J Korean Ophthalmol Soc.  2009 Aug;50(8):1259-1265. 10.3341/jkos.2009.50.8.1259.

The Changes in Myosin Heavy Chain Isoforms After Extraocular Muscle Recession in Rabbits

Affiliations
  • 1Department of Ophthalmology, Samsung Medical Center, Sungkyunkwan University School of Medicine, Seoul, Korea. syoh@skku.edu

Abstract

PURPOSE
To study the changes in the amount and isoform pattern of the myosin heavy chain (MyHC) in rabbit extraocular muscle (EOM) fibers after recession. METHODS: Sixteen New Zealand white rabbits were used. Recession surgery was performed on the right superior rectus (SR) muscle by 3 mm in eight rabbits, and performed by 8 mm in other eight rabbits. The left SR muscles were left intact as the control groups. The SR muscles in both eyes were harvested from two rabbits from each recession group at 3 days and 1, 2, and 4 weeks after surgery. The changes in MyHC amount and isoform pattern were analyzed by gel electrophoresis. RESULTS: Total MyHC content decreased from 1 week after surgery in the 3-mm recessed group and from 3 days in the 8-mm group. The type IIb MyHC (MyHCIIb) plus EOM-specific MyHC (MyHCeom) showed similar proportional changes to the total MyHC at the different time points after surgery. CONCLUSIONS: The fast MyHCIIb plus the superfast MyHCeom decreased after EOM recession, and these results appear to be related to the changes in the global layer rather than in the orbital one. This suggests that the global layer might be the fast and the superfast twitch portions of rabbit EOM, which perform the fast saccades in ocular movements.

Keyword

Extraocular muscle; Global layer; Myosin heavy chain; Orbital layer; Recession

MeSH Terms

Electrophoresis
Eye
Muscles
Myosin Heavy Chains
Myosins
Orbit
Protein Isoforms
Rabbits
Saccades
Myosin Heavy Chains
Myosins
Protein Isoforms

Figure

  • Figure 1. SDS gel electrophoresis of rabbit ocular muscle. (A)Silver-stained electrophoretogram of myosin heavy chain (MyHC) isoforms in each two superior rectus (SR) muscles, which were harvested at 3 days, 1, 2, and 4 weeks after recession surgery, two naive SR muscles (control), two gastrocnemius muscles (GA), and two soleus muscles (Sol). The type IIb MyHC (MyHCIIb) and the EOM-specific MyHC (MyHCeom) could not be resolved in these electrophoresis bands. (B) The amount of MyHC isoforms quantified by densitometry.

  • Figure 2. Changes in the total myosin heavy chain (MyHC) content and in the composition of MyHC isoforms after 3-mm recession of the superior rectus (SR) muscle. (A)The total MyHC content showed no difference from the control 3 days after surgery, but decreased gradually to be 13.2 %, 24.7 % and 25.4 % lower than in the control 1 week, 2 and 4 weeks after surgery, respectively. (B) Only the proportion of MyHCIIb plus MyHCeom remained at lower level than the control at the different time points after surgery.

  • Figure 3. Changes in the total myosin heavy chain (MyHC) content and in the composition of MyHC isoforms after 8-mm recession of the superior rectus (SR) muscle. (A) The total MyHC content decreased to be 26.3 % lower than in the control 3 days after surgery and remained at this lower level (between 16.1 % and 32.1 %) for 4 weeks after surgery. (B) The proportions of MyHCIIa, MyHCIIx and MyHCI did not show similar change in the total MyHC after surgery. The decreasing tendency of the proportion of MyHCIIb plus MyHCeom most resembled the changes in the total MyHC content at the different time points after surgery.


Reference

References

1. Porter JD, Baker RS, Ragusa RJ, Brueckner JK. Extraocular muscles; basic and clinical aspects of structure and function. Surv Ophthalmol. 1995; 39:451–84.
Article
2. Spencer RF, Porter JD. Structural organization of the extraocular muscles. Rev Oculomot Res. 1988; 2:33–79.
3. Oh SY, Poukens V, Cohen MS, Demer JL. Structure-function correlation of laminar vascularity in human rectus muscles. Invest Ophthalmol Vis Sci. 2001; 42:17–22.
4. Oh SY, Poukens V, Demer JL. Quantitative analysis of rectus muscle layers in monkey and humans. Invest Ophthalmol Vis Sci. 2001; 42:10–6.
5. Demer JL, Miller JM, Poukens V, et al. Evidence for fibromus-cular pulleys of the recti extraocular muscles. Invest Ophthalmol Vis Sci. 1995; 36:1125–36.
6. Demer JL. The orbital pulley system: a revolution in concepts of orbital anatomy. Ann N Y Acad Sci. 2002; 956:17–32.
Article
7. Bottinelli R. Functional heterogeneity of mammalian single muscle fibres: do myosin isoforms tell the whole story? Pflugers Arch. 2001; 443:6–17.
Article
8. Pette D, Staron RS. Cellular and molecular diversities of mam-malian skeletal muscle fibers. Rev Physiol Biochem Pharmacol. 1990; 116:1–76.
Article
9. Schiaffino S, Reggiani C. Myosin isoforms in mammalian skeletal muscle. J Appl Physiol. 1994; 77:493–501.
Article
10. Bottinelli R, Schiaffino S, Reggiani C. Force-velocity relations and myosin heavy chain isoform compositions of skinned fibres from rat skeletal muscle. J Physiol. 1991; 437:655–72.
Article
11. Smerdu V, Karsch-Mizrachi I, Campione M, et al. Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle. Am J Physiol. 1994; 267:1723–8.
Article
12. Wieczorek DF, Periasamy M, Butler-Browne GS, et al. Co− expression of multiple myosin heavy chain genes, in addition to a tissue-specific one, in extraocular musculature. J Cell Biol. 1985; 101:618–29.
13. Sartore S, Mascarello F, Rowlerson A, et al. Fibre types in extraocular muscles: a new myosin isoform in the fast fibres. J Muscle Res Cell Motil. 1987; 8:161–72.
Article
14. Rubinstein NA, Hoh JF. The distribution of myosin heavy chain isoforms among rat extraocular muscle fiber types. Invest Ophthalmol Vis Sci. 2000; 41:3391–8.
15. Pedrosa-Domellf F, Holmgren Y, Lucas CA, et al. Human extraocular muscles: unique pattern of myosin heavy chain expression during myotube formation. Invest Ophthalmol Vis Sci. 2000; 41:1608–16.
16. Brueckner JK, Itkis O, Porter JD. Spatial and temporal patterns of myosin heavy chain expression in developing rat extraocular muscle. J Muscle Res Cell Motil. 1996; 17:297–312.
Article
17. Bormioli SP, Torresan P, Sartore S, et al. Immunohistochemical identification of slow-tonic fibers in human extrinsic eye muscles. Invest Ophthalmol Vis Sci. 1979; 18:303–6.
18. Mascarello F, Rowlerson AM. Myosin isoform transitions during development of extra-ocular and masticatory muscles in the fetal rat. Anat Embryol. 1992; 185:143–53.
Article
19. Pedrosa-Domellf F, Eriksson PO, Butler-Browne GS, Thornell LE. Expression of alpha-cardiac myosin heavy chain in mammalian skeletal muscle. Experientia. 1992; 48:491–4.
Article
20. Jakubiec-Puka A, Catani C, Carraro U. Myosin heavy-chain composition in striated muscle after tenotomy. Biochem J. 1992; 282:237–42.
Article
21. Riley DA, Slocum GR, Bain JL, et al. Rat hindlimb unloading: soleus histochemistry, ultrastructure, and electromyography. J Appl Physiol. 1990; 69:58–66.
Article
22. Christiansen SP, Soulsby ME, Seifen EE. Effect of antagonist weakening on developed tension in cat extraocular muscle. Invest Ophthalmol Vis Sci. 1995; 36:2547–50.
23. Beisner DH. Reduction of ocular torque by medial rectus recession. Arch Ophthalmol. 1971; 85:13–7.
Article
24. Kushner BJ, Vrabec M. Theoretical effects of surgery on length tension relationships in extraocular muscles. J Pediatr Ophthalmol Starabismus. 1987; 24:126–31.
Article
25. Jakubiec-Puka A, Kulesza-Lipka D, Krajewski K. The contractile apparatus of striated muscle in the course of atrophy and regene-ration. Ⅱ. Myosin and actin filaments in mature rat soleus muscle regenerating after reinnervation. Cell Tissue Res. 1982; 227:641–50.
Article
26. Jakubiec-Puka A, Kulesza-Lipka D, Krajewski K. The contractile apparatus of striated muscle in the course of atrophy and regene-ration. Ⅰ. Myosin and actin filaments in mature rat soleus muscle regenerating after reinnervation. Cell Tissue Res. 1981; 220:651–63.
27. Lee HC, Oh SY, Chang BL. The changes of myosin heavy chain isoforms after tenotomy on extraocular muscle layers of rabbits. J Korean Ophthalmol Soc. 2003; 44:2402–9.
28. Kim YJ, Oh SY, Chang BL. The change of extraocular muscle layers after tenotomy; histologic and immunohistochemical study. J Korean Ophthalmol Soc. 2002; 43:2042–50.
29. Kranjc BS, Sketelj J, D'Albis A, Erzen I. Long-term changes in myosin heavy chain composition after botulinum toxin A injection into rat medial rectus muscle. Invest Ophthalmol Vis Sci. 2001; 42:3158–64.
30. Christiansen SP, Peterson D, To T, et al. Long term effects of ricin-mAb 35 on extraocular muscles of rabbits: potential treatment for strabismus. Invest Ophthalmol Vis Sci. 2002; 43:679–85.
31. Park KA, Oh SY. Distribution of myosin heavy chain isoform in human extraocular muscles. J Korean Ophthalmol Soc. 2009; 50:285–9.
Article
32. Inagi K, Connor NP, Schultz E, et al. Muscle fiber-type changes induced by botulinum toxin injection in the rat larynx. Oto-laryngol Head Neck Surg. 1999; 120:876–83.
Article
33. Starling EH, Evans CL. Principles of Human Physiology. Phila-delphia: Lea & Febiger;1968. p. 820–4.
34. Clark RA, Demer JL. Magnetic resonance imaging ofthe effects of horizontal rectus extraocular muscle surgery on pulley and globe positions and stability. Invest Ophthalmol Vis Sci. 2006; 47:188–94.
35. Briggs MM, Schachat F. Early specialization of the superfast myosin in extraocular and laryngeal muscles. J Exp Biol. 2000; 203:2485–94.
Article
36. Briggs MM, Schachat F. The superfast extraocular myosin (MYH13) is localized to the innervation zone in both the global and orbital layers of rabbit extraocular muscle. J Exp Biol. 2002; 205:3133–42.
Article
Full Text Links
  • JKOS
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