID   16115028.
  18. ↑ Leng L, Bucala R (February 2006). "Insight into the biology of macrophage migration inhibitory factor (MIF) revealed by the cloning of its cell surface receptor". Cell Research. 16 (2): 162–8. doi: 10.1038/sj.cr.7310022 . PMID   16474429.
  19. ↑ Chen PF, Luo YL, Wang W, Wang JX, Lai WY, Hu SM, et al. (2010). "ISO-1, a macrophage migration inhibitory factor antagonist, inhibits airway remodeling in a murine model of chronic asthma". Molecular Medicine. 16 (9–10): 400–8. doi:10.2119/molmed.2009.00128. PMC   2935952 . PMID   20485865.
  20. 1 2 Takahashi K, Koga K, Linge HM, Zhang Y, Lin X, Metz CN, et al. (May 2009). "Macrophage CD74 contributes to MIF-induced pulmonary inflammation". Respiratory Research. 10 (1): 33. doi: 10.1186/1465-9921-10-33 . PMC   2681459 . PMID   19413900.
  21. ↑ Flaster H, Bernhagen J, Calandra T, Bucala R (June 2007). "The macrophage migration inhibitory factor-glucocorticoid dyad: regulation of inflammation and immunity". Molecular Endocrinology. 21 (6): 1267–80. doi: 10.1210/me.2007-0065 . PMID   17389748.
  22. ↑ Al-Abed Y, Metz CN, Cheng KF, Aljabari B, VanPatten S, Blau S, et al. (May 2011). "Thyroxine is a potential endogenous antagonist of macrophage migration inhibitory factor (MIF) activity". Proceedings of the National Academy of Sciences of the United States of America. 108 (20): 8224–7. Bibcode:2011PNAS..108.8224A. doi: 10.1073/pnas.1017624108 . PMC   3100930 . PMID   21536912.
  23. ↑ "Entrez Gene: MIF macrophage migration inhibitory factor (glycosylation-inhibiting factor)".
  24. ↑ Bernhagen J, Calandra T, Mitchell RA, Martin SB, Tracey KJ, Voelter W, et al. (October 1993). "MIF is a pituitary-derived cytokine that potentiates lethal endotoxaemia". Nature. 365 (6448): 756–9. Bibcode:1993Natur.365..756B. doi:10.1038/365756a0. PMID   8413654. S2CID   4321353.
  25. ↑ Shi X, Leng L, Wang T, Wang W, Du X, Li J, et al. (October 2006). "CD44 is the signaling component of the macrophage migration inhibitory factor-CD74 receptor complex". Immunity. 25 (4): 595–606. doi:10.1016/j.immuni.2006.08.020. PMC   3707630 . PMID   17045821.
  26. ↑ Farr L, Ghosh S, Moonah S (2020). "Role of MIF Cytokine/CD74 Receptor Pathway in Protecting Against Injury and Promoting Repair". Frontiers in Immunology. 11: 1273. doi: 10.3389/fimmu.2020.01273 . PMC   7325688 . PMID   32655566.
  27. ↑ Shen L, Hu J, Lu H, Wu M, Qin W, Wan D, et al. (April 2003). "The apoptosis-associated protein BNIPL interacts with two cell proliferation-related proteins, MIF and GFER". FEBS Letters. 540 (1–3): 86–90. doi: 10.1016/S0014-5793(03)00229-1 . PMID   12681488.
  28. ↑ Farr L, Ghosh S, Jiang N, Watanabe K, Parlak M, Bucala R, Moonah S (2020). "CD74 Signaling Links Inflammation to Intestinal Epithelial Cell Regeneration and Promotes Mucosal Healing". Cellular and Molecular Gastroenterology and Hepatology. 10 (1): 101–112. doi:10.1016/j.jcmgh.2020.01.009. PMC   7215244 . PMID   32004754.
  29. ↑ Leng L, Metz CN, Fang Y, Xu J, Donnelly S, Baugh J, et al. (June 2003). "MIF signal transduction initiated by binding to CD74". The Journal of Experimental Medicine. 197 (11): 1467–76. doi:10.1084/jem.20030286. PMC   2193907 . PMID   12782713.
  30. ↑ Bacher M, Deuster O, Aljabari B, Egensperger R, Neff F, Jessen F, et al. (March 2010). "The role of macrophage migration inhibitory factor in Alzheimer's disease". Molecular Medicine. 16 (3–4): 116–21. doi:10.2119/molmed.2009.00123. PMC   2829616 . PMID   20200619.
  31. ↑ Shan ZX, Lin QX, Deng CY, Tan HH, Kuang SJ, Xiao DZ, et al. (December 2009). "[Identification of the interactions between the truncated fragments of macrophage migration inhibitory factor and CD74 using a yeast two-hybrid system]". Nan Fang Yi Ke da Xue Xue Bao = Journal of Southern Medical University (in Chinese). 29 (12): 2383–6, 2390. PMID   20034881.
  32. ↑ Wang F, Shen X, Guo X, Peng Y, Liu Y, Xu S, Yang J (February 2010). "Spinal macrophage migration inhibitory factor contributes to the pathogenesis of inflammatory hyperalgesia in rats". Pain. 148 (2): 275–83. doi:10.1016/j.pain.2009.11.011. PMID   20005040. S2CID   38141283.
  33. ↑ Dobson SE, Augustijn KD, Brannigan JA, Schnick C, Janse CJ, Dodson EJ, et al. (December 2009). "The crystal structures of macrophage migration inhibitory factor from Plasmodium falciparum and Plasmodium berghei". Protein Science. 18 (12): 2578–91. doi:10.1002/pro.263. PMC   2798171 . PMID   19827093.
  34. ↑ Ghosh S, Leaton LA, Farr L, Barfield A, Moonah S (July 2018). "Interaction between parasite-encoded JAB1/CSN5 and macrophage migration inhibitory factor proteins attenuates its proinflammatory function". Scientific Reports. 8 (1): 10241. Bibcode:2018NatSR...810241G. doi:10.1038/s41598-018-28625-1. PMC   6035221 . PMID   29980718.
  35. ↑ Kleemann R, Hausser A, Geiger G, Mischke R, Burger-Kentischer A, Flieger O, et al. (November 2000). "Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1". Nature. 408 (6809): 211–6. Bibcode:2000Natur.408..211K. doi:10.1038/35041591. PMID   11089976. S2CID   205010648.
  36. ↑ Schwartz V, Lue H, Kraemer S, Korbiel J, Krohn R, Ohl K, et al. (September 2009). "A functional heteromeric MIF receptor formed by CD74 and CXCR4". FEBS Letters. 583 (17): 2749–57. doi:10.1016/j.febslet.2009.07.058. PMC   2911026 . PMID   19665027.
  37. ↑ Schrader J, Deuster O, Rinn B, Schulz M, Kautz A, Dodel R, et al. (December 2009). "Restoration of contact inhibition in human glioblastoma cell lines after MIF knockdown". BMC Cancer. 9: 464. doi: 10.1186/1471-2407-9-464 . PMC   2810303 . PMID   20038293.
  38. ↑ Stosic-Grujicic S, Stojanovic I, Maksimovic-Ivanic D, Momcilovic M, Popadic D, Harhaji L, et al. (June 2008). "Macrophage migration inhibitory factor (MIF) is necessary for progression of autoimmune diabetes mellitus". Journal of Cellular Physiology. 215 (3): 665–75. doi:10.1002/jcp.21346. PMID   18064633. S2CID   36047003.
  39. ↑ Filip AM, Klug J, Cayli S, Fröhlich S, Henke T, Lacher P, et al. (March 2009). "Ribosomal protein S19 interacts with macrophage migration inhibitory factor and attenuates its pro-inflammatory function". The Journal of Biological Chemistry. 284 (12): 7977–85. doi: 10.1074/jbc.M808620200 . PMC   2658091 . PMID   19155217.
  40. ↑ Lue H, Kleemann R, Calandra T, Roger T, Bernhagen J (April 2002). "Macrophage migration inhibitory factor (MIF): mechanisms of action and role in disease". Microbes and Infection. 4 (4): 449–60. doi:10.1016/S1286-4579(02)01560-5. PMID   11932196.
  41. ↑ Bloom J, Sun S, Al-Abed Y (December 2016). "MIF, a controversial cytokine: a review of structural features, challenges, and opportunities for drug development". Expert Opinion on Therapeutic Targets. 20 (12): 1463–1475. doi:10.1080/14728222.2016.1251582. PMID   27762152. S2CID   36752674.
  42. ↑ Ghosh S, Jiang N, Farr L, Ngobeni R, Moonah S (21 August 2019). "Parasite-Produced MIF Cytokine: Role in Immune Evasion, Invasion, and Pathogenesis". Frontiers in Immunology. 10: 1995. doi: 10.3389/fimmu.2019.01995 . PMC   6712082 . PMID   31497025.
  43. ↑ Bennett JE, Dolin R, Blaser MJ (2014). Principles and Practice of Infectious Diseases. Elsevier Health Sciences. p. 32. ISBN   9781455748013.
  44. ↑ Ghosh S, Padalia J, Ngobeni R, Abendroth J, Farr L, Shirley DA, et al. (March 2020). "Targeting Parasite-Produced Macrophage Migration Inhibitory Factor as an Antivirulence Strategy With Antibiotic-Antibody Combination to Reduce Tissue Damage". The Journal of Infectious Diseases. 221 (7): 1185–1193. doi: 10.1093/infdis/jiz579 . PMC   7325720 . PMID   31677380.
  45. ↑ Ngobeni R, Abhyankar MM, Jiang NM, Farr LA, Samie A, Haque R, Moonah SN (April 2017). "Entamoeba histolytica-Encoded Homolog of Macrophage Migration Inhibitory Factor Contributes to Mucosal Inflammation during Amebic Colitis". The Journal of Infectious Diseases. 215 (8): 1294–1302. doi:10.1093/infdis/jix076. PMC   5853319 . PMID   28186296.
  46. ↑ Sun T, Holowka T, Song Y, Zierow S, Leng L, Chen Y, et al. (July 2012). "A Plasmodium-encoded cytokine suppresses T-cell immunity during malaria". Proceedings of the National Academy of Sciences of the United States of America. 109 (31): E2117-26. doi: 10.1073/pnas.1206573109 . PMC   3411961 . PMID   22778413.
  47. ↑ Sommerville C, Richardson JM, Williams RA, Mottram JC, Roberts CW, Alexander J, Henriquez FL (May 2013). "Biochemical and immunological characterization of Toxoplasma gondii macrophage migration inhibitory factor". The Journal of Biological Chemistry. 288 (18): 12733–41. doi: 10.1074/jbc.M112.419911 . PMC   3642319 . PMID   23443656.
  48. ↑ Holowka T, Castilho TM, Garcia AB, Sun T, McMahon-Pratt D, Bucala R (June 2016). "Leishmania-encoded orthologs of macrophage migration inhibitory factor regulate host immunity to promote parasite persistence". FASEB Journal. 30 (6): 2249–65. doi: 10.1096/fj.201500189R . PMC   4871794 . PMID   26956417.
  49. ↑ Twu O, Dessí D, Vu A, Mercer F, Stevens GC, de Miguel N, et al. (June 2014). "Trichomonas vaginalis homolog of macrophage migration inhibitory factor induces prostate cell growth, invasiveness, and inflammatory responses". Proceedings of the National Academy of Sciences of the United States of America. 111 (22): 8179–84. Bibcode:2014PNAS..111.8179T. doi: 10.1073/pnas.1321884111 . PMC   4050605 . PMID   24843155.

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