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LMNB2  -  lamin B2

Homo sapiens

 
 
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Disease relevance of LMNB2

 

High impact information on LMNB2

  • The initiation sites of bidirectional synthesis at the DNA replication origin located at the 3' end of the human lamin B2 gene were investigated [3].
  • Few genes have generated as much recent interest as LMNA, LMNB1 and LMNB2, which encode the components of the nuclear lamina [4].
  • The proteins bound in vivo at the human lamin B2 DNA replication origin and their precise sites of binding were investigated along the cell cycle utilizing two novel procedures based on immunoprecipitation following UV irradiation with a pulsed laser light source [5].
  • Sequences derived from the human lamin B2 origin can serve as a potent activator for the Mcm helicase, and substitution of its thymine clusters with guanine leads to loss of this activation [6].
  • We followed the variations of protein-DNA interactions occurring in vivo over the early firing replication origin located near the human lamin B2 gene, in IMR-90 cells synchronized in different moments of the cell cycle [7].
 

Biological context of LMNB2

 

Anatomical context of LMNB2

  • Finally, lamin B2 was expressed in all epithelial cells but was not expressed in dermal fibroblasts [13].
  • The lamin B2 antibodies appeared to decorate the nuclear lamina in all tissues examined, except hepatocytes, in which very little lamin B2 expression was observed [14].
  • In Orc2(delta/-) cells, the association of HsOrc-2 with the lamin B2, beta-globin, and c-myc origins was decreased by 2.8-, 4.9-, and 2.8-fold, respectively, relative to wild-type HCT116 cells [15].
  • Lamin B2 modification in synchronously dividing populations of human diploid fibroblasts was determined by 2-dimensional gel electrophoresis and [32P]orthophosphate labelling [11].
  • Our observation that lamin B2 expression in the follicle centre cells of the reactive lymph node is low or absent indicates that this lamin subtype is not always expressed in nucleated cells, which is in clear contrast to the results obtained in previous studies in other diseases and in normal tissues [16].
 

Associations of LMNB2 with chemical compounds

 

Other interactions of LMNB2

 

Analytical, diagnostic and therapeutic context of LMNB2

  • The origin was localized, by means of quantitative PCR within approximately 3000 bp, in a highly transcribed region containing at least two closely spaced genes with the same polarity of transcription, one encoding lamin B2 and the other an unidentified protein [24].
  • As assayed by both fluorescence observing and quantitative RT-PCR, the protein and mRNA products of exogenous gene RFP were efficiently and specifically inhibited; quantitative RT-PCR and western blotting results respectively demonstrated that endogenous lamin B2 mRNA and protein was suppressed without global down-regulation of protein synthesis [25].

References

  1. Sequencing of the reannotated LMNB2 gene reveals novel mutations in patients with acquired partial lipodystrophy. Hegele, R.A., Cao, H., Liu, D.M., Costain, G.A., Charlton-Menys, V., Rodger, N.W., Durrington, P.N. Am. J. Hum. Genet. (2006) [Pubmed]
  2. Autoantibodies to human nuclear lamin B2 protein. Epitope specificity in different autoimmune diseases. Brito, J., Biamonti, G., Caporali, R., Montecucco, C. J. Immunol. (1994) [Pubmed]
  3. Start sites of bidirectional DNA synthesis at the human lamin B2 origin. Abdurashidova, G., Deganuto, M., Klima, R., Riva, S., Biamonti, G., Giacca, M., Falaschi, A. Science (2000) [Pubmed]
  4. Human laminopathies: nuclei gone genetically awry. Capell, B.C., Collins, F.S. Nat. Rev. Genet. (2006) [Pubmed]
  5. Localization of proteins bound to a replication origin of human DNA along the cell cycle. Abdurashidova, G., Danailov, M.B., Ochem, A., Triolo, G., Djeliova, V., Radulescu, S., Vindigni, A., Riva, S., Falaschi, A. EMBO J. (2003) [Pubmed]
  6. Thymine-rich single-stranded DNA activates Mcm4/6/7 helicase on Y-fork and bubble-like substrates. You, Z., Ishimi, Y., Mizuno, T., Sugasawa, K., Hanaoka, F., Masai, H. EMBO J. (2003) [Pubmed]
  7. Cell cycle modulation of protein-DNA interactions at a human replication origin. Abdurashidova, G., Riva, S., Biamonti, G., Giacca, M., Falaschi, A. EMBO J. (1998) [Pubmed]
  8. Modular structure of the human lamin B2 replicator. Paixão, S., Colaluca, I.N., Cubells, M., Peverali, F.A., Destro, A., Giadrossi, S., Giacca, M., Falaschi, A., Riva, S., Biamonti, G. Mol. Cell. Biol. (2004) [Pubmed]
  9. Noncanonical DNA elements in the lamin B2 origin of DNA replication. Kusic, J., Kojic, S., Divac, A., Stefanovic, D. J. Biol. Chem. (2005) [Pubmed]
  10. In vitro protein-DNA interactions at the human lamin B2 replication origin. Stefanovic, D., Stanojcic, S., Vindigni, A., Ochem, A., Falaschi, A. J. Biol. Chem. (2003) [Pubmed]
  11. S-phase phosphorylation of lamin B2. Kill, I.R., Hutchison, C.J. FEBS Lett. (1995) [Pubmed]
  12. Nuclear lamin expression in chronic hibernating myocardium in man. Ausma, J., van Eys, G.J., Broers, J.L., Thoné, F., Flameng, W., Ramaekers, F.C., Borgers, M. J. Mol. Cell. Cardiol. (1996) [Pubmed]
  13. Expression of individual lamins in basal cell carcinomas of the skin. Venables, R.S., McLean, S., Luny, D., Moteleb, E., Morley, S., Quinlan, R.A., Lane, E.B., Hutchison, C.J. Br. J. Cancer (2001) [Pubmed]
  14. A- and B-type lamins are differentially expressed in normal human tissues. Broers, J.L., Machiels, B.M., Kuijpers, H.J., Smedts, F., van den Kieboom, R., Raymond, Y., Ramaekers, F.C. Histochem. Cell Biol. (1997) [Pubmed]
  15. Ku80 binds to human replication origins prior to the assembly of the ORC complex. Sibani, S., Price, G.B., Zannis-Hadjopoulos, M. Biochemistry (2005) [Pubmed]
  16. Comparison of A and B-type lamin expression in reactive lymph nodes and nodular sclerosing Hodgkin's disease. Jansen, M.P., Machiels, B.M., Hopman, A.H., Broers, J.L., Bot, F.J., Arends, J.W., Ramaekers, F.C., Schouten, H.C. Histopathology (1997) [Pubmed]
  17. Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lysates and requires the cysteine residue of the C-terminal CXXM motif. Vorburger, K., Kitten, G.T., Nigg, E.A. EMBO J. (1989) [Pubmed]
  18. Concurrent replication and methylation at mammalian origins of replication. Araujo, F.D., Knox, J.D., Szyf, M., Price, G.B., Zannis-Hadjopoulos, M. Mol. Cell. Biol. (1998) [Pubmed]
  19. The quest for a human ori. Falaschi, A., Giacca, M. Genetica (1994) [Pubmed]
  20. Site-specific and temporally controlled initiation of DNA replication in a human cell-free system. Keller, C., Hyrien, O., Knippers, R., Krude, T. Nucleic Acids Res. (2002) [Pubmed]
  21. Studies of the properties of human origin recognition complex and its Walker A motif mutants. Giordano-Coltart, J., Ying, C.Y., Gautier, J., Hurwitz, J. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  22. Linkage of an autosomal dominant clefting syndrome (Van der Woude) to loci on chromosome Iq. Murray, J.C., Nishimura, D.Y., Buetow, K.H., Ardinger, H.H., Spence, M.A., Sparkes, R.S., Falk, R.E., Falk, P.M., Gardner, R.J., Harkness, E.M. Am. J. Hum. Genet. (1990) [Pubmed]
  23. Reassembling proteins and chaperones in human nuclear matrix protein fractions. Gerner, C., Holzmann, K., Meissner, M., Gotzmann, J., Grimm, R., Sauermann, G. J. Cell. Biochem. (1999) [Pubmed]
  24. A human DNA replication origin: localization and transcriptional characterization. Biamonti, G., Perini, G., Weighardt, F., Riva, S., Giacca, M., Norio, P., Zentilin, L., Diviacco, S., Dimitrova, D., Falaschi, A. Chromosoma (1992) [Pubmed]
  25. shRNA Transcribed by RNA Pol II Promoter Induce RNA Interference in Mammalian Cell. Yuan, J., Wang, X., Zhang, Y., Hu, X., Deng, X., Fei, J., Li, N. Mol. Biol. Rep. (2006) [Pubmed]
 
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