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Gene Review

Lmnb1  -  lamin B1

Mus musculus

Synonyms: Lamin-B1
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Disease relevance of Lmnb1


High impact information on Lmnb1


Biological context of Lmnb1


Anatomical context of Lmnb1

  • Its position on two-dimensional gel suggested that p70 is nuclear envelope lamin B. This possibility was confirmed by the co-migration of p70 with the lamin fraction of mouse liver and its immunoprecipitation with antinuclear lamina antibody [11].
  • Lamin B also conforms to the general molecular organization principle of the members of the intermediate filament (IF) protein family, i.e., an extended alpha-helical rod domain that is interrupted by two non alpha-helical linkers and flanked by non-alpha-helical head (amino-terminal) and tail (carboxy-terminal) domains [1].
  • On immunoblots anti-lamin B reacts with a approximately 68 kD polypeptide in all germ cells and, to a lesser extent, with four additional polypeptides present only in meiotic and post-meiotic nuclear matrices [10].
  • Anti-lamin B binds to the nuclear periphery of all cell types examined, including Sertoli cells, primitive type A spermatogonia, preleptotene, leptotene, zygotene and pachytene spermatocytes, and round spermatids [10].
  • In mouse morulae or blastocysts, lamins A/C are no longer recognized, although lamin B remains [12].

Associations of Lmnb1 with chemical compounds


Regulatory relationships of Lmnb1

  • Lamin B2 is coexpressed with lamin B1 (formerly termed lamin B) in all somatic cells and mammalian species that we analysed, including a variety of cells currently believed to contain only a single lamin [16].
  • The occurrence of nuclear abnormalities was reduced when lamin B1 was coexpressed with mutant lamin A, emphasizing the functional interaction of the two types of lamins [17].
  • The cleavage of lamin B was inhibited by caspase inhibitors [18].

Other interactions of Lmnb1

  • This view and earlier results on lamin B predict multiple post-translational modifications shared by lamins A and B. While retained by lamin B, which is present in all cells, they are lost by maturation from lamin A, which probably acts only as an additional lamina constituent in differentiated cells [19].
  • Apoptosis was accompanied by the processing and activation of CPP32 and Mch3 alpha, together with the cleavage of poly(ADP-ribose) polymerase and lamin B1 [20].
  • The results agree in that a major part of the enzyme co-localizes with lamin B under physiological conditions, where PARP-1 only has basal activity [21].
  • Apoptosis induced by IL-3 deprivation but not BSO also caused lamin B1 cleavage, suggesting activation of caspase-6 [22].
  • In eggs collected at the pronuclear stage and cultured to the late two-cell stage in the presence of alpha-amanitin, the matrix morphology was altered for Pl1 and Pl2. alpha-Amanitin had no affect on the distribution of P1 or lamin B antigens [23].

Analytical, diagnostic and therapeutic context of Lmnb1

  • Western blot analysis of the expression of lamins with specific antibodies indicates that lamin B is expressed throughout liver development, unlike lamins A and C which are absent in fetal liver [24].
  • Co-localization of PARP-1 and lamin B in the nuclear architecture: a halo-fluorescence- and confocal-microscopy study [21].


  1. Amino acid sequence and molecular characterization of murine lamin B as deduced from cDNA clones. Höger, T.H., Krohne, G., Franke, W.W. Eur. J. Cell Biol. (1988) [Pubmed]
  2. Differential timing of nuclear lamin A/C expression in the various organs of the mouse embryo and the young animal: a developmental study. Röber, R.A., Weber, K., Osborn, M. Development (1989) [Pubmed]
  3. Toxic bile salts induce rodent hepatocyte apoptosis via direct activation of Fas. Faubion, W.A., Guicciardi, M.E., Miyoshi, H., Bronk, S.F., Roberts, P.J., Svingen, P.A., Kaufmann, S.H., Gores, G.J. J. Clin. Invest. (1999) [Pubmed]
  4. In vitro phosphorylation of lamin B by protein kinase C in friend erythroleukemia. Effect of chemically induced differentiation. Billi, A.M., Matteucci, A., Bertagnolo, V., Previati, M., Manzoli, F.A., Capitani, S. Cell Biol. Int. Rep. (1991) [Pubmed]
  5. Teratocarcinoma stem cells and early mouse embryos contain only a single major lamin polypeptide closely resembling lamin B. Stewart, C., Burke, B. Cell (1987) [Pubmed]
  6. Nuclear lamins A and B1: different pathways of assembly during nuclear envelope formation in living cells. Moir, R.D., Yoon, M., Khuon, S., Goldman, R.D. J. Cell Biol. (2000) [Pubmed]
  7. Dynamic properties of nuclear lamins: lamin B is associated with sites of DNA replication. Moir, R.D., Montag-Lowy, M., Goldman, R.D. J. Cell Biol. (1994) [Pubmed]
  8. Lamin B1 is required for mouse development and nuclear integrity. Vergnes, L., Péterfy, M., Bergo, M.O., Young, S.G., Reue, K. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  9. Genomic structure of the mouse gene (Lmnb1) encoding nuclear lamin B1. Maeno, H., Sugimoto, K., Nakajima, N. Genomics (1995) [Pubmed]
  10. The differential expression of lamin epitopes during mouse spermatogenesis. Moss, S.B., Burnham, B.L., Bellvé, A.R. Mol. Reprod. Dev. (1993) [Pubmed]
  11. Identification of lamin B2 as a substrate of protein kinase C in BALB/MK-2 mouse keratinocytes. Kasahara, K., Chida, K., Tsunenaga, M., Kohno, Y., Ikuta, T., Kuroki, T. J. Biol. Chem. (1991) [Pubmed]
  12. Nuclear lamins and peripheral nuclear antigens during fertilization and embryogenesis in mice and sea urchins. Schatten, G., Maul, G.G., Schatten, H., Chaly, N., Simerly, C., Balczon, R., Brown, D.L. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  13. Evidence for modification of lamin B by a product of mevalonic acid. Wolda, S.L., Glomset, J.A. J. Biol. Chem. (1988) [Pubmed]
  14. Nuclear envelope remodeling during mouse spermiogenesis: postmeiotic expression and redistribution of germline lamin B3. Schütz, W., Alsheimer, M., Ollinger, R., Benavente, R. Exp. Cell Res. (2005) [Pubmed]
  15. Geraniol, an inhibitor of mevalonate biosynthesis, suppresses the growth of hepatomas and melanomas transplanted to rats and mice. Yu, S.G., Hildebrandt, L.A., Elson, C.E. J. Nutr. (1995) [Pubmed]
  16. Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin. Höger, T.H., Zatloukal, K., Waizenegger, I., Krohne, G. Chromosoma (1990) [Pubmed]
  17. Expression of lamin A mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy. Favreau, C., Dubosclard, E., Ostlund, C., Vigouroux, C., Capeau, J., Wehnert, M., Higuet, D., Worman, H.J., Courvalin, J.C., Buendia, B. Exp. Cell Res. (2003) [Pubmed]
  18. Caspase activation during apoptotic cell death induced by expanded polyglutamine in N2a cells. Wang, G.H., Mitsui, K., Kotliarova, S., Yamashita, A., Nagao, Y., Tokuhiro, S., Iwatsubo, T., Kanazawa, I., Nukina, N. Neuroreport (1999) [Pubmed]
  19. Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure of the nuclear lamina. Weber, K., Plessmann, U., Traub, P. FEBS Lett. (1989) [Pubmed]
  20. Activation of CPP32 and Mch3 alpha in wild-type p53-induced apoptosis. Chandler, J.M., Alnemri, E.S., Cohen, G.M., MacFarlane, M. Biochem. J. (1997) [Pubmed]
  21. Co-localization of PARP-1 and lamin B in the nuclear architecture: a halo-fluorescence- and confocal-microscopy study. Vidaković, M., Koester, M., Goetze, S., Winkelmann, S., Klar, M., Poznanović, G., Bode, J. J. Cell. Biochem. (2005) [Pubmed]
  22. Apoptosis in hematopoietic cells (FL5.12) caused by interleukin-3 withdrawal: relationship to caspase activity and the loss of glutathione. Bojes, H.K., Feng, X., Kehrer, J.P., Cohen, G.M. Cell Death Differ. (1999) [Pubmed]
  23. Construction of the nuclear matrix at the transition from maternal to zygotic control of development in the mouse: an immunocytochemical study. Prather, R.S., Schatten, G. Mol. Reprod. Dev. (1992) [Pubmed]
  24. Developmental changes in the organization of the nuclear lamina in mouse liver. Pandey, S., Parnaik, V.K. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
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