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Gene Review

Casq1  -  calsequestrin 1

Mus musculus

Synonyms: CSQ, CSQ-1, CSQ1, Calmitine, Calsequestrin, skeletal muscle isoform, ...
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Disease relevance of Casq1


High impact information on Casq1


Chemical compound and disease context of Casq1

  • Transgenic mice with cardiac-targeted calsequestrin overexpression show marked suppression of Ca(2+)-induced Ca(2+) release, myocyte hypertrophy, and premature death by 16 weeks of age (Jones, L. R., Suzuki, Y. J., Wang, W., Kobayashi, Y. M., Ramesh, V., Franzini-Armstrong, C., Cleemann, L., and Morad, M. (1998) J. Clin. Invest. 101, 1385-1393) [8].

Biological context of Casq1


Anatomical context of Casq1


Associations of Casq1 with chemical compounds

  • The mRNA levels of angiotensin II type1a receptor which requires AP-1 and GATA-4 for gene transcription was suppressed in CSQ overexpressing hearts [10].
  • Calsequestrin (CSQ) is a high capacity Ca(2+)-binding protein present in the lumen of sarcoplasmic reticulum (SR) in striated muscle cells and has been shown to regulate the ryanodine receptor Ca(2+) release channel activity through interaction with other proteins present in the SR [14].
  • These results indicate that the aspartate-rich segment of CSQ, under conditions of overexpression, can sustain structural interactions that interfere with the SOCE mechanism [14].
  • CS (calsequestrin) is an acidic glycoprotein of the SR (sarcoplasmic reticulum) lumen and plays a crucial role in the storage of Ca2+ and in excitation-contraction coupling of skeletal muscles [13].
  • This apparent lower responsiveness of ICa to cAMP could be reversed by the non-hydrolysable cAMP analogue 8-Br-cAMP or the phosphodiesterase inhibitor IBMX, suggesting high phosphodiesterase activity of CSQ myocytes [3].

Physical interactions of Casq1

  • Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction [15].

Other interactions of Casq1


Analytical, diagnostic and therapeutic context of Casq1


  1. Regulation of Ca2+ signaling in transgenic mouse cardiac myocytes overexpressing calsequestrin. Jones, L.R., Suzuki, Y.J., Wang, W., Kobayashi, Y.M., Ramesh, V., Franzini-Armstrong, C., Cleemann, L., Morad, M. J. Clin. Invest. (1998) [Pubmed]
  2. Rescue of contractile parameters and myocyte hypertrophy in calsequestrin overexpressing myocardium by phospholamban ablation. Sato, Y., Kiriazis, H., Yatani, A., Schmidt, A.G., Hahn, H., Ferguson, D.G., Sako, H., Mitarai, S., Honda, R., Mesnard-Rouiller, L., Frank, K.F., Beyermann, B., Wu, G., Fujimori, K., Dorn, G.W., Kranias, E.G. J. Biol. Chem. (2001) [Pubmed]
  3. Remodelling of ionic currents in hypertrophied and failing hearts of transgenic mice overexpressing calsequestrin. Knollmann, B.C., Knollmann-Ritschel, B.E., Weissman, N.J., Jones, L.R., Morad, M. J. Physiol. (Lond.) (2000) [Pubmed]
  4. Cardiac-specific overexpression of calsequestrin results in left ventricular hypertrophy, depressed force-frequency relation and pulsus alternans in vivo. Schmidt, A.G., Kadambi, V.J., Ball, N., Sato, Y., Walsh, R.A., Kranias, E.G., Hoit, B.D. J. Mol. Cell. Cardiol. (2000) [Pubmed]
  5. Changes in calcium cycling precede cardiac dysfunction during autoimmune myocarditis in mice. Stull, L.B., Matteo, R.G., Sweet, W.E., Damron, D.S., Schomisch Moravec, C. J. Mol. Cell. Cardiol. (2001) [Pubmed]
  6. The L-type calcium channel inhibitor diltiazem prevents cardiomyopathy in a mouse model. Semsarian, C., Ahmad, I., Giewat, M., Georgakopoulos, D., Schmitt, J.P., McConnell, B.K., Reiken, S., Mende, U., Marks, A.R., Kass, D.A., Seidman, C.E., Seidman, J.G. J. Clin. Invest. (2002) [Pubmed]
  7. A transgenic myogenic cell line lacking ryanodine receptor protein for homologous expression studies: reconstitution of Ry1R protein and function. Moore, R.A., Nguyen, H., Galceran, J., Pessah, I.N., Allen, P.D. J. Cell Biol. (1998) [Pubmed]
  8. Defective beta-adrenergic receptor signaling precedes the development of dilated cardiomyopathy in transgenic mice with calsequestrin overexpression. Cho, M.C., Rapacciuolo, A., Koch, W.J., Kobayashi, Y., Jones, L.R., Rockman, H.A. J. Biol. Chem. (1999) [Pubmed]
  9. Cloning of the genes encoding mouse cardiac and skeletal calsequestrins: expression pattern during embryogenesis. Park, K.W., Goo, J.H., Chung, H.S., Kim, H., Kim, D.H., Park, W.J. Gene (1998) [Pubmed]
  10. Regulation of GATA-4 and AP-1 in transgenic mice overexpressing cardiac calsequestrin. Suzuki, Y.J., Ikeda, T., Shi, S.S., Kitta, K., Kobayashi, Y.M., Morad, M., Jones, L.R., Blumberg, J.B. Cell Calcium (1999) [Pubmed]
  11. Cardiac-specific overexpression of mouse cardiac calsequestrin is associated with depressed cardiovascular function and hypertrophy in transgenic mice. Sato, Y., Ferguson, D.G., Sako, H., Dorn, G.W., Kadambi, V.J., Yatani, A., Hoit, B.D., Walsh, R.A., Kranias, E.G. J. Biol. Chem. (1998) [Pubmed]
  12. Calsequestrin, a calcium sequestering protein localized at the sarcoplasmic reticulum, is not essential for body-wall muscle function in Caenorhabditis elegans. Cho, J.H., Oh, Y.S., Park, K.W., Yu, J., Choi, K.Y., Shin, J.Y., Kim, D.H., Park, W.J., Hamada, T., Kagawa, H., Maryon, E.B., Bandyopadhyay, J., Ahnn, J. J. Cell. Sci. (2000) [Pubmed]
  13. Vesicle budding from endoplasmic reticulum is involved in calsequestrin routing to sarcoplasmic reticulum of skeletal muscles. Nori, A., Bortoloso, E., Frasson, F., Valle, G., Volpe, P. Biochem. J. (2004) [Pubmed]
  14. A retrograde signal from calsequestrin for the regulation of store-operated Ca2+ entry in skeletal muscle. Shin, D.W., Pan, Z., Kim, E.K., Lee, J.M., Bhat, M.B., Parness, J., Kim, d.o. .H., Ma, J. J. Biol. Chem. (2003) [Pubmed]
  15. Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction. Kobayashi, Y.M., Alseikhan, B.A., Jones, L.R. J. Biol. Chem. (2000) [Pubmed]
  16. Targeted inhibition of beta-adrenergic receptor kinase-1-associated phosphoinositide-3 kinase activity preserves beta-adrenergic receptor signaling and prolongs survival in heart failure induced by calsequestrin overexpression. Perrino, C., Naga Prasad, S.V., Patel, M., Wolf, M.J., Rockman, H.A. J. Am. Coll. Cardiol. (2005) [Pubmed]
  17. Junctin and calsequestrin overexpression in cardiac muscle: the role of junctin and the synthetic and delivery pathways for the two proteins. Tijskens, P., Jones, L.R., Franzini-Armstrong, C. J. Mol. Cell. Cardiol. (2003) [Pubmed]
  18. Surface plasmon resonance studies prove the interaction of skeletal muscle sarcoplasmic reticular Ca(2+) release channel/ryanodine receptor with calsequestrin. Herzog, A., Szegedi, C., Jona, I., Herberg, F.W., Varsanyi, M. FEBS Lett. (2000) [Pubmed]
  19. Tubular aggregates are from whole sarcoplasmic reticulum origin: alterations in calcium binding protein expression in mouse skeletal muscle during aging. Chevessier, F., Marty, I., Paturneau-Jouas, M., Hantaï, D., Verdière-Sahuqué, M. Neuromuscul. Disord. (2004) [Pubmed]
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