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IFIH1 is a DEAD box protein which is upregulated in response to treatment with beta-interferon and a protein kinase C-activating compound, mezerein. Irreversible reprogramming of melanomas can be attained by therapy with both these agents; treatment with either agent alone only achieves reversible differentiation. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly.

S100A9 is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A9 protein is localized in the cytoplasm and/or nucleus of a wide range of cells, and participates in the regulation of several cellular processes such as cell cycle progression and differentiation. S100 genes include no less than 13 proteins which are localized as a cluster on chromosome 1q21. S100A9 is involved in the inhibition of casein kinase and altered expression of this protein is associated with the disease cystic fibrosis.

c-Myc is a multifunctional, nuclear phosphoprotein that plays a role in cell cycle progression, apoptosis and cellular transformation. It functions as a transcription factor that regulates transcription of specific target genes. Mutations, overexpression, rearrangement and translocation of c-Myc have been associated with a variety of hematopoietic tumors, leukemias and lymphomas, including Burkitt lymphoma. There is evidence to show that alternative translation initiations from an upstream, in-frame non-AUG (CUG) and a downstream AUG start site result in the production of two isoforms with distinct N-termini. The synthesis of non-AUG initiated protein is suppressed in Burkitt's lymphomas, suggesting its importance in the normal function of this gene.

Hemoglobin subunit zeta (HBZ) is part of the globin family. Hemoglobin Zeta is alpha-like hemoglobin. The HBZ polypeptide is synthesized in the yolk sac of the early embryo, while alpha-globin is produced throughout fetal and adult life.

MMADHC is a mitochondrial protein which takes part in an early step of vitamin B1 2 metabolism. Vitamin B12 (cobalamin) is vital for regular development and existence in humans. Mutations in MMADHC can result in methylmalonic aciduria and homocystinuria type cblD, a cobalamin metabolism syndrome which is characterized by decreased levels of the coenzymes methylcobalamin and adenosylcobalamin.

Non muscle Myosins are required for cytokinesis at the end of cell division, when a contractile ring near the plasmalemma divides the cytoplasm of the daughter cells. They are involved in cytoplasmic streaming movements in tissues, and especially in activation of motile cells such as fibroblasts and macrophages. Activation of non-muscle myosin-II is achieved by phosphorylation of Ser33 in the motif KKRPQRATSN by a dedicated, Ca +2 Calmodulin regulated light chain kinase (MLCK).

Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.

GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

MUC16, aka CA125, is a mucin protein that might be found in type I transmembrane or secreted forms that are used monitor the progress of epithelial ovarian cancer therapy.
The CA125 molecule is heterogeneous with regard to both size and charge, almost certainly due to continuous deglycosylation of side chains during its life-span in bodily fluids.
MUC16 is most likely a glycoprotein with a predominance of O-linkages.

c-Myc is a multifunctional, nuclear phosphoprotein that plays a role in cell cycle progression, apoptosis and cellular transformation. It functions as a transcription factor that regulates transcription of specific target genes. Mutations, overexpression, rearrangement and translocation of c-Myc have been associated with a variety of hematopoietic tumors, leukemias and lymphomas, including Burkitt lymphoma. There is evidence to show that alternative translation initiations from an upstream, in-frame non-AUG (CUG) and a downstream AUG start site result in the production of two isoforms with distinct N-termini. The synthesis of non-AUG initiated protein is suppressed in Burkitt's lymphomas, suggesting its importance in the normal function of this gene.

B2M is a part of the MHC class I family that participates in the presentation of peptide antigens to the immune system. B2M is localized on the surface of numerous cells and abundant on the surface of white blood cells. High production or destruction of these cells causes B2M levels in the blood to raise. This increase is observed in people with cancers involving white blood cells, but it is mainly significant in people newly diagnosed with multiple myeloma. B2M Testing is done primarily when evaluating a person for certain kinds of cancer affecting white blood cells including chronic lymphocytic leukemia, non-Hodgkin''s lymphoma, and multiple myeloma or kidney disease.

MCL1 is a member of the Bcl-2 family. MCL1 takes part in the control of apoptosis against cell existence, and in the preservation of viability but not of proliferation. Alternative splicing happens at this locus and two transcript variants encoding different isoforms are known. Isoform 1 is the longer gene product and it increases cell existence by inhibiting apoptosis. Isoform 2 is a shorter gene product which indorses apoptosis and is death-inducing.

Though the exact role of MMACHC is unknown, its C-terminal region shows similarity to TonB, which is a bacterial protein involved in energy transduction for cobalamin (vitamin B12) uptake. Therefore, it is suggested that MMACHC may have a role in the binding and intracellular trafficking of cobalamin. MMACHC mutations are linked with methylmalonic aciduria and homocystinuria type cblC. MMACHC is widely expressed, it is expressed at higher level in the fetal liver, however it is also expressed in the spleen, lymph node, thymus and bone marrow. MMACHC is weakly or not expressed in the peripheral blood leukocytes.

Marginal zone B- and B1-cell-specific protein (MZB1) functions as a hormone-regulated adipokine/proinflammatory cytokine which is implicated in causing chronic inflammation and affecting cellular expansion. MZB1 links with immunoglobulin M (IgM) heavy and light chains and stimulate s IgM assembly and secretion. MZB1 exerts its effect by acting as a molecular chaperone or as an oxidoreductase as it exhibits a low level of oxidoreductase activity. MZB1 helps to diversify peripheral B-cell functions by regulating Ca(2+) stores, antibody secretion and integrin activation.

Myostatin (GDF-8) is expressed uniquely in human skeletal muscle as a 12 kDa mature glycoprotein consisting of 113 amino acid residues and secreted into plasma. Myostatin is a member of the transforming growth factor ? superfamily of secreted growth and differentiation factors that is essential for proper regulation of skeletal muscle mass. Studies have shown that myostatin could play an important role in cardiac development and physiology.

MICB (MHC class I chain-related gene B) is a transmembrane glycoprotein that functions as a ligand for human NKG2D type II receptor. A closely related protein, MICA, shares 85% amino acid identity with MICB. These 2 proteins are distantly related to the MHC class I proteins. MICA and MICB (MICA/B) possess three extracellular immunoglobulin-like domains, but have no capacity to bind peptide or interact with ?2-microglobulin. The genes encoding MICA/B are found within the major histocompatibility complex on human chromosome 6. The MICB locus is polymorphic with more than 15 recognized human alleles. MICA/B are minimally expressed on normal cells, but are frequently expressed on epithelial tumors and can be induced by bacterial and viral infections. MICA/B are ligands for NKG2D, an activating receptor expressed on NK cells, NKT cells, ?? T cells, and CD8+ ?? T cells. Recognition of MICA/B by NKG2D results in the activation of cytolytic activity and/or cytokine production by these effector cells. MICA/B recognition is involved in tumor surveillance, viral infections, and autoimmune diseases. The release of soluble forms of MICA/B from tumors down-regulates NKG2D surface expression on effector cells resulting in the impairment of anti-tumor immune response.

The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.

Myeloid leukemia factor 1 (MLF1) is a member of the MLF family, and is a widely expressed negative regulator of cell cycle progression functioning upstream of the tumor suppressor p53. MLF1 hinders the erythropoietin-induced erythroid terminal differentiation by averting cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. MLF1 generally functions in multi-potent progenitor cells, and its dysregulation may be to some extent responsible for leukemogenesis. Translocations between the MLF1 gene and nucleophosmin are linked to myelodysplastic syndrome and acute myeloid leukemia.

Beta 2 microglobulin is an 11 kDa protein associated with the outer membrane of many cells including lymphocytes. It is the small subunit of the MHC class I molecule. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. Beta 2 microglobulin associates with class I-like molecules such as CD1 and Qa as well as with the alpha chain of MHC class I molecules. Very limited amounts of MHC class I molecules can be found on the surface in the absence of Beta 2 microglobulin. CD8 T cells cannot develop in the absence of MHC class I.
Beta 2-microglobulin is present in small amounts in serum, csf, and urine of normal people, and to a much greater degree in the urine and plasma of patients with tubular proteinaemia, renal failure, or kidney transplants. Human Beta 2 microglobulin levels can rise either because its rate of synthesis has increased (e.g. in AIDS, malignant monoclonal plasma cell dyscrasia, solid tumors and autoimmune disease) or because of impaired renal filtration (e.g. due to renal insufficiency, graft rejection or nephrotoxicity induced by post-transplantation immunosuppressive therapy). Beta-2 microglobulin levels might also be elevated in multiple myeloma and lymphoma cases. Dialysis-related amyloidosis develops after a long-term hemodialysis, it can aggregate into amyloid fibers that deposit in joint spaces.

The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

Troponin I, (TNNI1) is a member of the troponin I family. Troponin complex has 3 subunits, TNNI1 known as the inhibitory Subunit which prevents the actin-myosin interactions and thus mediating striated muscle relaxation. TNNI1 combines with tropomyosin and regulates calcium sensitivity of striated muscles by structural modifications in actin-myosin complexes.