Macrophage migration inhibitory factor (MIF) is an immunoregulatory cytokine, the effect of which on arresting random immune cell movement was recognized several decades ago. Despite its historic name, MIF also has a direct chemokine-like function and promotes cell recruitment. MIF is a ubiquitously expressed protein that plays a crucial role in many inflammatory and autoimmune disorders. Increasing evidence suggests that MIF also controls metabolic and inflammatory processes underlying the development of metabolic pathologies associated with obesity. Further research has shown that MIF plays a particularly critical part in cell cycle regulation and therefore in tumorigenesis as well. The significance of the role of MIF in a variety of both solid and hematologic tumors has been established. More recently, interest has increased in the role of MIF in the development of the central nervous system (CNS) tumors, in which it appears to influence cell cycle control. MIF contributes to malignant disease progression on several different levels. Both circulating and intracellular MIF protein levels are elevated in cancer patients and MIF expression reportedly correlates with stage, metastatic spread, and disease-free survival. Blockade of MIF bioactivity successfully inhibited tumor cell growth in vivo and in vitro. MIF plays important role in the pathogenesis of gastrointestinal, hepatic, and pancreatic disorders.
Macrophage migration inhibitory factor (MIF) is an immunoregulatory cytokine, the effect of which on arresting random immune cell movement was recognized several decades ago. Despite its historic name, MIF also has a direct chemokine-like function and promotes cell recruitment. MIF is a ubiquitously expressed protein that plays a crucial role in many inflammatory and autoimmune disorders. Increasing evidence sμggests that MIF also controls metabolic and inflammatory processes underlying the development of metabolic pathologies associated with obesity. Further research has shown that MIF plays a particularly critical part in cell cycle regulation and therefore in tumorigenesis as well. The significance of the role of MIF in a variety of both solid and hematologic tumors has been established. More recently, interest has increased in the role of MIF in the development of the central nervous system (CNS) tumors, in which it appears to influence cell cycle control. MIF contributes to malignant disease progression on several different levels. Both circulating and intracellular MIF protein levels are elevated in cancer patients and MIF expression reportedly correlates with stage, metastatic spread, and disease-free survival. Blockade of MIF bioactivity successfully inhibited tumor cell growth in vivo and in vitro. MIF plays important role in the pathogenesis of gastrointestinal, hepatic, and pancreatic disorders.
Multiple Inositol Polyphosphate Phosphatase 1/MINPP1 is an enzyme that removes 3-phosphate from inositol phosphate substrates. MINPP1 also converts 2,3 bisphosphoglycerate (2,3-BPG) to 2-phosphoglycerate. MINPP1 is synthesized as a 487 amino acid precursor that contains an 30 amino acid signal peptide and a 457 amino aicd mature chain. MINPP1 is widely expressed with the highest levels found in kidney, liver and placenta. It acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). MINPP1 may play a role in bone development (endochondral ossification).
Mitochondrial Fission 1 Protein (FIS1) is a member of the FIS1 family. FIS1 is a single-pass membrane protein and contains one TPR repeat. FIS1 is part of the mitochondrial complex that promotes mitochondrial fission. FIS1 can induce cytochrome C discharge from the mitochondrion to the cytosol, eventually leading to apoptosis. In addition, FIS1 participates in peroxisomal growth and division. The C-terminus of FIS1 is required for mitochondrial or peroxisomal localization, while the N-terminus is necessary for mitochondrial or peroxisomal fission, localization and regulation of the interaction with DNM1L.
Prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226)
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