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What is Melanostatin DM?

Melanostatin DM, also known as melanotropin release-inhibiting factor (MIF or MRIF) is a peptide that inhibits the release of melanotropin and melanosin from the pituitary gland and other cells by binding to a specific membrane-associated receptor. Melanotropin is the naturally occurring ligand for the MIF receptor. MIF was first identified in the media of the T hybridoma MIF I and later confirmed in the supernatants of B16 melanoma and other tumor cell lines by a series of biophysical and biochemical assays that characterized it as a novel cytokine.

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In the body, MIF has the function of an inflammatory cytokine (1-4) and is produced in many cell types such as activated macrophages, activated lymphocytes, activated mast cells, activated osteoclasts, activated endothelial cells, activated glial cells, activated keratinocytes and activated platelets. Some of these cells produce MIF constitutively or after stimulation. Most of these cells produce MIF at low concentrations. An increasing number of cells release MIF after activation.

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MIF is not related to the ciliary neurotrophic factor (CNTF), interleukin 1 (IL1), tumor necrosis factor (TNF) or interleukin 4 (IL4), which are also known as neurotrophic factors, proinflammatory cytokines, or TH2 lymphocyte cytokines. MIF is closely related to interleukin 1 beta (IL1β) and interleukin 6 (IL6) in terms of amino acid sequence and biochemical activity. Unlike IL1, MIF is a broad-acting immunostimulant. MIF is also closely related to interleukin 2 (IL2) (14) and a number of hematopoietic cytokines including tumor necrosis factor-α (TNF-α).

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MIF is a multifunctional cytokine that belongs to the interleukin-1 cytokine family. MIF is widely distributed in cells and body fluids such as tears, saliva, cerebrospinal fluid, blood, serum, and urine. When human leukocytes are activated by various stimulants, MIF is secreted by the leukocytes. For instance, when blood cells such as leukocytes, monocytes, macrophages, and polymorphonuclear leukocytes (neutrophils, eosinophils, and basophils) are activated, MIF is released from the cells.


The secretion of MIF from neutrophils and monocytes after stimulation with endotoxin or N-formyl-methionyl-leucyl-phenylalanine is also reported in the literature. Studies show that MIF is expressed in monocytes, monocyte-derived macrophages, neutrophils, eosinophils, and NK cells.

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Studies also demonstrate that the secretion of MIF is associated with many immune and inflammatory disorders, including various infectious diseases, inflammatory conditions, cancer, immunological disorders, transplant rejection, bone diseases, and neurological diseases. The effects of MIF on inflammatory conditions and tumor cells also include cell proliferation, angiogenesis, cell migration and invasion, adhesion, and metastasis.

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A number of studies on the effects of MIF on immune and inflammatory disorders, tumor cells, inflammatory diseases, and other conditions have been published (33-37). For example, it is reported that the production of MIF is increased in patients with systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA). Furthermore, patients with autoimmune diabetes mellitus (DM) have increased levels of MIF. It has also been reported that MIF levels are increased in sera and synovial fluid of patients with juvenile RA and that the serum level of MIF is significantly higher in a group of patients with RA than in a healthy control group.


It has also been reported that administration of a neutralizing antibody to MIF prevents joint erosion in collagen-induced arthritis (CIA) mice and that administration of a recombinant adenovirus containing an antisense RNA against MIF inhibits synovial hyperplasia in rats with adjuvant arthritis. It is also reported that injection of MIF into the joints of arthritis-susceptible mice induces joint swelling.


MIF has been reported to play a role in various aspects of chronic pain and to modulate the sensitivity of nociceptive neurons. It is also reported that inhibition of MIF synthesis may be useful for treating inflammatory and neuropathic pain.

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It is also reported that administration of anti-MIF antibody reduces the severity of skin lesions and decreases the incidence of lung metastasis in an experiment in which an adenocarcinoma is transferred into the footpad of mice.

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It is further reported that MIF induces the expression of matrix metalloproteinases (MMPs) in cultured human prostate cells and that MIF is a potent mitogen for prostate cells. It is also reported that IL-1α, IL-1β, IL-4, IL-6, IL-10, TNF-α, and interferon-γ (IFN-γ) increase the production of MIF by primary cultures of monocytes. Furthermore, MIF stimulates the secretion of VEGF by retinal epithelial cells.

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It is further reported that MIF causes proliferation of cells (e.g. B16 melanoma cells) and angiogenesis and regulates the migration and invasion of cancer cells. It is also reported that MIF enhances cell adhesion of human colon cancer cells, fibrosarcoma cells, and gastric cancer cells. Studies report that MIF stimulates metastasis in experimental models of breast and colon cancer. It is also reported that MIF suppresses tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in A375 melanoma cells.

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