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

Cnn1  -  calponin 1, basic, smooth muscle

Rattus norvegicus

Synonyms: Basic calponin, Calponin H1, smooth muscle, Calponin-1
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 Cnn1


High impact information on Cnn1


Biological context of Cnn1

  • Single and double immunocytochemical techniques together with semiquantitative analyses revealed a Cp upregulation in SM at all time frames post-TBI; with the protein migrating from SM cytosol to the vicinity of the cell membrane [1].
  • The molecular basis for the autoregulation of calponin by isoform-specific C-terminal tail sequences [6].
  • Cell phenotype was determined by immunoblot and immunocytofluorescence using antisera specific for the differentiation markers alpha-actin, myosin, calponin, osteopontin, and phospholamban [7].
  • As the 22-kDa fragment contained only T2, the phosphorylation site in T2 appeared to regulate the binding of calponin to F-actin and tropomyosin [8].
  • Here we report on smooth muscle-specific enhancer activity within the first intron of smooth muscle calponin [2].

Anatomical context of Cnn1

  • Removal of the inhibitory tail resulted in an increased binding and bundling activity, and caused a prominent re-localization of h2 CaP from the peripheral actin network to the central actin stress fibers in transfected A7r5 smooth muscle cells [6].
  • Altogether, these results are consistent with an involvement of acidic calponin in dendritic spine plasticity [9].
  • Our data show that the intensity of immunolabeling for acidic calponin was clearly increased in the inner one-third of the molecular layer of the dentate gyrus, the site of mossy fiber sprouting, and neo-synaptogenesis, at 1 and 2 weeks after pilocarpine injection (silent period) when the reorganization was taking place [9].
  • Cloning and expression of a novel acidic calponin isoform from rat aortic vascular smooth muscle [10].
  • To assess the physiological significance and the molecular basis of the calponin-microtubule interaction, we have first studied the solution binding of recombinant acidic calponin to microtubules using quantitative cosedimentation analyses [11].

Associations of Cnn1 with chemical compounds

  • In contrast, in chronic pilocarpine-treated animals, when the reorganization was established, the levels of labeling for acidic calponin in the inner molecular layer were similar to those observed in control rats [9].
  • Structure-function relations of smooth muscle calponin. The critical role of serine 175 [12].
  • These results indicate that the hydroxyl side chain at position 175 of calponin plays a critical role in the binding of calponin to actin and inhibition of the cross-bridge cycling rate [12].
  • The effect of endogenous Ang II on aortic calponin mRNA expression was studied in Goldblatt hypertensive rats with (2K1C model), or without (1K1C model) activation of the renin-angiotensin system [3].
  • Angiotensin II modulates calponin gene expression in rat vascular smooth muscle cells in vivo [3].

Physical interactions of Cnn1

  • Calponin interacts with both the alpha and beta tubulins and only slightly with the tyrosinated and acetylated form of alpha tubulin [13].

Other interactions of Cnn1

  • However, while Cp and Cd in SM remained elevated, their levels in En returned to normal at 48 h post-TBI [1].
  • However, in contrast to SMCs, TGF-beta did not induce expression of h(1) calponin and SM MHC in non-SMCs [14].
  • Several putative functional motifs are present in the protein, including a calponin homology domain, three nuclear localization signals, a consensus P-loop, and a proline-rich region, suggesting that KPL2 has a unique function [15].
  • Immunological analyses and reverse transcriptase-polymerase chain reaction indicated that the differentiated cells expressed smooth-muscle-specific marker proteins such as SM-1, SM-2, and SMemb myosin heavy chains, SM-22, basic calponin and alpha-smooth-muscle actin, but not the astrocyte marker glial fibrillary acidic protein [16].
  • A longitudinal section of myometrium was removed, total RNA was extracted, and semiquantitative reverse transcription-polymerase chain reaction (RT-PCR) was performed for glyceraldehyde phosphate dehydrogenase (GAPDH), calponin, EP2, and FP receptor mRNA expression [17].

Analytical, diagnostic and therapeutic context of Cnn1


  1. Calponin and caldesmon cellular domains in reacting microvessels following traumatic brain injury. Kreipke, C.W., Morgan, N.C., Petrov, T., Rafols, J.A. Microvasc. Res. (2006) [Pubmed]
  2. Serum response factor-dependent regulation of the smooth muscle calponin gene. Miano, J.M., Carlson, M.J., Spencer, J.A., Misra, R.P. J. Biol. Chem. (2000) [Pubmed]
  3. Angiotensin II modulates calponin gene expression in rat vascular smooth muscle cells in vivo. Castoldi, G., di Gioia, C.R., Pieruzzi, F., van De Greef, W.M., Busca, G., Sperti, G., Stella, A. J. Hypertens. (2001) [Pubmed]
  4. Hyperplasia of myoepithelial cells expressing calponin during atrophy of the rat parotid gland induced by duct ligation. Miguel, M.C., Andrade, E.S., Taga, R., Pinto, L.P., Souza, L.B. Histochem. J. (2002) [Pubmed]
  5. Calponin repeats regulate actin filament stability and formation of podosomes in smooth muscle cells. Gimona, M., Kaverina, I., Resch, G.P., Vignal, E., Burgstaller, G. Mol. Biol. Cell (2003) [Pubmed]
  6. The molecular basis for the autoregulation of calponin by isoform-specific C-terminal tail sequences. Burgstaller, G., Kranewitter, W.J., Gimona, M. J. Cell. Sci. (2002) [Pubmed]
  7. Phenotype dictates the growth response of vascular smooth muscle cells to pulse pressure in vitro. Cappadona, C., Redmond, E.M., Theodorakis, N.G., McKillop, I.H., Hendrickson, R., Chhabra, A., Sitzmann, J.V., Cahill, P.A. Exp. Cell Res. (1999) [Pubmed]
  8. Identification of the regulatory site in smooth muscle calponin that is phosphorylated by protein kinase C. Nakamura, F., Mino, T., Yamamoto, J., Naka, M., Tanaka, T. J. Biol. Chem. (1993) [Pubmed]
  9. Increased levels of acidic calponin during dendritic spine plasticity after pilocarpine-induced seizures. Ferhat, L., Esclapez, M., Represa, A., Fattoum, A., Shirao, T., Ben-Ari, Y. Hippocampus. (2003) [Pubmed]
  10. Cloning and expression of a novel acidic calponin isoform from rat aortic vascular smooth muscle. Applegate, D., Feng, W., Green, R.S., Taubman, M.B. J. Biol. Chem. (1994) [Pubmed]
  11. Mapping the microtubule binding regions of calponin. Fattoum, A., Roustan, C., Smyczynski, C., Der Terrossian, E., Kassab, R. Biochemistry (2003) [Pubmed]
  12. Structure-function relations of smooth muscle calponin. The critical role of serine 175. Tang, D.C., Kang, H.M., Jin, J.P., Fraser, E.D., Walsh, M.P. J. Biol. Chem. (1996) [Pubmed]
  13. Identification of the binding region of basic calponin on alpha and beta tubulins. Fujii, T., Koizumi, Y. J. Biochem. (1999) [Pubmed]
  14. Similarities and differences in smooth muscle alpha-actin induction by TGF-beta in smooth muscle versus non-smooth muscle cells. Hautmann, M.B., Adam, P.J., Owens, G.K. Arterioscler. Thromb. Vasc. Biol. (1999) [Pubmed]
  15. Cloning and characterization of KPL2, a novel gene induced during ciliogenesis of tracheal epithelial cells. Ostrowski, L.E., Andrews, K., Potdar, P., Matsuura, H., Jetten, A., Nettesheim, P. Am. J. Respir. Cell Mol. Biol. (1999) [Pubmed]
  16. Contractile responses of smooth muscle cells differentiated from rat neural stem cells. Oishi, K., Ogawa, Y., Gamoh, S., Uchida, M.K. J. Physiol. (Lond.) (2002) [Pubmed]
  17. Changes in expression of contractile FP and relaxatory EP2 receptors in pregnant rat myometrium during late gestation, at labor, and postpartum. Brodt-Eppley, J., Myatt, L. Biol. Reprod. (1998) [Pubmed]
  18. The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin. Fontao, L., Geerts, D., Kuikman, I., Koster, J., Kramer, D., Sonnenberg, A. J. Cell. Sci. (2001) [Pubmed]
  19. Distribution of caldesmon and of the acidic isoform of calponin in cultured cerebellar neurons and in different regions of the rat brain: an immunofluorescence and confocal microscopy study. Represa, A., Trabelsi-Terzidis, H., Plantier, M., Fattoum, A., Jorquera, I., Agassandian, C., Ben-Ari, Y., der Terrossian, E. Exp. Cell Res. (1995) [Pubmed]
  20. Expression of an acidic isoform of calponin in rat brain: western blots on one- or two-dimensional gels and immunolocalization in cultured cells. Trabelsi-Terzidis, H., Fattoum, A., Represa, A., Dessi, F., Ben-Ari, Y., der Terrossian, E. Biochem. J. (1995) [Pubmed]
  21. Characterization of smooth muscle cell and pericyte differentiation in the rat retina in vivo. Hughes, S., Chan-Ling, T. Invest. Ophthalmol. Vis. Sci. (2004) [Pubmed]
WikiGenes - Universities