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CNN1  -  calponin 1, basic, smooth muscle

Homo sapiens

Synonyms: Basic calponin, Calponin H1, smooth muscle, Calponin-1, HEL-S-14, SMCC, ...
 
 
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Disease relevance of CNN1

 

High impact information on CNN1

  • RESULTS: The morphology of calponin h1-transfected cells in culture resembled that of cultured normal myometrial smooth muscle cells [5].
  • In assays of anchorage-independent growth and in vivo tumorigenicity, both growth and tumorigenicity were statistically significantly reduced in calponin h1-transfected leiomyosarcoma cells [5].
  • With SK-LMS-1 cells, proliferation of calponin h1-transfection cells was reduced to 69% of control; with SKN cells, calponin h1 transfection reduced proliferation to 70% of control [5].
  • METHODS: A plasmid containing a human calponin h1 complementary DNA and a bacterial neomycin-resistance gene was transfected into the human leiomyosarcoma cell lines SKN and SK-LMS-1 by electroporation [5].
  • The pattern of expression of these two genes contrasted markedly with that of calponin and SM22 alpha, genes expressed predominantly by differentiated smooth muscle cells and whose expression was generally confined to the media of the vessel [6].
 

Chemical compound and disease context of CNN1

  • RESULTS: All renal angiomyolipomas stained positive for HMB-45, HMB-50, NKI/C3, muscle-specific actin (HHF-35), and calponin [7].
  • METHODS: Formalin-fixed and paraffin-embedded specimens from 25 randomly selected patients with renal cell carcinoma were stained with mouse monoclonal antibodies, anti-human CD31, anti-alpha smooth muscle actin (alphaSMA), and anti-human calponin by the indirect immunoperoxidase method [8].
 

Biological context of CNN1

  • In association with this methylation, h2-calponin gene expression was attenuated to the normal level, although other genes in the DS region of chromosome 21 were expressed dose dependently at 1.5 times the normal level [2].
  • Role of H1-calponin in pancreatic AR42J cell differentiation into insulin-producing cells [9].
  • Finally, the localization of SMCC to a defined genomic interval will facilitate an analysis of its potential as a candidate gene for disease phenotypes mapping to 19p13.2 [10].
  • 2. These results provide new information concerning the regulation of SMCC gene expression and demonstrate the utility of two human SMC lines for the further characterization of this gene's expression control [10].
  • Southern blot and PCR analysis of a 70-kb human bacterial artificial chromosome (BAC) revealed a genomic structure (seven exons spanning > 11 kb) very similar to that reported for the mouse SMCC gene [10].
 

Anatomical context of CNN1

 

Associations of CNN1 with chemical compounds

  • High resolution digital confocal studies indicated that calponin redistributes to the cell membrane during phenylephrine stimulation at a time when mitogen-activated protein kinase and protein kinase C-epsilon are targeted to the plasmalemma [13].
  • Here, we identify, for the first time, tyrosine-phosphorylated calponin h3 within COS 7 cells, before and after their transfection with the pSV vector containing cDNA encoding the cytoplasmic, Src-related, tyrosine kinase, Fyn [14].
  • The phosphorylation-dephosphorylation of serine and threonine residues of calponin is known to modulate in vitro its interaction with F-actin and is thought to regulate several biological processes in cells, involving either of the calponin isoforms [14].
  • On the other hand, the SLIM1 expression induced by the 25-HC or 9-cis RA (as well as SM alpha-actin and CNN-1) was decreased by the treatment of 15d-PGJ2 [15].
  • Following photolysis of caged ATP, cells without calponin that contained a nonphosphorylatable RLC shortened at 30% of the velocity and produced 65% of the isometric force of cells reconstituted with the thiophosphorylated RLC [16].
 

Physical interactions of CNN1

  • The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin [17].
  • We report in this study that calponin binds to both ERK1 and ERK2 under native conditions as well as in an overlay assay [18].
  • The major hsp90-binding site is located in the N-terminal (residues 7-144) part of calponin [19].
  • In the present study we demonstrate that calponin binds directly to the regulatory domain of PKC both in overlay assays and, under native conditions, by sedimentation with lipid vesicles [20].
  • The N-terminal actin-binding region consists of two calponin homology domains and is related to the actin-binding domains of a superfamily of proteins including alpha-actinin, spectrin and fimbrin [17].
 

Co-localisations of CNN1

 

Regulatory relationships of CNN1

  • We have also found that calponin can directly activate PKC autophosphorylation [20].
  • In tissue culture, calponin was strongly expressed by fibronectin-expressing fibroblasts from OM, sciatic nerve and skin and by meningeal cells from the OB, but not by p75(NTR)- and S100beta-expressing OECs [21].
  • Calponin inhibits actomyosin Mg2+ ATPase and is proposed to regulate smooth muscle contraction; however, the mechanism by which it exerts its effect and the regulation of its behavior is still under investigation [22].
  • Based primarily on the results of these motility studies, a qualitative model is proposed in which LC20 phosphorylation, tropomyosin, and caldesmon all regulate fapp and calponin regulates gapp [23].
 

Other interactions of CNN1

 

Analytical, diagnostic and therapeutic context of CNN1

References

  1. Expression of the smooth muscle calponin gene in human osteosarcoma and its possible association with prognosis. Yamamura, H., Yoshikawa, H., Tatsuta, M., Akedo, H., Takahashi, K. Int. J. Cancer (1998) [Pubmed]
  2. A unique downregulation of h2-calponin gene expression in Down syndrome: a possible attenuation mechanism for fetal survival by methylation at the CpG island in the trisomic chromosome 21. Kuromitsu, J., Yamashita, H., Kataoka, H., Takahara, T., Muramatsu, M., Sekine, T., Okamoto, N., Furuichi, Y., Hayashizaki, Y. Mol. Cell. Biol. (1997) [Pubmed]
  3. Reactive stroma in human prostate cancer: induction of myofibroblast phenotype and extracellular matrix remodeling. Tuxhorn, J.A., Ayala, G.E., Smith, M.J., Smith, V.C., Dang, T.D., Rowley, D.R. Clin. Cancer Res. (2002) [Pubmed]
  4. Distribution of calponin and smooth muscle myosin heavy chain in fine-needle aspiration biopsies of the breast. Dabbs, D.J., Gown, A.M. Diagn. Cytopathol. (1999) [Pubmed]
  5. Possible role of calponin h1 as a tumor suppressor in human uterine leiomyosarcoma. Horiuchi, A., Nikaido, T., Taniguchi, S., Fujii, S. J. Natl. Cancer Inst. (1999) [Pubmed]
  6. High expression of genes for calcification-regulating proteins in human atherosclerotic plaques. Shanahan, C.M., Cary, N.R., Metcalfe, J.C., Weissberg, P.L. J. Clin. Invest. (1994) [Pubmed]
  7. Renal angiomyolipoma: further immunophenotypic characterization of an expanding morphologic spectrum. Stone, C.H., Lee, M.W., Amin, M.B., Yaziji, H., Gown, A.M., Ro, J.Y., Têtu, B., Paraf, F., Zarbo, R.J. Arch. Pathol. Lab. Med. (2001) [Pubmed]
  8. Immature tumor angiogenesis in high-grade and high-stage renal cell carcinoma. Kinouchi, T., Mano, M., Matsuoka, I., Kodama, S., Aoki, T., Okamoto, M., Yamamura, H., Usami, M., Takahashi, K. Urology (2003) [Pubmed]
  9. Role of H1-calponin in pancreatic AR42J cell differentiation into insulin-producing cells. Morioka, T., Koyama, H., Yamamura, H., Tanaka, S., Fukumoto, S., Emoto, M., Mizuguchi, H., Hayakawa, T., Kojima, I., Takahashi, K., Nishizawa, Y. Diabetes (2003) [Pubmed]
  10. Expression, genomic structure and high resolution mapping to 19p13.2 of the human smooth muscle cell calponin gene. Miano, J.M., Krahe, R., Garcia, E., Elliott, J.M., Olson, E.N. Gene (1997) [Pubmed]
  11. Synergistic roles of platelet-derived growth factor-BB and interleukin-1beta in phenotypic modulation of human aortic smooth muscle cells. Chen, C.N., Li, Y.S., Yeh, Y.T., Lee, P.L., Usami, S., Chien, S., Chiu, J.J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  12. The presence of h2-calponin in human keratinocyte. Fukui, Y., Masuda, H., Takagi, M., Takahashi, K., Kiyokane, K. J. Dermatol. Sci. (1997) [Pubmed]
  13. Calponin and mitogen-activated protein kinase signaling in differentiated vascular smooth muscle. Menice, C.B., Hulvershorn, J., Adam, L.P., Wang, C.A., Morgan, K.G. J. Biol. Chem. (1997) [Pubmed]
  14. Tyrosine phosphorylation of calponins. Inhibition of the interaction with F-actin. Abouzaglou, J., Bénistant, C., Gimona, M., Roustan, C., Kassab, R., Fattoum, A. Eur. J. Biochem. (2004) [Pubmed]
  15. Up-regulation of skeletal muscle LIM protein 1 gene by 25-hydroxycholesterol may mediate morphological changes of rat aortic smooth muscle cells. Kang, M.A., Jeoung, N.H., Kim, J.Y., Lee, J.E., Jung, U.J., Choi, M.S., Lee, W.H., Kwon, O.S., Lee, H., Park, Y.B. Life Sci. (2007) [Pubmed]
  16. Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed. Malmqvist, U., Trybus, K.M., Yagi, S., Carmichael, J., Fay, F.S. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  17. The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin. Keep, N.H., Norwood, F.L., Moores, C.A., Winder, S.J., Kendrick-Jones, J. J. Mol. Biol. (1999) [Pubmed]
  18. Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins. Leinweber, B.D., Leavis, P.C., Grabarek, Z., Wang, C.L., Morgan, K.G. Biochem. J. (1999) [Pubmed]
  19. Heat shock protein (hsp90) interacts with smooth muscle calponin and affects calponin-binding to actin. Ma, Y., Bogatcheva, N.V., Gusev, N.B. Biochim. Biophys. Acta (2000) [Pubmed]
  20. Regulation of protein kinase C by the cytoskeletal protein calponin. Leinweber, B., Parissenti, A.M., Gallant, C., Gangopadhyay, S.S., Kirwan-Rhude, A., Leavis, P.C., Morgan, K.G. J. Biol. Chem. (2000) [Pubmed]
  21. Calponin is expressed by fibroblasts and meningeal cells but not olfactory ensheathing cells in the adult peripheral olfactory system. Ibanez, C., Ito, D., Zawadzka, M., Jeffery, N.D., Franklin, R.J. Glia (2007) [Pubmed]
  22. Smooth muscle calponin-caltropin interaction: effect on biological activity and stability of calponin. Wills, F.L., McCubbin, W.D., Kay, C.M. Biochemistry (1994) [Pubmed]
  23. A model for the coregulation of smooth muscle actomyosin by caldesmon, calponin, tropomyosin, and the myosin regulatory light chain. Haeberle, J.R., Hemric, M.E. Can. J. Physiol. Pharmacol. (1994) [Pubmed]
  24. Expression of smooth muscle calponin in tumor vessels of human hepatocellular carcinoma and its possible association with prognosis. Sasaki, Y., Yamamura, H., Kawakami, Y., Yamada, T., Hiratsuka, M., Kameyama, M., Ohigashi, H., Ishikawa, O., Imaoka, S., Ishiguro, S., Takahashi, K. Cancer (2002) [Pubmed]
  25. A critical role for calponin 2 in vascular development. Tang, J., Hu, G., Hanai, J., Yadlapalli, G., Lin, Y., Zhang, B., Galloway, J., Bahary, N., Sinha, S., Thisse, B., Thisse, C., Jin, J.P., Zon, L.I., Sukhatme, V.P. J. Biol. Chem. (2006) [Pubmed]
  26. Profiling molecular targets of TGF-beta1 in prostate fibroblast-to-myofibroblast transdifferentiation. Untergasser, G., Gander, R., Lilg, C., Lepperdinger, G., Plas, E., Berger, P. Mech. Ageing Dev. (2005) [Pubmed]
  27. Molecular cloning and gene mapping of human basic and acidic calponins. Maguchi, M., Nishida, W., Kohara, K., Kuwano, A., Kondo, I., Hiwada, K. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  28. The prostacyclin receptor induces human vascular smooth muscle cell differentiation via the protein kinase A pathway. Fetalvero, K.M., Shyu, M., Nomikos, A.P., Chiu, Y.F., Wagner, R.J., Powell, R.J., Hwa, J., Martin, K.A. Am. J. Physiol. Heart Circ. Physiol. (2006) [Pubmed]
  29. The mTOR/p70 S6K1 pathway regulates vascular smooth muscle cell differentiation. Martin, K.A., Rzucidlo, E.M., Merenick, B.L., Fingar, D.C., Brown, D.J., Wagner, R.J., Powell, R.J. Am. J. Physiol., Cell Physiol. (2004) [Pubmed]
 
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