MACH
MORT 1 associated CED-3 homolog; also called FLICE or Caspase-8.
MALT lymphomas
B cell lymphomas of Mucosa-Associated Lymphoid Tissue, in most cases arising in the gastric mucosa, either as low-grade or high-grade form. High-grade MALT lymphoma might result from transformation of low-grade disease. There is an etological link between low-grade gastric malt lymphoma and infection with Helicobacter pilori. Cytogenetic studies of low-grade MALT lymphomas identified abnormalities of chromosome 1p22, in particular translocation t(1;14)(p22,q32): on 1p22 the gene Bcl-10 was cloned and found to be mutated in MALT lymphomas but also in other tumor types (Willis et al., 1999, Cel, 96: 35-45).
MAP3K
Mitogen-Activated Protein kinase kinase kinase.
mdm-2
The mdm-2 gene was identified by virtue of its amplification in transformed mouse lines and in 30-40% of human sarcomas mdm2 is amplified. Its overexpression was shown to be tumourigenic. Homologous deletion of mdm-2 in mice is lethal at early stages of embryogenesis but is completely rescued by additional deletion of the p53 gene. By binding to p53, the mdm-2 gene product MDM2 can target p53 for nuclear export and degradation. Moreover, it can block transcriptional activity of p53. Interestingly, mdm-2 is a transcriptional target of p53, what gives rise to a feedback loop (Freedman and Levine, 1999, Cancer Research, 59: 1-7)!
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MEFs
Mouse Embryonic Fibroblasts
MMPs
Matrix MetalloProteinases (MMPs) break down collagen and other proteins that form connective tissue. This is important for cell mobility, e.g. during embryonic development and for the migration of immune cells or the cells necessary for wound healing to places where they are needed. But overactivity of MMPs can be involved in disorders such as arthritis and cancer. MMP-2 was found to be overexpressed in metatstatic tumors, obviously helping the tumors to spread by degrading collagen in basement membranes, which usually are a first barrier for tumor cells during the metastatic process.
MORT1
Synonym for FADD.
Myc
Myc is a nuclear protein that belongs to the helix-loop-helix / leucin zipper family of transcriptional factors.
Similar to other members of this family, it binds specifically to DNA elements with a central E-box element
(Blackwell, 1990; Kerkhoff et al., 1991; Prendergast and Ziff, 1991).
As a heterodimeric complex with Max, the affinity of Myc to target E-box elements is greatly enhanced
and the complex acts as an activator of transcription (Amati et al., 1992; Kretzner et al., 1992, Amin et al., 1993).
Properties like cellular transformation, induction of cell proliferation and induction of apoptosis by Myc all require heterodimerization with Max
(Stone et al, 1987; Amati et al. 1993a,b).
Mad-1, Mad-2 (=Mxi-1), Mad-3 and Mad-4, often accumulated in quiescent cells, form heterodimeric complexes with Max but not with Myc
(Ayer et al., 1993; Zervos et al., 1993; Hurlin et al., 1995) and these complexes are active repressors of transcription through increased
HDAC1 binding and histone deacetylation (Ayer et al, 1995; Schreiber-Agus et al., 1995, Bouchard et al., 2001).
Taken together, it is strongly suggested that Myc, Max and Mad form a network of interacting proteins that controls a set of target genes
critically involved in proliferation and apoptosis (for review see Amati and Land, 1994).
MyD88
Myeloid Differentiation Factor 88; necessary for Toll receptor and IL-1R signaling; MyD88 initiates a signaling pathway which sequentially involves IRAK-1, TRAF6, and NIK. MyD88 also contains a DD and binds to FADD, thereby activating caspase-8 and apoptosis (Aliprantis et al., 2000, EMBO, 19(13):3325-36).