The effects of mutated skeletal ryanodine receptors on calreticulin and calsequestrin expression in the brain and pituitary gland of boars

Molecular Brain Research

Volumn 75, Issue 1, 2000, Pages 46-53

  Weaver, Shelley A ^a   Schaefer, Allan L ^b   Dixon, Walter T ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

^b LACOMBE RESEARCH CENTRE   (Canada)

Author keywords

Brain; Calreticulin; Calsequestrin; Malignant hyperthermia; Porcine stress syndrome; Skeletal ryanodine receptor

Indexed keywords

CALCIUM BINDING PROTEIN; CALRETICULIN; CALSEQUESTRIN; MUTANT PROTEIN; RYANODINE RECEPTOR;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BRAIN REGION; CONTROLLED STUDY; GENOTYPE; HYPOPHYSIS; IN SITU HYBRIDIZATION; MALE; MALIGNANT HYPERTHERMIA; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STRESS; SWINE; WESTERN BLOTTING;

ANIMALS; BONE AND BONES; BRAIN; CALCIUM-BINDING PROTEINS; CALRETICULIN; CALSEQUESTRIN; FRONTAL LOBE; GENE EXPRESSION REGULATION; HETEROZYGOTE; HIPPOCAMPUS; HYPOTHALAMUS; MALE; MUTATION; PITUITARY GLAND; PROTEIN ISOFORMS; RIBONUCLEOPROTEINS; RNA, MESSENGER; RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL; SWINE;

EID: 0033954582     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(99)00289-2     Document Type: Article

References (43)

1. Adeola O., Ball R.O., House J.D., O'Brien P.J. Regional brain neurotransmitter concentrations in stress-susceptible pigs. J. Anim. Sci. 71:1993;968-974.
2. 2+ binding domains. J. Biol. Chem. 266:1991;21458-21465.
3. R.L. Barchi, The muscle fiber and disorders of muscle excitability, in: G.J. Siegel, B.W. Agranoff, R.W. Albera, P.B. Molinoff (Eds.), Basic Neurochemistry, fifth edn., Raven Press, New York, 1994, pp. 703-722.
4. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
5. Burns K., Duggan B., Atkinson E.A., Famulski K.S., Nemer M., Bleackley R.C., Michalak M. Modulation of gene expression by calreticulin binding to the glucocorticoid receptor. Nature. 367:1994;476-483.
6. Burns K., Opas M., Michalak M. Calreticulin inhibits glucocorticoid but not cAMP-sensitive expression of tyrosine aminotransferase gene in cultured McA-RH7777 hepatocytes. Mol. Cell. Biochem. 171:1997;37-43.
7. Canadian Council on Animal Care, E.D. Olfert, B.M. Cross, A.A. McWilliams (Eds.), A guide to the care and use of experimental animals, Vol. 1, 2nd edn., Canadian Council on Animal Care, Ottawa, 1993.
8. Dedhar S., Rennie P., Shago M., Leung-Hagestein C.Y., Yang H., Filmus J., Hawley R.G., Bruchovsky N., Cheng H., Matusik R.J., Giguere V. Inhibition of nuclear hormone receptor activity by calreticulin. Nature. 367:1994;480-483.
9. 2+ release. J. Biol. Chem. 272:1997;20967-20970.
10. Ervasti J.M., Mickelson J.R., Louis C.F. Transverse tubule calcium regulation in malignant hyperthermia. Arch. Biochem. Biophys. 269:1989;497-506.
11. Fletcher J.E., Tripolitis L., Hubert M., Vita G.M., Levitt R.C., Rosenberg H. Genotype and phenotype relationships for mutations in the ryanodine receptor in patients referred for diagnosis of malignant hyperthermia. Br. J. Anaesth. 75:1995;307-310.
12. Fujii J., Otsu K., Zorzato F., De Leon S., Khanna V., Weiler J., O'Brien P.J., MacLennan D.H. Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia. Science. 253:1991;448-451.
13. 2+ release channels are differentially expressed in rabbit brain. J. Neurosci. 14:1994;4794-4805.
14. Guan S.H., Falick A.M., Williams D.E., Cashman J.R. Evidence for complex formation between rabbit flavin-containing monooxygenase and calreticulin. Biochemistry. 30:1991;9892-9900.
15. Hails M.R. Transport stress in animals: a review. Anim. Reg. Stud. 1:1978;289-343.
16. Ledbetter M.W., Preiner J.K., Louis C.F., Mickelson J.R. Tissue distribution of ryanodine receptor isoforms and alleles determined by reverse transcription polymerase chain reaction. J. Biol. Chem. 269:1994;31544-31551.
17. Leung-Hagesteijn C.Y., Milankov K., Michalak M., Wilkins J., Dedhar S. Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin alpha-subunit-binding protein. J. Cell Sci. 107:1994;589-600.
18. 2+ release from internal stores: role in generating depolarizing after-potentials in rat supraoptic neurons. J. Physiol. 498.2:1997;339-350.
19. D. Lister, The physiology and biochemistry of the porcine stress syndrome, in: P.V. Tarrant, G. Eikelenboom, G. Monin (Eds.), Evaluation and Control of Meat Quality in Pigs, Martinus Nijhoff Publishers, Boston, 1987, pp. 3-16.
20. Llewellyn D.H., Sheikh F.N., Kendall J.M., Campbell A.K. Upregulation of calreticulin expression in HeLa cells by calcium-stress. Biochem. Soc. Trans. 23:1995;330S.
21. 2+ store and inhibition of N-linked glycosylation. Biochem. J. 318:1996;555-560.
22. J. Lytton, D.H. MacLennan, The sarcoplasmic reticulum, in: H.A. Bozzard, E. Haber, R.B. Jennings, A.M. Katz, H.E. Morgan (Eds.), The Heart and Cardiovascular System, Raven Press, New York, 1991, pp. 1203-1222.
23. MacLennan D.H., Philips M.S. Malignant hyperthermia. Science. 256:1992;789-794.
24. Martin C., Chapman K.E., Seckl J.R., Ashley R.H. Partial cloning and differential expression of ryanodine receptor calcium-release channel genes in human tissues including the hippocampus and cerebellum. Neuroscience. 85:1998;205-216.
25. 2+ influx. J. Biol. Chem. 271:1996;9332-9339.
26. Mickelson J.R., Ross J.A., Hyslop R.J., Gallant E.M., Louis C.F. Skeletal muscle sarcolemma in malignant hyperthermia: evidence for a defect in calcium regulation. Biochim. Biophys. Acta. 897:1987;364-376.
27. 2+ regulation defects. Physiol. Rev. 76:1996;537-592.
28. Milner R.E., Baksh S., Shemanko C., Carpenter M.R., Smillie L., Vance J.E., Opas M., Michalak M. Calreticulin and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum. J. Biol. Chem. 266:1991;7155-7163.
29. Murray B.E., Ohlendieck K. Complex formation between calsequestrin and the ryanodine receptor in fast - and slow - twitch rabbit skeletal muscle. FEBS Lett. 429:1998;317-322.
30. Nguyen T.Q., Capra J.D., Sontheimer R.D. Calreticulin is transcriptionally upregulated by heat shock, calcium and heavy metals. Mol. Immunol. 33:1996;379-386.
31. O'Brien P.J., Shen H., Corey C.R., Zhang X. Use of a DNA-based test for the mutation associated with porcine stress syndrome (malignant hyperthermia) in 10,000 breeding swine. J. Am. Vet. Med. 203:1993;842-851.
32. Otsu K., Phillips M.S., Khanna V.K., De Leon S., MacLennan D.H. Refinement of diagnostic assays for a probable causal mutation for porcine and human malignant hyperthermia. Genomics. 13:1992;201-214.
33. 2+ stores in chick cerebellum Purkinje neurons: ontogenetic and functional studies. Am. J. Physiol. 269:1995;C1219-1227.
34. 2+ release channels of pigs heterozygous for malignant hyperthermia. Muscle and Nerve. 18:1995;1167-1176.
35. Sundaresan S., Weiss J., Bower-Dantoin A.C., Jameson J.L. Expression of ryanodine receptors in the pituitary gland: evidence for a role in gonadotropin releasing hormone signalling. Endocrinology. 138:1997;2056-2065.
36. Takeshima H., Nishimura S., Matsumoto T., Ishida H., Kangawa K., Minamino N., Matsuo H., Ueda M., Hanaoka M., Hirose T., Numa S. Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor. Nature. 339:1989;439-445.
37. 2+-storage compartments (calcisomes) of liver and brain. Biochem. J. 271:1990;473-480.
38. 2+ binding protein similar to mammalian calreticulin. Biochem. Biophys. Res. Commun. 175:1991;444-450.
39. Waser M., Mesaeli N., Spencer C., Michalak M. Regulation of calreticulin gene expression by calcium. J. Cell Biol. 138:1997;547-557.
40. S.A. Weaver, W.T. Dixon, A.L. Schaefer, The effects of mutated skeletal ryanodine receptors on hypothalamic-pituitary-adrenal axis function in boars, submitted.
41. S.A. Weaver, A.L. Schaefer, W.T. Dixon, Western blotting for detection of glucocorticoid receptors in the brain and pituitary gland from adrenal-intact pigs, submitted.
42. Yano K., Zarain-Herzberg A. Sarcoplasmic reticulum calsequestrins: structural and functional properties. Mol. Cell. Biochem. 135:1994;61-70.
43. Zhang L., Kelley J., Schmeisser G., Kobayashi Y.M., Jones L.R. Complex formation between junction, triadin, calsequestrin and the ryanodine receptor - proteins of the cardiac junctional sarcoplasmic reticulum membrane. J. Biol. Chem. 272:1997;23389-23397.