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Jsrp1  -  junctional sarcoplasmic reticulum protein 1

Mus musculus

Synonyms: 2300003C06Rik, 2310032K21Rik, JP-45, JP45, Jp45, ...
 
 
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High impact information on Jsrp1

 

Anatomical context of Jsrp1

  • The functional effect of JP-45 on Cav1.1 activity was assessed by investigating charge movement in differentiated C2C12 myotubes after overexpression or depletion of JP-45 [3].
  • Quantitative and qualitative analysis of structural changes in the overexpressing as well as in the normally differentiating myocardium illustrate the synthetic pathways and the events in the targeting and delivery of CSQ and JNC to the jSR of the differentiating cardiac myocyte [4].
 

Associations of Jsrp1 with chemical compounds

  • Both these values exceed the limit of resolution of the optical system, but their similarity suggests that at high [EGTA] the Ca(2+) domains in adult mammalian muscle fibers are confined to Ca(2+) release sites located at the junctional sarcoplasmic reticulum (SR) [5].
  • Extracellular Na(+) removal lead to Ca(2+) accumulation in the JSR inducing further SR-Ca(2+) release and increased energy release [6].
 

Analytical, diagnostic and therapeutic context of Jsrp1

  • Western blot analysis revealed that isolated triads contained the integral membrane subunits gp91(phox) and p22(phox), which were markedly enriched in isolated transverse tubules but absent from junctional sarcoplasmic reticulum vesicles [7].

References

  1. Compensatory mechanisms associated with the hyperdynamic function of phospholamban-deficient mouse hearts. Chu, G., Luo, W., Slack, J.P., Tilgmann, C., Sweet, W.E., Spindler, M., Saupe, K.W., Boivin, G.P., Moravec, C.S., Matlib, M.A., Grupp, I.L., Ingwall, J.S., Kranias, E.G. Circ. Res. (1996) [Pubmed]
  2. Dyspedic mouse skeletal muscle expresses major elements of the triadic junction but lacks detectable ryanodine receptor protein and function. Buck, E.D., Nguyen, H.T., Pessah, I.N., Allen, P.D. J. Biol. Chem. (1997) [Pubmed]
  3. The junctional SR protein JP-45 affects the functional expression of the voltage-dependent Ca2+ channel Cav1.1. Anderson, A.A., Altafaj, X., Zheng, Z., Wang, Z.M., Delbono, O., Ronjat, M., Treves, S., Zorzato, F. J. Cell. Sci. (2006) [Pubmed]
  4. 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]
  5. Calcium release domains in mammalian skeletal muscle studied with two-photon imaging and spot detection techniques. Gómez, J., Neco, P., DiFranco, M., Vergara, J.L. J. Gen. Physiol. (2006) [Pubmed]
  6. Energetics of Na(+)-Ca(2+) exchange in resting cardiac muscle. Ponce-Hornos, J.E., Philipson, K.D., Bonazzola, P., Langer, G.A. Biophys. J. (1999) [Pubmed]
  7. A transverse tubule NADPH oxidase activity stimulates calcium release from isolated triads via ryanodine receptor type 1 S -glutathionylation. Hidalgo, C., Sánchez, G., Barrientos, G., Aracena-Parks, P. J. Biol. Chem. (2006) [Pubmed]
 
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