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Gene Review

Cald1  -  caldesmon 1

Rattus norvegicus

Synonyms: CDM, L-caldesmon, Non-muscle caldesmon
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Disease relevance of Cald1

  • Calponin and caldesmon cellular domains in reacting microvessels following traumatic brain injury [1].
  • The cellular level of caldesmon 77 in transformed S7-1 cells decreased to about one-third of that in their normal counterparts (cell line no. 7). Essentially the same result was obtained with normal rat kidney cells infected with the temperature-sensitive transformation mutant Schmidt-Ruppin strain of Rous sarcoma virus (68 N2 clone) [2].
  • Neurotoxicity following anoxia or glutamate receptor activation was studied in primary neuronal cultures grown in serum-free, chemically defined CDM R12 medium [3].
  • Both CDM and DCDM induced a dose-dependent mydriasis and bradycardia and DCDM was 10 times more potent than CDM in causing these effects [4].

High impact information on Cald1


Chemical compound and disease context of Cald1

  • The alpha 2-adrenoreceptor antagonist, idazoxan (0.2 mg/kg, i.v.) abolished or reduced CDM- and DCDM-induced mydriasis and bradycardia, whereas the alpha 1-adrenoreceptor antagonist, prazosin (1.5 mg/kg, i.v.) did not change these effects of CDM and DCDM [4].

Biological context of Cald1


Anatomical context of Cald1


Associations of Cald1 with chemical compounds


Physical interactions of Cald1

  • Similar short average lengths are obtained when gelsolin severs actin complexed with low Mr TMs (0.080 +/- 0.045 micron) or with nonmuscle caldesmon (0.11 +/- 0.072 micron) while longer average length (0.22 +/- 0.18 micron) is measured in the presence of high Mr TMs [16].
  • The 145,000- and 240,000-dalton calmodulin-binding bands contained polypeptides that were immunologically similar to caldesmon and to the alpha-subunit of the non-erythroid spectrin (fodrin) respectively [17].

Enzymatic interactions of Cald1

  • We also investigated which of the three putative substrates at the contractile apparatus - MLCK, caldesmon or r-MLC - is phosphorylated by PAK1 in smooth muscle tissue [18].

Regulatory relationships of Cald1

  • Furthermore, the actin binding of gelsolin is strongly inhibited by co-addition of high Mr TMs and nonmuscle caldesmon [16].
  • Caldesmon competes with the Arp2/3 complex for actin binding and thereby inhibits podosome formation. p21-activated kinases (PAK)1 and 2 are also repressors of podosome formation via phosphorylation of caldesmon [19].

Other interactions of Cald1

  • The results suggest that Cp and Cd levels increase while compartmentalizing to specific subcellular domains [1].
  • ERK1/2-mediated phosphorylation of myometrial caldesmon during pregnancy and labor [20].
  • Anti-mitogen-activated protein kinase immunoprecipitates possessed kinase activities toward myelin basic protein and caldesmon, which were activated within 15 minutes after serum stimulation and declined within a few hours [21].
  • In line with this, we found that MLCK was significantly phosphorylated by PAK1 while there was very little 32P incorporation into caldesmon [18].
  • While nonmuscle caldesmon alone or low Mr TMs alone show no significant protection against fragmentation by gelsolin, the low Mr TMs coupled with 83-kDa protein are able to protect actin filaments [16].

Analytical, diagnostic and therapeutic context of Cald1


  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. Occurrence of caldesmon (a calmodulin-binding protein) in cultured cells: comparison of normal and transformed cells. Owada, M.K., Hakura, A., Iida, K., Yahara, I., Sobue, K., Kakiuchi, S. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  3. Attenuation of neurotoxicity following anoxia or glutamate receptor activation in EGF- and hippocampal extract-treated neuronal cultures. Pauwels, P.J., van Assouw, H.P., Leysen, J.E. Cell. Signal. (1989) [Pubmed]
  4. The bradycardic and mydriatic effects of chlordimeform and its demethylated analogs in the rat: antagonism by idazoxan but not by prazosin. Hsu, W.H., Smith, B.E., Hollingworth, R.M. Life Sci. (1988) [Pubmed]
  5. Phosphorylation of non-muscle caldesmon by p34cdc2 kinase during mitosis. Yamashiro, S., Yamakita, Y., Hosoya, H., Matsumura, F. Nature (1991) [Pubmed]
  6. Mitosis-specific phosphorylation causes 83K non-muscle caldesmon to dissociate from microfilaments. Yamashiro, S., Yamakita, Y., Ishikawa, R., Matsumura, F. Nature (1990) [Pubmed]
  7. Localization of caldesmon and its dephosphorylation during cell division. Hosoya, N., Hosoya, H., Yamashiro, S., Mohri, H., Matsumura, F. J. Cell Biol. (1993) [Pubmed]
  8. p38 mitogen-activated protein kinase contributes to the diminished aortic contraction by endothelin-1 in DOCA-salt hypertensive rats. Kim, B., Kim, J., Bae, Y.M., Cho, S.I., Kwon, S.C., Jung, J.Y., Park, J.C., Ahn, H.Y. Hypertension (2004) [Pubmed]
  9. c-Jun N-terminal kinase contributes to norepinephrine-induced contraction through phosphorylation of caldesmon in rat aortic smooth muscle. Lee, Y.R., Lee, C.K., Park, H.J., Kim, H., Kim, J., Kim, J., Lee, K.S., Lee, Y.L., Min, K.O., Kim, B. J. Pharmacol. Sci. (2006) [Pubmed]
  10. Identification and localization of immunoreactive forms of caldesmon in smooth and nonmuscle cells: a comparison with the distributions of tropomyosin and alpha-actinin. Bretscher, A., Lynch, W. J. Cell Biol. (1985) [Pubmed]
  11. Characterization of 83-kilodalton nonmuscle caldesmon from cultured rat cells: stimulation of actin binding of nonmuscle tropomyosin and periodic localization along microfilaments like tropomyosin. Yamashiro-Matsumura, S., Matsumura, F. J. Cell Biol. (1988) [Pubmed]
  12. Role of pp60(c-src) and p(44/42) MAPK in ANG II-induced contraction of rat tonic gastrointestinal smooth muscles. Puri, R.N., Fan, Y.P., Rattan, S. Am. J. Physiol. Gastrointest. Liver Physiol. (2002) [Pubmed]
  13. Regulation of vascular smooth muscle tone by caldesmon. Katsuyama, H., Wang, C.L., Morgan, K.G. J. Biol. Chem. (1992) [Pubmed]
  14. Identification and localization of caldesmon in cardiac muscle. Scott-Woo, G.C., Walsh, M.P., Ikebe, M., Kargacin, G.J. Biochem. J. (1998) [Pubmed]
  15. A mosaic multiple-binding model for the binding of caldesmon and myosin subfragment-1 to actin. Chen, Y.D., Chalovich, J.M. Biophys. J. (1992) [Pubmed]
  16. Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of protective ability of tropomyosins by 83-kDa nonmuscle caldesmon. Ishikawa, R., Yamashiro, S., Matsumura, F. J. Biol. Chem. (1989) [Pubmed]
  17. Developmental pattern of calmodulin-binding proteins in rat jejunal epithelial cells. Rochette-Egly, C., Haffen, K. Differentiation (1987) [Pubmed]
  18. Inhibition of contraction and myosin light chain phosphorylation in guinea-pig smooth muscle by p21-activated kinase 1. Wirth, A., Schroeter, M., Kock-Hauser, C., Manser, E., Chalovich, J.M., De Lanerolle, P., Pfitzer, G. J. Physiol. (Lond.) (2003) [Pubmed]
  19. Changes in the balance between caldesmon regulated by p21-activated kinases and the Arp2/3 complex govern podosome formation. Morita, T., Mayanagi, T., Yoshio, T., Sobue, K. J. Biol. Chem. (2007) [Pubmed]
  20. ERK1/2-mediated phosphorylation of myometrial caldesmon during pregnancy and labor. Li, Y., Je, H.D., Malek, S., Morgan, K.G. Am. J. Physiol. Regul. Integr. Comp. Physiol. (2003) [Pubmed]
  21. Smooth muscle cell proliferation. Expression and kinase activities of p34cdc2 and mitogen-activated protein kinase homologues. Watson, M.H., Venance, S.L., Pang, S.C., Mak, A.S. Circ. Res. (1993) [Pubmed]
  22. Bladder smooth muscle cell phenotypic changes and implication of expression of contractile proteins (especially caldesmon) in rats after partial outlet obstruction. Matsumoto, S., Hanai, T., Ohnishi, N., Yamamoto, K., Kurita, T. International journal of urology : official journal of the Japanese Urological Association. (2003) [Pubmed]
  23. Mutant Caldesmon lacking cdc2 phosphorylation sites delays M-phase entry and inhibits cytokinesis. Yamashiro, S., Chern, H., Yamakita, Y., Matsumura, F. Mol. Biol. Cell (2001) [Pubmed]
  24. Morphological and biochemical analyses of contractile proteins (actin, myosin, caldesmon and tropomyosin) in normal and transformed cells. Tanaka, J., Watanabe, T., Nakamura, N., Sobue, K. J. Cell. Sci. (1993) [Pubmed]
  25. 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]
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