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Gene Review

RYR1  -  ryanodine receptor 1 (skeletal)

Sus scrofa

Synonyms: CRC, RYR
 
 
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Disease relevance of RYR1

 

High impact information on RYR1

 

Chemical compound and disease context of RYR1

 

Biological context of RYR1

  • We screened a porcine bacterial artificial chromosome (BAC) and a P1 derived artificial chromosome (PAC) library to construct a sequence-ready approximately 1.2-Mb BAC/PAC contig of the ryanodine receptor-1 gene (RYR1) region on porcine chromosome (SSC) 6q1 [15].
  • In this report, we describe the genomic organization of a 15.5-kb genomic fragment comprising 18 exons coding for region 4624 to 7929 of the porcine skeletal muscle ryanodine receptor gene [16].
  • The coefficients of correlation for the Nn genotype of the RYR1 gene between the values after slaughter and both the first and the second biopsy for pH1 and EC50 were very low (r = 0.06, r = 0.14; and r = 0.26, r = 0.26; P ? 0.05) [17].
  • Our data suggest that (i) RYR1 gene expression is regulated by at least two novel transcription factors (designated RYREF-1 and RYREF-2), and (ii) tissue specificity results from a transcriptional repression in nonmuscle cells mediated by the first intron [18].
  • Missense mutation analysis indicates that the Lys and Arg residues are essential for calmodulin binding to the synthetic peptide RYR1 PM3 [19].
 

Anatomical context of RYR1

 

Associations of RYR1 with chemical compounds

 

Enzymatic interactions of RYR1

 

Regulatory relationships of RYR1

 

Other interactions of RYR1

 

Analytical, diagnostic and therapeutic context of RYR1

  • This population allowed us to narrow the genetic region harbouring the affected gene(s) and to demonstrate that the region was confined between RYR1 and SW782 (5.7 cM on the National Institute of Animal Industry (NIAI) map and 100 cR on the INRA/University of Minnesota porcine radiation hybrid panel map) [29].
  • In multiplex PCR amplification, two amplicons were simultaneously produced: a 272 bp fragment of RYR1 gene and a 185 bp fragment of ESR gene and were then subjected to "one-tube" restriction enzyme digestion with Hin6 I and Ava I, respectively [24].
  • The tissue distribution of mRNA for ryanodine receptor (ryr) isoforms in various porcine tissues has been determined using the reverse transcription-polymerase chain reaction (RT-PCR) [30].
  • The specific amplification of each of the ryr isoforms was confirmed by restriction enzyme mapping and DNA sequencing [30].
  • Immunoprecipitation of solubilized, [(3)H]azidodantrolene-photolabeled SR protein reveals that the cleaved 160/172 kDa protein remains associated with the C-terminal, 410 kDa portion of the RyR [31].

References

  1. Mutations in the ryanodine receptor gene in central core disease and malignant hyperthermia. Quane, K.A., Healy, J.M., Keating, K.E., Manning, B.M., Couch, F.J., Palmucci, L.M., Doriguzzi, C., Fagerlund, T.H., Berg, K., Ording, H. Nat. Genet. (1993) [Pubmed]
  2. A mutation in the human ryanodine receptor gene associated with central core disease. Zhang, Y., Chen, H.S., Khanna, V.K., De Leon, S., Phillips, M.S., Schappert, K., Britt, B.A., Browell, A.K., MacLennan, D.H. Nat. Genet. (1993) [Pubmed]
  3. Genes specifying receptors for F18 fimbriated Escherichia coli, causing oedema disease and postweaning diarrhoea in pigs, map to chromosome 6. Vögeli, P., Bertschinger, H.U., Stamm, M., Stricker, C., Hagger, C., Fries, R., Rapacz, J., Stranzinger, G. Anim. Genet. (1996) [Pubmed]
  4. The RYR1 g.1843C>T mutation is associated with the effect of the IGF2 intron3-g.3072G>A mutation on muscle hypertrophy. Stinckens, A., Van den Maagdenberg, K., Luyten, T., Georges, M., De Smet, S., Buys, N. Anim. Genet. (2007) [Pubmed]
  5. Discordance, in a malignant hyperthermia pedigree, between in vitro contracture-test phenotypes and haplotypes for the MHS1 region on chromosome 19q12-13.2, comprising the C1840T transition in the RYR1 gene. Deufel, T., Sudbrak, R., Feist, Y., Rübsam, B., Du Chesne, I., Schäfer, K.L., Roewer, N., Grimm, T., Lehmann-Horn, F., Hartung, E.J. Am. J. Hum. Genet. (1995) [Pubmed]
  6. Malignant hyperthermia: excitation-contraction coupling, Ca2+ release channel, and cell Ca2+ regulation defects. Mickelson, J.R., Louis, C.F. Physiol. Rev. (1996) [Pubmed]
  7. Ryanodine receptor gene is a candidate for predisposition to malignant hyperthermia. MacLennan, D.H., Duff, C., Zorzato, F., Fujii, J., Phillips, M., Korneluk, R.G., Frodis, W., Britt, B.A., Worton, R.G. Nature (1990) [Pubmed]
  8. Malignant hyperthermia. MacLennan, D.H., Phillips, M.S. Science (1992) [Pubmed]
  9. Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia. Fujii, J., Otsu, K., Zorzato, F., de Leon, S., Khanna, V.K., Weiler, J.E., O'Brien, P.J., MacLennan, D.H. Science (1991) [Pubmed]
  10. Refinement of diagnostic assays for a probable causal mutation for porcine and human malignant hyperthermia. Otsu, K., Phillips, M.S., Khanna, V.K., de Leon, S., MacLennan, D.H. Genomics (1992) [Pubmed]
  11. Alteration of intracellular Ca2+ transients in COS-7 cells transfected with the cDNA encoding skeletal-muscle ryanodine receptor carrying a mutation associated with malignant hyperthermia. Treves, S., Larini, F., Menegazzi, P., Steinberg, T.H., Koval, M., Vilsen, B., Andersen, J.P., Zorzato, F. Biochem. J. (1994) [Pubmed]
  12. Arg(615)Cys substitution in pig skeletal ryanodine receptors increases activation of single channels by a segment of the skeletal DHPR II-III loop. Gallant, E.M., Curtis, S., Pace, S.M., Dulhunty, A.F. Biophys. J. (2001) [Pubmed]
  13. Increased cardiomyocyte intracellular calcium during endotoxin-induced cardiac dysfunction in guinea pigs. Thompson, M., Kliewer, A., Maass, D., Becker, L., White, D.J., Bryant, D., Arteaga, G., Horton, J., Giroir, B.P. Pediatr. Res. (2000) [Pubmed]
  14. Mg2+ dependence of halothane-induced Ca2+ release from the sarcoplasmic reticulum in skeletal muscle from humans susceptible to malignant hyperthermia. Duke, A.M., Hopkins, P.M., Halsal, J.P., Steele, D.S. Anesthesiology (2004) [Pubmed]
  15. Construction of a 1.2-Mb BAC/PAC contig of the porcine gene RYR1 region on SSC 6q1.2 and comparative analysis with HSA 19q13.13. Martins-Wess, F., Voss-Nemitz, R., Drögemüller, C., Brenig, B., Leeb, T. Genomics (2002) [Pubmed]
  16. Genomic organization of the porcine skeletal muscle ryanodine receptor (RYR1) gene coding region 4624 to 7929. Leeb, T., Schmölzl, S., Brem, G., Brenig, B. Genomics (1993) [Pubmed]
  17. Prediction of meat quality from biopsy in live pigs with different RYR1 genotypes. Kuciel, J., Urban, T., Krenková, L. J. Appl. Genet. (2000) [Pubmed]
  18. Regulation of tissue-specific expression of the skeletal muscle ryanodine receptor gene. Schmoelzl, S., Leeb, T., Brinkmeier, H., Brem, G., Brenig, B. J. Biol. Chem. (1996) [Pubmed]
  19. Identification and characterization of three calmodulin binding sites of the skeletal muscle ryanodine receptor. Menegazzi, P., Larini, F., Treves, S., Guerrini, R., Quadroni, M., Zorzato, F. Biochemistry (1994) [Pubmed]
  20. IVM media, oocyte diameter and donor genotype at RYR1 locus in relation to the incidence of porcine diploid oocytes after maturation in vitro. Lechniak, D., Szczepankiewicz, D., Kauss, D., Szulc, J., Szydłowski, M. Theriogenology (2005) [Pubmed]
  21. Direct detection of calmodulin tuning by ryanodine receptor channel targets using a Ca2+-sensitive acrylodan-labeled calmodulin. Fruen, B.R., Balog, E.M., Schafer, J., Nitu, F.R., Thomas, D.D., Cornea, R.L. Biochemistry (2005) [Pubmed]
  22. A cysteine-for-arginine substitution (R614C) in the human skeletal muscle calcium release channel cosegregates with malignant hyperthermia. Hogan, K., Couch, F., Powers, P.A., Gregg, R.G. Anesth. Analg. (1992) [Pubmed]
  23. Technical note: use of a PCR-single strand conformation polymorphism (PCR-SSCP) for detection of a point mutation in the swine ryanodine receptor (RYR1) gene. Nakajima, E., Matsumoto, T., Yamada, R., Kawakami, K., Takeda, K., Ohnishi, A., Komatsu, M. J. Anim. Sci. (1996) [Pubmed]
  24. Simultaneous identification of ryanodine receptor 1 (RYR1) and estrogen receptor (ESR) genotypes with the multiplex PCR-RFLP method in Polish Large White and Polish Landrace pigs. Kamiński, S., Ruść, A., Wojtasik, K. J. Appl. Genet. (2002) [Pubmed]
  25. Phosphorylation of the porcine skeletal and cardiac muscle sarcoplasmic reticulum ryanodine receptor. Strand, M.A., Louis, C.F., Mickelson, J.R. Biochim. Biophys. Acta (1993) [Pubmed]
  26. Involvement of Ca2+ signaling in tachykinin-mediated contractile responses in swine trachea. Lin, Y.R., Kao, P.C., Chan, M.H. J. Biomed. Sci. (2005) [Pubmed]
  27. Regulation of the RYR1 and RYR2 Ca2+ release channel isoforms by Ca2+-insensitive mutants of calmodulin. Fruen, B.R., Black, D.J., Bloomquist, R.A., Bardy, J.M., Johnson, J.D., Louis, C.F., Balog, E.M. Biochemistry (2003) [Pubmed]
  28. Construction of a porcine YAC library and mapping of the cardiac muscle ryanodine receptor gene to chromosome 14q22-q23. Leeb, T., Rettenberger, G., Hameister, H., Brem, G., Brenig, B. Mamm. Genome (1995) [Pubmed]
  29. Analysis of recessive lethality on swine chromosome 6 in a Göttingen miniature resource family. Mikawa, S., Kishi, H., Ogawa, H., Iga, K., Uenishi, H., Yasue, H. Anim. Genet. (2005) [Pubmed]
  30. Tissue distribution of ryanodine receptor isoforms and alleles determined by reverse transcription polymerase chain reaction. Ledbetter, M.W., Preiner, J.K., Louis, C.F., Mickelson, J.R. J. Biol. Chem. (1994) [Pubmed]
  31. The skeletal muscle ryanodine receptor identified as a molecular target of [3H]azidodantrolene by photoaffinity labeling. Paul-Pletzer, K., Palnitkar, S.S., Jimenez, L.S., Morimoto, H., Parness, J. Biochemistry (2001) [Pubmed]
 
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