Yonsei Med J.  2006 Apr;47(2):207-213. 10.3349/ymj.2006.47.2.207.

Calcium Uptake and Release through Sarcoplasmic Reticulum in the Inferior Oblique Muscles of Patients with Inferior Oblique Overaction

Affiliations
  • 1Department of Ophthalmology, Institute of Vision Research, Yonsei University College of Medicine, Seoul, Korea. 491209@yumc.yonsei.ac.kr
  • 2Department of Ophthalmology, Ajou University School of Medicine, Suwon, Korea.
  • 3Department of Life Science, Kwangju Institute of Science and Technology, Kwangju, Korea.
  • 4Department of Physiology, Inha University College of Medicine, Incheon, Korea.

Abstract

We characterized and compared the characteristics of Ca2+ movements through the sarcoplasmic reticulum of inferior oblique muscles in the various conditions including primary inferior oblique overaction (IOOA), secondary IOOA, and controls, so as to further understand the pathogenesis of primary IOOA. Of 15 specimens obtained through inferior oblique myectomy, six were from primary IOOA, 6 from secondary IOOA, and the remaining 3 were controls from enucleated eyes. Ryanodine binding assays were performed, and Ca2+ uptake rates, calsequestrins and SERCA levels were determined. Ryanodine bindings and sarcoplasmic reticulum Ca2+ uptake rates were significantly decreased in primary IOOA (p < 0.05). Western blot analysis conducted to quantify calsequestrins and SERCA, found no significant difference between primary IOOA, secondary IOOA, and the controls. Increased intracellular Ca2+ concentration due to reduced sarcoplasmic reticulum Ca2+ uptake may play a role in primary IOOA.

Keyword

Calcium; calsequestrin; inferior oblique overaction; ryanodine receptor; sarcoplasmic reticulum; sarcoplasmic reticulum Ca2+ - ATPase 1

MeSH Terms

Sarcoplasmic Reticulum Calcium-Transporting ATPases
Sarcoplasmic Reticulum/*metabolism
Ryanodine Receptor Calcium Release Channel/metabolism
Ryanodine/metabolism
Oxalates/metabolism
Oculomotor Muscles
Ocular Motility Disorders/*metabolism/*pathology
Muscles/*pathology
Models, Statistical
Middle Aged
Male
Humans
Female
Child, Preschool
Child
Calsequestrin/metabolism
Calcium-Transporting ATPases/metabolism
Calcium/metabolism/*pharmacokinetics
Blotting, Western
Aged
Adult
Adolescent

Figure

  • Fig. 1 The expression of calsequestrin in inferior oblique muscles. C, P, and S represent inferior oblique muscles from the controls, and primary and secondary inferior oblique overaction cases, respectively. These three groups were similar with respect to calsequestrin expression.

  • Fig. 2 The expressions of sarco-endoplasmic reticulum Ca2+-ATPase 1 in inferior oblique muscles. C, P, and S represent inferior oblique muscles from the controls, and primary and secondary inferior oblique overaction cases, respectively. No significant difference was found between these three groups in terms of SERCA1 expression.


Reference

1. Von Noorden GK, Campos EC. Binocular vision and ocular motility. 2002. 6th ed. revised. St. Louis London Philadelphia Sydney Toronto: Mosby.
2. Aihara T, Miyata M, Ishikawa S. The lactate dehydrogenase isoenzyme pattern in the overacting inferior oblique muscle. J Pediatr Ophthalmol Strabismus. 1978. 15:43–47.
3. Clark RA, Miller JM, Rosenbaum AL, Demer JL. Heterotropic muscle pulleys or oblique muscle dysfunction? J AAPOS. 1998. 2:17–25.
4. Guibor GP. Synkinetic overaction of the inferior oblique muscle. Am J Ophthalmol. 1949. 32:221–229.
5. Spencer RF, McNeer KW. Structural alterations in overacting inferior oblique muscles. Arch Ophthalmol. 1980. 98:128–133.
6. Block BA, Imagawa T, Campbell KP, Franzini-Armstrong C. Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle. J Cell Biol. 1988. 107(6 Pt 2):2587–2600.
7. Dulhunty AF, Gage PW. Effect of extracellular calcium concentration and dihydropyridines on contraction in mammalian skeletal muscle. J Physiol. 1988. 399:63–80.
8. Meissner G. Ryanodine activation and inhibition of the Ca2+ release channel of sarcoplasmic reticulum. J Biol Chem. 1986. 261:6300–6306.
9. Pessah IN, Warterhouse AL, Casida JE. The calciumryanodine receptor complex of skeletal and cardiac muscle. Biochem Biophys Res Commun. 1985. 128:449–456.
10. Mintz E, Guillian F. Ca2+ transport by the sarcoplasmic reticulum ATPase. Biochim Biophys Acta. 1997. 1318:52–70.
11. Damiani E, Margreth A. Specific protein-protein interaction of calsequestrin with junctional sarcoplasmic reticulum of skeletal muscle. Biochem Biophys Res Commun. 1990. 172:1253–1259.
12. Cheung WY. Calmodulin. Sci Am. 1982. 246:62–70.
13. Coronado R, Morrissette J, Sukhareva M, Vaughn DM. Structure and function of ryanodine receptors. Am J Physiol. 1994. 266(6 Pt 1):C1485–C1504.
14. Jenden DJ, Fairhurst AS. The pharmacology of ryanodine. Pharmacol Rev. 1969. 21:1–25.
15. Jones LR, Zhang L, Sanborn K, Jorgensen AO, Kelley J. Purification, primary structure, and immunological characterization of the 26-kDa calsequestrin binding protein (junctin) from cardiac junctional sarcoplasmic reticulum. J Biol Chem. 1995. 270:30787–30796.
16. Knudson CM, Stang KK, Moomaw CR, Slaughter CA, Campbell KP. Primary structure and topological analysis of a skeletal muscle-specific junctional sarcoplasmic reticulum glycoprotein (triadin). J Biol Chem. 1993. 268:12646–12654.
17. Brillantes AM, Allen P, Takahashi T, Izumo S, Marks AR. Differences in cardiac calcium release channel (ryanodine receptor) expression in myocardium from patients with end-stage heart failure caused by ischemic versus dilated cardiomyopathy. Circ Res. 1992. 71:18–26.
18. Fabiato A. Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum. Am J Physiol. 1983. 245:C1–C14.
19. Gwathmey JK, Copelas L, MacKinnon R, Schoen FJ, Feldman MD, Grossman W, et al. Abnormal intracellular calcium handling in myocardium from patients with end-stage heart failure. Circ Res. 1987. 61:70–76.
20. Go LO, Moschella MC, Watras J, Handa KK, Fyfe BS, Marks AR. Differential regulation of two types of intracellular calcium release channels during end-stage heart failure. J Clin Invest. 1995. 95:888–894.
21. Schillinger W, Meyer M, Kuwajima G, Mikoshiba K, Just H, Hasenfuss G. Unaltered ryanodine receptor protein levels in ischemic cardiomyopathy. Mol Cell Biochem. 1996. 160-161:297–302.
22. Daniel MB, Michael DR, Stuart JE. Protein methods. 1996. 2nd ed. New York: Wiley-Liss publisher.
23. Airey JA, Deerinck TJ, Ellisman MH, Houenou LJ, Ivanenko A, Kenyon JL, et al. Crooked neck dwarf (cn) mutant chicken skeletal muscle cells in low density primary cultures fail to express normal alpha ryanodine receptor and exhibit a partial mutant phenotype. Dev Dyn. 1993. 197:189–202.
24. Riccardo Z, Simonetta RT. The sarcoplasmic reticulum Ca2+ channel/ryanodine receptor: Modulation by endogenous factors, drugs and disease states. Pharmacol Rev. 1997. 49:1–43.
25. Martonosi AN, Beeler TJ. Peachey LD, Adrian RH, Geiger SR, editors. Skeletal muscle. Handbook of physiology. 1983. 3rd ed, revised. Bethesda: American physiological society Press;417–485.
26. Orlova EV, Serysheva II, van Heel M, Hamilton SL, Chiu W. Two structural configurations of the skeletal muscle calcium release channel. Nat Struct Biol. 1996. 3:547–552.
27. Anderson K, Lai FA, Liu QY, Rousseau E, Erikson HP, Meissner G. Structural and functional characterization of the purified cardiac ryanodine receptor-Ca2+ release channel complex. J Biol Chem. 1989. 264:1329–1335.
28. Arai M, Alpert NR, MacLennan DH, Barton P, Periasamy M. Alterations in sarcoplasmic reticulum gene expression in human heart failure. A possible mechanism for alterations in systolic and diastolic properties of the failing myocardium. Circ Res. 1993. 72:463–469.
Full Text Links
  • YMJ
Actions
Cited
CITED
export Copy
Close
Share
  • Twitter
  • Facebook
Similar articles
Copyright © 2024 by Korean Association of Medical Journal Editors. All rights reserved.     E-mail: koreamed@kamje.or.kr