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MCM2  -  minichromosome maintenance complex...

Homo sapiens

Synonyms: BM28, CCNL1, CDCL1, D3S3194, DNA replication licensing factor MCM2, ...
 
 
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Disease relevance of MCM2

  • Further studies are needed to understand the significance of ABCG2 and MCM2 expression in retinoblastoma [1].
  • This study examined the clinicopathological significance of minichromosome maintenance-2 (MCM2) expression in 38 human malignant fibrous histiocytomas (MFHs) and 36 benign fibrohistiocytic tumors (BFHTs) immunohistochemically, and in 9 human sarcoma or carcinoma cell lines, as well as 7 surgical specimens by Western blotting [2].
  • Future studies will determine if use of anti-MCM2 makes possible sufficiently early detection to significantly enhance lung cancer survival rates [3].
  • Here we compared the sensitivities of a classic proliferation marker, Ki-67, with a new proliferation marker, MCM2, in 41 bronchial biopsy specimens representing normal mucosa, metaplasia, dysplasia, and carcinoma in situ [3].
  • We aim to develop a non-invasive, stool-based assay that can identify colorectal cancer by detection of minichromosome maintenance protein 2 (MCM2) expression in colonocytes retrieved from the faecal surface [4].
 

High impact information on MCM2

 

Chemical compound and disease context of MCM2

 

Biological context of MCM2

 

Anatomical context of MCM2

  • Expression of minichromosome maintenance 2 (MCM2), Ki-67, and cell-cycle-related molecules, and apoptosis in the normal-dysplasia-carcinoma sequence of the oral mucosa [11].
  • BACKGROUND/AIM: The authors studied the expression of cancer stem cell surface marker, ABCG2, and neural stem cell marker, MCM2, in retinoblastoma and correlated clinicopathologically [1].
  • The promise of MCM2 as a sensitive marker for premalignant lung cells is enhanced by the fact that it is present in cells at the surface of metaplastic lung lesions, which are more likely to be exfoliated into sputum [3].
  • At 36, 48, 60, and 72 hours after wounding, the percentage of MCM2-positive cells in the central or peripheral area of older corneas was significantly less than in the corresponding region in younger corneas [12].
  • Mitotin is a 125 kDa/pI 6.5 nuclear matrix protein present in proliferating but not in resting cells [13].
 

Associations of MCM2 with chemical compounds

  • Alanine substitution experiments with Mcm2 peptides showed that the phosphorylation of (5)S and (53)S by Cdc7 required the presence of an acidic amino acid adjacent to a serine residue [6].
  • Brief treatment of IL-1 alpha/TNF alpha-stimulated CDCL cells with cycloheximide before receptor induction reduces the synergistic increase in growth factor mRNA by 40% to 60% compared with cells not treated with CHX [14].
  • The results from the immunofluorescent study show a gradual disappearance of mitotin in differentiating HL 60 cells starting from the fourth day after DMSO induction [15].
 

Enzymatic interactions of MCM2

  • ASK forms an active kinase complex with huCdc7 that is capable of phosphorylating MCM2 protein [16].
 

Regulatory relationships of MCM2

  • MCM2 is regulated via a P53-independent pathway, and a useful biomarker of proliferating cells [11].
 

Other interactions of MCM2

  • MCM-BP also formed a complex with the MCM4/6/7 core helicase in vitro, but, unlike MCM2, did not inhibit this helicase activity [17].
  • Indeed, over-expression of both huCdc7 and ASK results in the elevated phosphorylation of endogenous MCM2 protein, as manifested by appearance of the mobility-shifted form on SDS-PAGE, but does not cause any significant effects on cell cycle progression [18].
  • The LI of MCM2, P21 and the TI were not correlated with P53 expression [11].
  • The higher LI of MCM2 and P53 and the lower LI of P21 might predict malignant transformation of oral dysplasia [11].
  • Moreover, the LI was significantly higher for MCM2 than that for Ki-67 in the MFHs of both types (p<0.05) [2].
 

Analytical, diagnostic and therapeutic context of MCM2

References

  1. Stem cell markers: ABCG2 and MCM2 expression in retinoblastoma. Mohan, A., Kandalam, M., Ramkumar, H.L., Gopal, L., Krishnakumar, S. The British journal of ophthalmology. (2006) [Pubmed]
  2. Expression of minichromosome maintenance-2 in human malignant fibrous histiocytomas: Correlations with Ki-67 and P53 expression, and apoptosis. Osaki, M., Osaki, M., Yamashita, H., Shomori, K., Yoshida, H., Ito, H. Int. J. Mol. Med. (2002) [Pubmed]
  3. MCM2--a promising marker for premalignant lesions of the lung: a cohort study. Tan, D.F., Huberman, J.A., Hyland, A., Loewen, G.M., Brooks, J.S., Beck, A.F., Todorov, I.T., Bepler, G. BMC Cancer (2001) [Pubmed]
  4. Analysis of minichromosome maintenance proteins as a novel method for detection of colorectal cancer in stool. Davies, R.J., Freeman, A., Morris, L.S., Bingham, S., Dilworth, S., Scott, I., Laskey, R.A., Miller, R., Coleman, N. Lancet (2002) [Pubmed]
  5. BM28, a human member of the MCM2-3-5 family, is displaced from chromatin during DNA replication. Todorov, I.T., Attaran, A., Kearsey, S.E. J. Cell Biol. (1995) [Pubmed]
  6. CDC7 kinase phosphorylates serine residues adjacent to acidic amino acids in the minichromosome maintenance 2 protein. Cho, W.H., Lee, Y.J., Kong, S.I., Hurwitz, J., Lee, J.K. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  7. Minimally Invasive Follicular Carcinoma Versus Follicular Adenoma: MCM2 Proliferation Marker may be Helpful. Akhtar, M., Scognamiglio, T. Advances in anatomic pathology. (2006) [Pubmed]
  8. Phosphorylation of MCM4 by Cdc7 Kinase Facilitates Its Interaction with Cdc45 on the Chromatin. Masai, H., Taniyama, C., Ogino, K., Matsui, E., Kakusho, N., Matsumoto, S., Kim, J.M., Ishii, A., Tanaka, T., Kobayashi, T., Tamai, K., Ohtani, K., Arai, K. J. Biol. Chem. (2006) [Pubmed]
  9. A human nuclear protein with sequence homology to a family of early S phase proteins is required for entry into S phase and for cell division. Todorov, I.T., Pepperkok, R., Philipova, R.N., Kearsey, S.E., Ansorge, W., Werner, D. J. Cell. Sci. (1994) [Pubmed]
  10. Essential Role of Phosphorylation of MCM2 by Cdc7/Dbf4 in the Initiation of DNA Replication in Mammalian Cells. Tsuji, T., Ficarro, S.B., Jiang, W. Mol. Biol. Cell (2006) [Pubmed]
  11. Expression of minichromosome maintenance 2 (MCM2), Ki-67, and cell-cycle-related molecules, and apoptosis in the normal-dysplasia-carcinoma sequence of the oral mucosa. Kodani, I., Shomori, K., Osaki, M., Kuratate, I., Ryoke, K., Ito, H. Pathobiology (2001) [Pubmed]
  12. Replication competence and senescence in central and peripheral human corneal endothelium. Mimura, T., Joyce, N.C. Invest. Ophthalmol. Vis. Sci. (2006) [Pubmed]
  13. Nuclear matrix protein mitotin messenger RNA is expressed at constant levels during the cell cycle. Todorov, I.T., Lavigne, J., Sakr, F., Kaneva, R., Foisy, S., Bibor-Hardy, V. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  14. Interleukin-1 alpha upregulates tumor necrosis factor receptors expressed by a human bone marrow stromal cell strain: implications for cytokine redundancy and synergy. Caldwell, J., Emerson, S.G. Blood (1995) [Pubmed]
  15. Expression of the nuclear protein mitotin in differentiating in vitro HL 60 cells. Philipova, R.N., Vassilev, A.P., Kaneva, R.P., Andreeva, P., Todorov, I.T., Hadjiolov, A.A. Biol. Cell (1991) [Pubmed]
  16. A novel growth- and cell cycle-regulated protein, ASK, activates human Cdc7-related kinase and is essential for G1/S transition in mammalian cells. Kumagai, H., Sato, N., Yamada, M., Mahony, D., Seghezzi, W., Lees, E., Arai, K., Masai, H. Mol. Cell. Biol. (1999) [Pubmed]
  17. Identification and characterization of a novel component of the human minichromosome maintenance complex. Sakwe, A.M., Nguyen, T., Athanasopoulos, V., Shire, K., Frappier, L. Mol. Cell. Biol. (2007) [Pubmed]
  18. Cell cycle regulation of chromatin binding and nuclear localization of human Cdc7-ASK kinase complex. Sato, N., Sato, M., Nakayama, M., Saitoh, R., Arai, K., Masai, H. Genes Cells (2003) [Pubmed]
  19. Two immunologically distinct human DNA polymerase alpha-primase subpopulations are involved in cellular DNA replication. Dehde, S., Rohaly, G., Schub, O., Nasheuer, H.P., Bohn, W., Chemnitz, J., Deppert, W., Dornreiter, I. Mol. Cell. Biol. (2001) [Pubmed]
 
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