Disease relevance of MIB2

• Treatment with a demethylating agent, 5'-aza-2-deoxycytidine, restored skeletrophin expression in cultured Mewo melanoma cells [1].
• In malignant plasma cells from 23 of 40 multiple myeloma specimens, strong skeletrophin expression was observed, especially from patients with osteolytic bone lesions [2].
• Promoter swapping between the genes for a novel zinc finger protein and beta-catenin in pleiomorphic adenomas with t(3;8)(p21;q12) translocations [3].
• Isolation of a cDNA encoding a novel zinc-finger protein from neuroblastoma x glioma NG108-15 cells [4].
• Cloning and characterization of a novel zinc finger protein (MDZF) that is associated with monocytic differentiation of acute promyelocytic leukemia cells [5].

High impact information on MIB2

• We describe a novel zinc finger protein, ZID (zinc finger protein with interaction domain) [6].
• We have identified the novel zinc finger protein APA-1, whose expression increased in senescent human fibroblasts independent of telomere shortening [7].
• Cytoplasmic localization, which may indicate Jagged-2 internalization, was found in many skeletrophin-positive myeloma cells [2].
• In contrast, skeletrophin was only weakly expressed in a few nonneoplasmic plasma cells in chronically inflamed tissues [2].
• Down-regulation of a novel actin-binding molecule, skeletrophin, in malignant melanoma [1].

Biological context of MIB2

• Fluorescence in situ hybridization mapped the skeletrophin gene on human chromosome 1p36.2-36.3, in which putative tumor suppressor genes for malignant melanoma have been postulated to exist [1].
• Skeletrophin, a novel RING molecule controlled by the chromatin remodeling complex, is downregulated in malignant melanoma [8].
• Surprisingly, the skeletrophin gene is located in 1p36.32, where the putative tumor suppressor gene of cutaneous malignant melanoma has long been postulated to be on [8].
• Skeletrophin, was therefore identified as a candidate molecule for the indication of change to a malignant phenotype due to the aberrant function of the chromatin remodeling complex [8].
• Activation of the B-cell surface receptor CD40 induces A20, a novel zinc finger protein that inhibits apoptosis [9].

Anatomical context of MIB2

• Northern blot analysis revealed that the 3.2-kb skeletrophin mRNA was expressed in normal skeletal muscle, and to a lesser extent in heart, brain, and kidney [1].
• The A20 gene product is a novel zinc finger protein originally described as a tumor necrosis factor alpha (TNF)-inducible early response gene in human umbilical vein endothelial cells (HUVEC) [10].
• We also found that skeletrophin downregulated transcription of the Met oncogene, which encodes the hepatocyte growth factor receptor and plays a role in the determination of the invasive phenotype of many malignant tumors [11].
• GLP-1: A novel zinc finger protein required in somatic cells of the gonad for germ cell development [12].
• Identification and characterization of a novel zinc finger protein (HZF1) gene and its function in erythroid and megakaryocytic differentiation of K562 cells [13].

Associations of MIB2 with chemical compounds

• Formalin-fixed, paraffin-embedded sections routinely processed for immunohistochemistry failed to stain for Ki-67 and MIB 2 [14].
• Cloning and characterization of a novel zinc finger protein (rZFP96) in the rat corpus luteum [15].

Other interactions of MIB2

• Skeletrophin (mindbomb homolog 2 (MIB2)) is a RING (Really Interesting New Gene) finger-dependent ubiquitin ligase, which targets the intracellular region of Notch ligands [11].
• Skeletrophin is an actin-binding cytoskeleton-related molecule, which is induced by the overexpression of truncated human SWI1 (SMARCF1) [8].
• Activation of transcriptional activities of AP1 and SRE by a novel zinc finger protein ZNF445 [16].
• In the present study, we have identified a promoter region of skeletrophin on a CpG island and detected aberrant methylation of this region in six of 31 invasive melanomas, but in none of 25 benign nevi or five non-invasive superficial spreading melanomas [11].
• An activator protein-2, which has a tumor suppressor-like role in melanoma, increased skeletrophin expression [11].

Analytical, diagnostic and therapeutic context of MIB2

• Specific antibody was prepared to human skeletrophin peptide, and a single protein band with an approximate molecular weight of 70 kd was detected in tissue extracts by immunoblotting using the antibody [1].
• Co-immunoprecipitation experiments also demonstrated that skeletrophin was able to bind to actin monomer [1].
• Molecular cloning and characteristics of a novel zinc finger protein and its splice variant whose transcripts are expressed during spermatogenesis [17].

References