Disease relevance of PFDN5

• A survey of the A157R mutation of MM-1 in 57 cultured cancer cells and 90 tissues from cancer patients showed that the A157R was present in about 50-60% of leukemia/lymphoma cells and in more than 75% of squamous cell carcinoma of tongue cancer [1].
• MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in leukemia/lymphoma and tongue cancer [1].
• We isolated a variant of phage MM1, named MM1-1998, from a serotype 24 strain of Streptococcus pneumoniae [2].
• In the MM1 peritoneal dissemination model, tumor burden and ascites production were reduced by >50% (P < 0.05) [3].
• Carba derivatives, in which the phosphate oxygen was replaced with a methylene group at either the sn-2 or the sn-3 position, showed much more potent inhibitory effects on MM1 tumor cell transcellular migration and the pulmonary metastasis of B16-F0 melanoma than the natural pal-cPA [4].

Psychiatry related information on PFDN5

• Clusterin expression was examined in seven sporadic cases of CJD (codon 129 genotype, PrP type: 4 MM1, 1 MV1, 1 MV2, 1 VV2) and three age-matched controls by immunohistochemistry, Western blotting and solubility [5].

High impact information on PFDN5

• Expression of MM1 strongly reduced the c-Myc-mediated inhibitory activity on p73 alpha [6].
• We found MM1, a nuclear c-Myc-binding protein, was associated with p73 alpha in both yeast two-hybrid and in vitro pull-down assays [6].
• Moreover, the inhibitory activity of MM-1 toward c-Myc was canceled by trichostatin A, an inhibitor of HDAC1 [7].
• The human MM-1 gene was mapped at chromosome 12q12-12q13, where many chromosome abnormalities in cancer cells have been reported [1].
• MM-1 was found to bind to the central portion of TIF1 beta in vitro and in vivo, and these proteins were found to be colocalized in the nucleus [7].

Biological context of PFDN5

• We have isolated the cDNA encoding a novel c-Myc-binding protein, MM-1, by the yeast two-hybrid screening of a human HeLa cell cDNA library [8].
• We investigated the structural and dynamical properties of B-Myc, free or associated with the transactivation inhibitor, MM-1, and the activator, TBP, using NMR spectroscopy [9].
• The local regions of B-Myc involved in binding differ for MM-1 and TBP, and regions not identified by mutagenesis are found to be involved in MM-1 binding [9].
• Stable active RhoA transfectants of W1 cells (low invasive counterpart of MM1) also demonstrated promoted invasive ability in vitro and in vivo, and enhanced phosphorylation level of MLC20 [10].
• Lysogeny of Streptococcus pneumoniae with MM1 phage: improved adherence and other phenotypic changes [2].

Anatomical context of PFDN5

• The MM-1 mRNA was highly expressed in human pancreas and skeletal muscle and moderately in other tissues [8].
• The mammalian two-hybrid assays in hamster CHO cells revealed that MM-1 interacts in vivo with the N-terminal domain covering the myc box 2, a transcription-activating domain, of c-Myc [8].
• Compounds were further examined on other tumor cell lines such as Jurkat, H1299, and MM1, respectively [11].
• A clone named MM1 was isolated from a library of monoclonal antibodies to adult porcine aorta, which in vivo binds to arterial but not venous SM cells, except for the pulmonary vein [12].

Associations of PFDN5 with chemical compounds

• In an EST data base search for cDNAs homologous to MM-1, we found a frequent substitution of amino acid 157 of MM-1, from alanine to arginine (A157R), and the substitution was observed more in tumor cells than in normal cells [1].
• Herein we made stable transfectants of MM1 expressing active and Botulinum exoenzyme C3 (C3)-sensitive (Val14), or active and C3-insensitive (Val14/Ile41) forms of human RhoA [10].
• The theoretical docking studies showed that MM1 acts on the same site of the receptor as losartan [13].

Physical interactions of PFDN5

• These results indicate that MM-1 is a connecting factor that forms a novel transcription repression pathway of c-Myc [7].

Regulatory relationships of PFDN5

• Furthermore, MM-1 repressed the activation of E-box-dependent transcription by c-Myc [8].

Other interactions of PFDN5

• PTPN18, ABI3BP, and PFDN5 revealed a statistically significant differential splicing profile [14].
• The N-terminal half (Myc1-88) is unfolded and does not alone bind to target proteins, whereas the C-terminal half (Myc92-167) has a partly helical fold and specifically binds both MM-1 and TBP [15].

Analytical, diagnostic and therapeutic context of PFDN5

• In addition, real-time PCR analysis revealed that expression of an alternative PFDN5 variant was higher in malignant lesions than in benign lesions or normal tissues [14].
• However, immunoprecipitation experiments revealed that MM1 bound to a 100-kDa polypeptide that was present only in the arterial SM extract [12].
• A typical EEG was most often seen in MM1 patients and was significantly less likely in the MV1, MV2 and VV2 sub-types, whereas VV2 patients had an increased likelihood of a typical brain MRI [16].

References