Skip to main content
Journal of Anatomy logoLink to Journal of Anatomy
. 2001 Mar;198(Pt 3):283–294. doi: 10.1046/j.1469-7580.2001.19830283.x

Muscle fibre types in the suprahyoid muscles of the rat

A R COBOS 1, L A G SEGADE 1,, I FUENTES 1
PMCID: PMC1468218  PMID: 11322721

Abstract

Five muscle fibre types (I, IIc, IIa, IIx and IIb) were found in the suprahyoid muscles (mylohyoid, geniohyoid, and the anterior and posterior bellies of the digastric) of the rat using immuno and enzyme histochemical techniques. More than 90% of fibres in the muscles examined were fast contracting fibres (types IIa, IIx and IIb). The geniohyoid and the anterior belly of the digastric had the greatest number of IIb fibres, whilst the mylohyoid was almost exclusively formed by aerobic fibres. The posterior belly of the digastric contained a greater percentage of aerobic fibres (83.4%) than the anterior belly (67.8%). With the exception of the geniohyoid, the percentage of type I and IIc fibres, which have slow myosin heavy chain (MHCβ), was relatively high and greater than has been previously reported in the jaw-closing muscles of the rat, such as the superficial masseter. The geniohyoid and mylohyoid exhibited a mosaic fibre type distribution, without any apparent regionalisation, although in the later MHCβ-containing fibres (types I and IIc) were primarily located in the rostral 2/3 region. In contrast, the anterior and posterior bellies of the digastric revealed a clear regionalisation. In the anterior belly of the digastric 2 regions were observed: both a central region, which was almost exclusively formed by aerobic fibres and where all of the type I and IIc fibres were located, and a peripheral region, where type IIb fibres predominated. The posterior belly of the digastric showed a deep aerobic region which was greater in size and where type I and IIc fibres were confined, and a superficial region, where primarily type IIx and IIb fibres were observed.

Keywords: Skeletal muscle, muscle histochemistry

Full Text

The Full Text of this article is available as a PDF (684.5 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andreo J. C., Pai V. D., Navarro J. A., de Oliveira J. A. Fiber types distribution in the digastric muscle of tufted capuchin monkey (Cebus apella). Anat Histol Embryol. 1994 Sep;23(3):226–231. doi: 10.1111/j.1439-0264.1994.tb00471.x. [DOI] [PubMed] [Google Scholar]
  2. Billeter R., Weber H., Lutz H., Howald H., Eppenberger H. M., Jenny E. Myosin types in human skeletal muscle fibers. Histochemistry. 1980;65(3):249–259. doi: 10.1007/BF00493174. [DOI] [PubMed] [Google Scholar]
  3. Bottinelli R., Betto R., Schiaffino S., Reggiani C. Maximum shortening velocity and coexistence of myosin heavy chain isoforms in single skinned fast fibres of rat skeletal muscle. J Muscle Res Cell Motil. 1994 Aug;15(4):413–419. doi: 10.1007/BF00122115. [DOI] [PubMed] [Google Scholar]
  4. Bredman J. J., Weijs W. A., Korfage H. A., Brugman P., Moorman A. F. Myosin heavy chain expression in rabbit masseter muscle during postnatal development. J Anat. 1992 Apr;180(Pt 2):263–274. [PMC free article] [PubMed] [Google Scholar]
  5. Bredman J. J., Weijs W. A., Moorman A. F., Brugman P. Histochemical and functional fibre typing of the rabbit masseter muscle. J Anat. 1990 Feb;168:31–47. [PMC free article] [PubMed] [Google Scholar]
  6. Bredman J. J., Wessels A., Weijs W. A., Korfage J. A., Soffers C. A., Moorman A. F. Demonstration of 'cardiac-specific' myosin heavy chain in masticatory muscles of human and rabbit. Histochem J. 1991 Apr;23(4):160–170. doi: 10.1007/BF01046587. [DOI] [PubMed] [Google Scholar]
  7. Brooke M. H., Kaiser K. K. Muscle fiber types: how many and what kind? Arch Neurol. 1970 Oct;23(4):369–379. doi: 10.1001/archneur.1970.00480280083010. [DOI] [PubMed] [Google Scholar]
  8. Bubb W. J., Sims M. H. Fiber type composition of rostral and caudal portions of the digastric muscle in the dog. Am J Vet Res. 1986 Aug;47(8):1834–1842. [PubMed] [Google Scholar]
  9. Bär A., Pette D. Three fast myosin heavy chains in adult rat skeletal muscle. FEBS Lett. 1988 Aug 1;235(1-2):153–155. doi: 10.1016/0014-5793(88)81253-5. [DOI] [PubMed] [Google Scholar]
  10. Clark R. W., Luschei E. S. Histochemical characteristics of mandibular muscles of monkeys. Exp Neurol. 1981 Dec;74(3):654–672. doi: 10.1016/0014-4886(81)90242-9. [DOI] [PubMed] [Google Scholar]
  11. Dick T. E., van Lunteren E. Fiber subtype distribution of pharyngeal dilator muscles and diaphragm in the cat. J Appl Physiol (1985) 1990 May;68(5):2237–2240. doi: 10.1152/jappl.1990.68.5.2237. [DOI] [PubMed] [Google Scholar]
  12. Dunn S. E., Michel R. N. Coordinated expression of myosin heavy chain isoforms and metabolic enzymes within overloaded rat muscle fibers. Am J Physiol. 1997 Aug;273(2 Pt 1):C371–C383. doi: 10.1152/ajpcell.1997.273.2.C371. [DOI] [PubMed] [Google Scholar]
  13. Eriksson P. O., Eriksson A., Ringqvist M., Thornell L. E. Histochemical fibre composition of the human digastric muscle. Arch Oral Biol. 1982;27(3):207–215. doi: 10.1016/0003-9969(82)90054-1. [DOI] [PubMed] [Google Scholar]
  14. Eriksson P. O., Thornell L. E. Histochemical and morphological muscle-fibre characteristics of the human masseter, the medial pterygoid and the temporal muscles. Arch Oral Biol. 1983;28(9):781–795. doi: 10.1016/0003-9969(83)90034-1. [DOI] [PubMed] [Google Scholar]
  15. Fuentes I., Cobos A. R., Segade L. A. Muscle fibre types and their distribution in the biceps and triceps brachii of the rat and rabbit. J Anat. 1998 Feb;192(Pt 2):203–210. doi: 10.1046/j.1469-7580.1998.19220203.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Gorza L. Identification of a novel type 2 fiber population in mammalian skeletal muscle by combined use of histochemical myosin ATPase and anti-myosin monoclonal antibodies. J Histochem Cytochem. 1990 Feb;38(2):257–265. doi: 10.1177/38.2.2137154. [DOI] [PubMed] [Google Scholar]
  17. Guth L., Samaha F. J. Procedure for the histochemical demonstration of actomyosin ATPase. Exp Neurol. 1970 Aug;28(2):365–367. [PubMed] [Google Scholar]
  18. Hintz C. S., Coyle E. F., Kaiser K. K., Chi M. M., Lowry O. H. Comparison of muscle fiber typing by quantitative enzyme assays and by myosin ATPase staining. J Histochem Cytochem. 1984 Jun;32(6):655–660. doi: 10.1177/32.6.6202737. [DOI] [PubMed] [Google Scholar]
  19. Hughes V. M. A new histochemical method for magnesium actomyosin adenosine triphosphatase at physiological pH. Stain Technol. 1986 Jul;61(4):201–214. doi: 10.3109/10520298609109938. [DOI] [PubMed] [Google Scholar]
  20. Hämäläinen N., Pette D. The histochemical profiles of fast fiber types IIB, IID, and IIA in skeletal muscles of mouse, rat, and rabbit. J Histochem Cytochem. 1993 May;41(5):733–743. doi: 10.1177/41.5.8468455. [DOI] [PubMed] [Google Scholar]
  21. Kiliaridis S., Engström C., Thilander B. Histochemical analysis of masticatory muscle in the growing rat after prolonged alteration in the consistency of the diet. Arch Oral Biol. 1988;33(3):187–193. doi: 10.1016/0003-9969(88)90044-1. [DOI] [PubMed] [Google Scholar]
  22. Kirkeby S. A monoclonal anticarbohydrate antibody detecting superfast myosin in the masseter muscle. Cell Tissue Res. 1996 Jan;283(1):85–92. doi: 10.1007/s004410050515. [DOI] [PubMed] [Google Scholar]
  23. Kugelberg E. Adaptive transformation of rat soleus motor units during growth. J Neurol Sci. 1976 Mar;27(3):269–289. doi: 10.1016/0022-510x(76)90001-0. [DOI] [PubMed] [Google Scholar]
  24. Kwa S. H., Weijs W. A., Jüch P. J. Contraction characteristics and myosin heavy chain composition of rabbit masseter motor units. J Neurophysiol. 1995 Feb;73(2):538–549. doi: 10.1152/jn.1995.73.2.538. [DOI] [PubMed] [Google Scholar]
  25. Lev-Tov A., Tal M. The organization and activity patterns of the anterior and posterior heads of the guinea pig digastric muscle. J Neurophysiol. 1987 Sep;58(3):496–509. doi: 10.1152/jn.1987.58.3.496. [DOI] [PubMed] [Google Scholar]
  26. Lind A., Kernell D. Myofibrillar ATPase histochemistry of rat skeletal muscles: a "two-dimensional" quantitative approach. J Histochem Cytochem. 1991 May;39(5):589–597. doi: 10.1177/39.5.1826695. [DOI] [PubMed] [Google Scholar]
  27. Lindman R., Eriksson P. O., Thornell L. E. Histochemical enzyme profile of the masseter, temporal and lateral pterygoid muscles of the European hedgehog (Erinaceus europeaus). Arch Oral Biol. 1986;31(1):51–55. doi: 10.1016/0003-9969(86)90113-5. [DOI] [PubMed] [Google Scholar]
  28. Maier A. Occurrence and distribution of muscle spindles in masticatory and suprahyoid muscles of the rat. Am J Anat. 1979 Aug;155(4):483–505. doi: 10.1002/aja.1001550406. [DOI] [PubMed] [Google Scholar]
  29. Matoba H., Gollnick P. D. Influence of ionic composition, buffering agent, and pH on the histochemical demonstration of myofibrillar actomyosin ATPase. Histochemistry. 1984;80(6):609–614. [PubMed] [Google Scholar]
  30. Maxwell L. C., Carlson D. S., McNamara J. A., Jr, Faulkner J. A. Histochemical characteristics of the masseter and temporalis muscles of the rhesus monkey (Macaca mulatta). Anat Rec. 1979 Mar;193(3):389–402. doi: 10.1002/ar.1091930306. [DOI] [PubMed] [Google Scholar]
  31. McWhorter D. L., Walro J. M., Signs S. A., Wang J. Expression of alpha-cardiac myosin heavy chain in normal and denervated rat muscle spindles. Neurosci Lett. 1995 Nov 10;200(1):2–4. doi: 10.1016/0304-3940(95)12085-i. [DOI] [PubMed] [Google Scholar]
  32. Miller A. J., Farias M. Histochemical and electromyographic analysis of craniomandibular muscles in the rhesus monkey, Macaca mulatta. J Oral Maxillofac Surg. 1988 Sep;46(9):767–776. doi: 10.1016/0278-2391(88)90187-5. [DOI] [PubMed] [Google Scholar]
  33. Pedrosa F., Soukup T., Thornell L. E. Expression of an alpha cardiac-like myosin heavy chain in muscle spindle fibres. Histochemistry. 1990;95(2):105–113. doi: 10.1007/BF00266582. [DOI] [PubMed] [Google Scholar]
  34. Petrof B. J., Kelly A. M., Rubinstein N. A., Pack A. I. Effect of hypothyroidism on myosin heavy chain expression in rat pharyngeal dilator muscles. J Appl Physiol (1985) 1992 Jul;73(1):179–187. doi: 10.1152/jappl.1992.73.1.179. [DOI] [PubMed] [Google Scholar]
  35. Pierobon-Bormioli S., Sartore S., Libera L. D., Vitadello M., Schiaffino S. "Fast" isomyosins and fiber types in mammalian skeletal muscle. J Histochem Cytochem. 1981 Oct;29(10):1179–1188. doi: 10.1177/29.10.7028858. [DOI] [PubMed] [Google Scholar]
  36. Pullen A. H. The distribution and relative sizes of three histochemical fibre types in the rat tibialis anterior muscle. J Anat. 1977 Feb;123(Pt 1):1–19. [PMC free article] [PubMed] [Google Scholar]
  37. Ringqvist M., Ringqvist I., Thornell L. E. Differentiation of fibres in human masseter, temporal and biceps brachii muscles. A histochemical study. J Neurol Sci. 1977 Jun;32(2):265–273. doi: 10.1016/0022-510x(77)90241-6. [DOI] [PubMed] [Google Scholar]
  38. Rokx J. T., van Willigen J. D., Jansen H. W. Muscle fibre types and muscle spindles in the jaw musculature of the rat. Arch Oral Biol. 1984;29(1):25–31. doi: 10.1016/0003-9969(84)90038-4. [DOI] [PubMed] [Google Scholar]
  39. Rowlerson A., Mascarello F., Barker D., Saed H. Muscle-spindle distribution in relation to the fibre-type composition of masseter in mammals. J Anat. 1988 Dec;161:37–60. [PMC free article] [PubMed] [Google Scholar]
  40. Rowlerson A., Mascarello F., Veggetti A., Carpene E. The fibre-type composition of the first branchial arch muscles in Carnivora and Primates. J Muscle Res Cell Motil. 1983 Aug;4(4):443–472. doi: 10.1007/BF00711949. [DOI] [PubMed] [Google Scholar]
  41. Schiaffino S. Histochemical enzyme profile of the masseter muscle in different mammalian species. Anat Rec. 1974 Sep;180(1):53–61. doi: 10.1002/ar.1091800107. [DOI] [PubMed] [Google Scholar]
  42. Schiaffino S., Reggiani C. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol Rev. 1996 Apr;76(2):371–423. doi: 10.1152/physrev.1996.76.2.371. [DOI] [PubMed] [Google Scholar]
  43. Sciote J. J., Kentish J. C. Unloaded shortening velocities of rabbit masseter muscle fibres expressing skeletal or alpha-cardiac myosin heavy chains. J Physiol. 1996 May 1;492(Pt 3):659–667. doi: 10.1113/jphysiol.1996.sp021335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Sciote J. J., Rowlerson A. M., Carlson D. S. Myosin expression in the jaw-closing muscles of the domestic cat and American opossum. Arch Oral Biol. 1995 May;40(5):405–413. doi: 10.1016/0003-9969(94)00181-a. [DOI] [PubMed] [Google Scholar]
  45. Sciote J. J., Rowlerson A. M., Hopper C., Hunt N. P. Fibre type classification and myosin isoforms in the human masseter muscle. J Neurol Sci. 1994 Oct;126(1):15–24. doi: 10.1016/0022-510x(94)90089-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Sfondrini G., Reggiani C., Gandini P., Bovenzi R., Pellegrino M. A. Adaptations of masticatory muscles to a hyperpropulsive appliance in the rat. Am J Orthod Dentofacial Orthop. 1996 Dec;110(6):612–617. doi: 10.1016/s0889-5406(96)80037-0. [DOI] [PubMed] [Google Scholar]
  47. Staron R. S., Pette D. The continuum of pure and hybrid myosin heavy chain-based fibre types in rat skeletal muscle. Histochemistry. 1993 Aug;100(2):149–153. doi: 10.1007/BF00572901. [DOI] [PubMed] [Google Scholar]
  48. Stål P. Characterization of human oro-facial and masticatory muscles with respect to fibre types, myosins and capillaries. Morphological, enzyme-histochemical, immuno-histochemical and biochemical investigations. Swed Dent J Suppl. 1994;98:1–55. [PubMed] [Google Scholar]
  49. Suzuki A. A comparative histochemical study of the masseter muscle of the cattle, sheep, swine, dog, guinea pig, and rat. Histochemistry. 1977 Mar 4;51(2-3):121–131. doi: 10.1007/BF00567218. [DOI] [PubMed] [Google Scholar]
  50. Tamari J. W., Tomey G. F., Ibrahim M. Z., Baraka A., Jabbur S. J., Bahuth N. Correlative study of the physiologic and morphologic characteristics of the temporal and masseter muscles of the cat. J Dent Res. 1973 May-Jun;52(3):538–543. doi: 10.1177/00220345730520032701. [DOI] [PubMed] [Google Scholar]
  51. Taylor A., Cody F. W., Bosley M. A. Histochemical and mechanical properties of the jaw muscles of the cat. Exp Neurol. 1973 Jan;38(1):99–109. doi: 10.1016/0014-4886(73)90011-3. [DOI] [PubMed] [Google Scholar]
  52. Thomas N. R., Peyton S. C. An electromyographic study of mastication in the freely-moving rat. Arch Oral Biol. 1983;28(10):939–945. doi: 10.1016/0003-9969(83)90090-0. [DOI] [PubMed] [Google Scholar]
  53. Vignon C., Pellissier J. F., Serratrice G. Further histochemical studies on masticatory muscles. J Neurol Sci. 1980 Mar;45(2-3):157–176. doi: 10.1016/0022-510x(80)90163-x. [DOI] [PubMed] [Google Scholar]
  54. Weijs W. A., Dantuma R. Electromyography and mechanics of mastication in the albino rat. J Morphol. 1975 May;146(1):1–33. doi: 10.1002/jmor.1051460102. [DOI] [PubMed] [Google Scholar]
  55. Weijs W. A., Jüch P. J., Kwa S. H., Korfage J. A. Motor unit territories and fiber types in rabbit masseter muscle. J Dent Res. 1993 Nov;72(11):1491–1498. doi: 10.1177/00220345930720110601. [DOI] [PubMed] [Google Scholar]
  56. van Lunteren E., Brass E. P. Metabolic profiles of cat and rat pharyngeal and diaphragm muscles. Respir Physiol. 1996 Sep;105(3):171–177. doi: 10.1016/0034-5687(96)00043-6. [DOI] [PubMed] [Google Scholar]
  57. van Lunteren E., Vafaie H., Salomone R. J. Comparative effects of aging on pharyngeal and diaphragm muscles. Respir Physiol. 1995 Jan;99(1):113–125. doi: 10.1016/0034-5687(94)00077-d. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Anatomy are provided here courtesy of Anatomical Society of Great Britain and Ireland

RESOURCES