The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

LOC396224  -  lamin A

Gallus gallus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of LMNA


High impact information on LMNA


Biological context of LMNA


Anatomical context of LMNA

  • Our results demonstrate that the P19 cells, although normally devoid of lamin A, properly incorporate and process chicken lamin A. Moreover, the stably transfected cell lines maintain the properties of undifferentiated cells, demonstrating that expression of lamin A does not directly induce differentiation [2].
  • However, whereas the lamin A precursor was stable, the translation product of the lamin B2 transcript was processed in the reticulocyte lysate to a polypeptide comigrating on two-dimensional gels with authentic mature lamin B2 [10].

Associations of LMNA with chemical compounds

  • Using N-(acetyltyrosinylvalinyl-Nepsilon-biotinyllysyl) aspartic acid [(2,6-dimethylbenzoyl)oxy] methyl ketone, which derivatizes the active forms of caspases, we could show that one of five caspases active in the extracts is inhibited both by CrmA/SPI-2 and by a peptide spanning the lamin A apoptotic cleavage site [1].
  • Conversely, when exposed to retinoic acid, an inducer of differentiation, lamin A-expressing P19 cells are able to differentiate normally [2].
  • We also report that, contrary to the predictions of previously published work, substitution of a critical residue in the nuclear lamin A/C nuclear localization signal (the equivalent of lysine 128 in the SV40 large T nuclear localization signal) retains nuclear localization, and discuss how amino acid context might affect targeting to the nucleus [9].

Analytical, diagnostic and therapeutic context of LMNA

  • First, peptide mapping experiments and immunological criteria demonstrate that these two proteins are not related to each other or to lamin A via postsynthetic modifications or precursor-product relationships [11].
  • Furthermore, we show that in vitro translation of transcripts derived from lamin A and lamin B2 cDNAs yielded polypeptides that were indistinguishable, by two-dimensional gel electrophoresis, from the putative in vivo precursors of lamins A and B2 respectively [10].


  1. CrmA/SPI-2 inhibition of an endogenous ICE-related protease responsible for lamin A cleavage and apoptotic nuclear fragmentation. Takahashi, A., Musy, P.Y., Martins, L.M., Poirier, G.G., Moyer, R.W., Earnshaw, W.C. J. Biol. Chem. (1996) [Pubmed]
  2. Ectopic expression of an A-type lamin does not interfere with differentiation of lamin A-negative embryonal carcinoma cells. Peter, M., Nigg, E.A. J. Cell. Sci. (1991) [Pubmed]
  3. The role of the head and tail domain in lamin structure and assembly: analysis of bacterially expressed chicken lamin A and truncated B2 lamins. Heitlinger, E., Peter, M., Lustig, A., Villiger, W., Nigg, E.A., Aebi, U. J. Struct. Biol. (1992) [Pubmed]
  4. Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation. Ruchaud, S., Korfali, N., Villa, P., Kottke, T.J., Dingwall, C., Kaufmann, S.H., Earnshaw, W.C. EMBO J. (2002) [Pubmed]
  5. Expression of nuclear lamin A and muscle-specific proteins in differentiating muscle cells in ovo and in vitro. Lourim, D., Lin, J.J. J. Cell Biol. (1989) [Pubmed]
  6. The fates of chicken nuclear lamin proteins during mitosis: evidence for a reversible redistribution of lamin B2 between inner nuclear membrane and elements of the endoplasmic reticulum. Stick, R., Angres, B., Lehner, C.F., Nigg, E.A. J. Cell Biol. (1988) [Pubmed]
  7. Differential expression of nuclear lamin proteins during chicken development. Lehner, C.F., Stick, R., Eppenberger, H.M., Nigg, E.A. J. Cell Biol. (1987) [Pubmed]
  8. Nuclear envelope breakdown requires overcoming the mechanical integrity of the nuclear lamina. Panorchan, P., Schafer, B.W., Wirtz, D., Tseng, Y. J. Biol. Chem. (2004) [Pubmed]
  9. Use of a general purpose mammalian expression vector for studying intracellular protein targeting: identification of critical residues in the nuclear lamin A/C nuclear localization signal. Frangioni, J.V., Neel, B.G. J. Cell. Sci. (1993) [Pubmed]
  10. A second higher vertebrate B-type lamin. cDNA sequence determination and in vitro processing of chicken lamin B2. Vorburger, K., Lehner, C.F., Kitten, G.T., Eppenberger, H.M., Nigg, E.A. J. Mol. Biol. (1989) [Pubmed]
  11. The nuclear lamin protein family in higher vertebrates. Identification of quantitatively minor lamin proteins by monoclonal antibodies. Lehner, C.F., Kurer, V., Eppenberger, H.M., Nigg, E.A. J. Biol. Chem. (1986) [Pubmed]
WikiGenes - Universities