Collagen pp 325-357 | Cite as

The Extracellular Matrix of Skeletal and Cardiac Muscle

  • P.P. Purslow


Well-organized and distinct extracellular matrix networks exist within both striated and cardiac muscles. Individual muscle cells are separated by a fine collagen fiber network embedded in a proteoglycan matrix (the endomysium). Larger groups or bundles of muscle cells are separated by a thicker connective tissue structure, the perimysium. The endomysium separating adjacent muscle cells joins together at the nodes between cells to form a continuous structure within the muscle fiber bundle, and perimysium similarly forms a continuous network throughout the entire organ.

In striated muscle, the networks of wavy (non-straight) collagen fibers in both endomysium and perimysium can easily reorientate and offer little tensile resistance to changing muscle length. However, forces can be transmitted efficiently by shear through the thickness of the endomysium. The endomysium fulfills the role of mechanically linking adjacent muscle fibers so as to coordinate their length changes and keep their sarcomere lengths uniform. Especially in series-fibered muscles, shear through the thickness of the endomysium is a key mechanism for transmission of forces generated by contraction of muscle fibers.

There is evidence that the perimysium of striated muscle can also play a role in muscle force transmission (myofascial force transmission), but there is also a clear role for the perimysial boundaries between adjacent muscle fiber bundles to accommodate shear deformations generated when muscles contract. Differences in shear strains generated in anatomically different muscles appear to be the main explanation of why the division of muscles into fiber bundles (fascicles) by perimysium varies so much from muscle to muscle.

The endomysium and perimysium in cardiac muscle shows strong similarities in structure and function to the same extracellular matrix structures in striated\break muscle.

The extracellular matrix in muscle is dynamically remodeled according to the loads imposed on it during muscle growth, exercise, and as a response to damage. This is especially relevant to the properties of cardiac muscle after ischemia. Matrix metalloproteinases responsible for remodeling extracellular matrix within muscle are secreted both by fibroblasts and by the muscle cells.

The atrioventricular valves in the heart are special connective tissue structures well adapted to their function. Collagen fiber orientation in the cusps of these valves is closely modulated to reinforce the valves against predominant haemodynamic stresses.

The connective tissue structures within striated and cardiac muscles are an integrated part of the muscle as a whole tissue or organ and play key roles in their in vivo mechanical functions and properties.


Cardiac Muscle Muscle Length Sarcomere Length Pennation Angle Adjacent Muscle 
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  1. Anderson MJ, Klier FG, Tanguay KE (1984) Acetylcholine receptor aggregation parallels the deposition of a basal lamina proteoglycan during development of the neuromuscular junction. J. Cell Biol. 99: 1769–1784.CrossRefGoogle Scholar
  2. Anderson RH, Ho SY, Redmann K, Sanchez-Quintana D, Lunkenheimer PP (2005) The anatomical arrangement of the myocardial cells making up the ventricular mass. Eur. J. Cario-thoracic Surg. 28: 517–525.CrossRefGoogle Scholar
  3. Anderson RH, Ho SY, Sanchez-Quintana D, Redmann K, Lunkenheimer PP (2006) Heuristic problems in defining three-dimensional arrangement of the ventricular myocytes. Anat. Rec. 288A: 579–586.CrossRefGoogle Scholar
  4. Arts T, Costa KD, Covell JW, McCulloch AD (2001) Relating myocardial laminar architecture to shear strain and muscle fiber orientation. Am. J. Physiol. Heart Circ. Physiol. 280: H2222–H2229.Google Scholar
  5. Balcerzak D, Querengesser L, Dixon WT, Baracos VE (2001) Coordinate expresión of matrix-degrading proteinases and their activators and inhibitors in bovine skeletal muscle. J. Anim. Sci. 79: 94–107.Google Scholar
  6. Bendall JR (1967) The elastin content of various muscles of beef animals. J.Sci. Food Agric. 18: 553–558.CrossRefGoogle Scholar
  7. Bigi A, RipamontiI A, Roveri N, Compostella L, Roncon L, Schivazappa L (1982) Structure and orientation of collagen-fibers in human mitral-valve. Int. J. Biol. Macromol. 4: 387–392.CrossRefGoogle Scholar
  8. Bishop JE, Lindahl G (1999) Regulation of cardiovascular collagen synthesis by mechanical load. Cardiovasc. Res. 42: 27–44.CrossRefGoogle Scholar
  9. Bloch RJ, Capetanaki Y, O’Neill A, Reed P, Williams MW, Resneck WG, Porter NC, Ursitti JA (2002) Costameres: repeating structures at the sarcolemma of skeletal muscle. Clin. Orthoped. Rel. Res. 403S: S203–S210.CrossRefGoogle Scholar
  10. Borg TK, Caulfield JB (1980) Morphology of connective tissue in skeletal muscle. Tissue Cell 12: 197–207.CrossRefGoogle Scholar
  11. Borg TK, Caulfield JB (1981) The collagen matrix of the heart. Federation Proc. 40: 2037–2041.Google Scholar
  12. Bourne GH (1973) The structure and function of muscle Vol. II Structure part 2. Academic Press, NY.Google Scholar
  13. Bovendeerd PHM, Huyghe JM, Arts T, Van Campen DH, Reneman RS (1994) Influence of endocardial–epicardial crossover of muscle fibers on left ventricular wall mechanics. J. Biomech. 27: 941–951.CrossRefGoogle Scholar
  14. Bowman W (1840) On the minute structure and movements of voluntary muscle. Phil. Trans. Roy. Soc. Lond. 130: 457–501.CrossRefGoogle Scholar
  15. Brooks JC, Savell JW (2004) Perimysium thickness as an indicator of beef tenderness. Meat Sci. 67: 329–334.CrossRefGoogle Scholar
  16. Brower GL, Gardner, JD, Forman MF, Murray DB, Voloshenyuk T, Levick SP, Janicki JS (2006) The relationship between myocardial extracellular matrix remodelling and ventricular function. Eur. J. Cardio-thoracic Surg. 30: 604–610.CrossRefGoogle Scholar
  17. Carrino DA, Caplan AI (1982) Isolation and preliminary characterization of proteoglycans synthesized by skeletal muscle. J. Biol. Chem. 257: 14145–14154.Google Scholar
  18. Cheng A, Langer F, Rodriguez F, Criscione JC, Daughters GT, Miller DC, Ingels NB. (2005) Transmural sheet strains in the lateral wall of the ovine left ventricle. Am. J. Physiol. Heart Circ. Physiol. 289: H1234–H1241.CrossRefGoogle Scholar
  19. Costa KD, Takayama Y, McCulloch AD, Covell JW (1999). Laminar fiber architecture and three-dimensional systolic mechanics in canine ventricular myocardium. Am. J. Physiol. Heart Circ. Physiol. 276:H595–H607.Google Scholar
  20. Debessa CRG, Maifrino LBM, de Souza RR (2001) Age related changes in the collagen network of the human heart. Mech. Ageing Dev. 122: 1049–1058.CrossRefGoogle Scholar
  21. Deschamps AM, Spinale FG (2005) Matrix modulation and heart failure: new concepts question old beliefs. Curr. Opinion Cardiol. 20: 211–216.CrossRefGoogle Scholar
  22. de Souza RR (2002) Ageing of myocardial collagen. Biogerontology 3: 325–335.CrossRefGoogle Scholar
  23. Dokos S, Smaill BH, Young AA, LaGrice IJ (2002) Shear properties of passive ventricular myocardium. Am. J. Physiol. Heart Cierc. Physiol. 283: H2650–H2659.Google Scholar
  24. Dorri F, Niederer PF, Redmann K, Lunkenheimer PP, Cryer CW, Anderson RH (2007) An analysis of the spatial arrangement of the myocardial aggregates making up the wall of the left ventricle. Eur. J. Cardio-thoracic Surg. 31: 430–437.CrossRefGoogle Scholar
  25. Eggen KH, Malmstrom A, Kolse, SO (1994) Decorin and a large dermatan sulfate proteoglycan in bovine striated muscle. Biochim. Biophys. Acta 1204: 287–297.Google Scholar
  26. Feneis H (1935) Uber die Anordnung und die Bedentung des indegewebes fur die Mechanik der Skelettmuskulatur. Morph. Jb. 76: 161–202.Google Scholar
  27. Gans C, Gaunt AS (1991) Muscle architecture in relation to function. J. Biomech. 24: 53–65.CrossRefGoogle Scholar
  28. Grounds MD, Sorokin L, White J (2005) Strength at the extracellular matrix – muscle interface. Scand. J. med. Sci. Sports 15: 381–391.CrossRefGoogle Scholar
  29. Hanley PJ, Young AA, leGrice IJ, Edgar SG, Loiselle DS (1999). 3-Dimensional configuration of perimysial collagen fibres in rat cardiac muscle at resting and extended sarcomere lengths. J. Physiol. 517: 831–837.CrossRefGoogle Scholar
  30. Harrington KB, Rodriguez F, Cheng A, Langer F, Ashikaga H, daughters GT, Criscione JC, Ingels, NB, Miller DC (2005) Direct measurement of transmural laminar architecture in the anterolateral wall of the ovine left ventricle: new implications for wall thickening mechanics. Am. J. Physiol. Heart Circ. Physiol. 258: H1324–H1330.Google Scholar
  31. He ZM, Ritchie J, Grashow JS, Sacks MS, Yoganathan AP (2005) In vitro dynamic strain behavior of the mitral valve posterior leaflet. J. Biomech. Eng. (Trans ASME) 127: 504–511.CrossRefGoogle Scholar
  32. Heeneman S, Cleutjens JP, Faber BC, Creemers EE, van Suylen R-J, Lutgens E, Cleutjens KB, Daemen MJ (2003) The dynamic extracellular matrix: intervention strategies during heart failure and atherosclerosis. J. Pathol. 200: 516–525.CrossRefGoogle Scholar
  33. Holmes JW, Borg TK, Covell JW (2005) Strucutre and mechanics of heraling myocardial infarcts. Ann. Rev. Biomed. Eng. 7: 223–253.CrossRefGoogle Scholar
  34. Huijing PA, Baan GC, Rebel G (1998) Non-myotendinousforce transmission in rat extensor digitorum longus muscle. J. Exp. Biol. 201, 682–691.Google Scholar
  35. Huijing PA, Baan, GC (2001) Extramuscular myofascial force transmission within the rat anterior tibial compartment; proximo-distal differences in muscle force. Acta Physiol. Scand. 173: 297–311.CrossRefGoogle Scholar
  36. Huijing, PA, Jaspers, RT (2005) Adaptation of muscle size and myofascial force transmission: a review and some new experimental results. Scand. J. Med. Sci. Sports 15: 349–380.CrossRefGoogle Scholar
  37. Icardo JM, Colvee E (1998) Collagenous skeleton of the human mitral papillary muscle. Anat. Rec. 252: 509–518.CrossRefGoogle Scholar
  38. Intrigila B, Melatti I, Tofani A, Macchiarelli G (2007) Computational models of myocardial endomysial collagen arrangement. Computer Methods and Programs in Biomedicine 86: 232–244.CrossRefGoogle Scholar
  39. Jaspers RT, Brunner R, Pel JMM, Huijing PA (1999) Acute effects of intramuscular aponeurotomy on rat gastrocnemius medialis: force transmission, muscle force and sarcomere length. J. Biomech. 32, 71–79.CrossRefGoogle Scholar
  40. Jolley PD, Purslow PP (1988) Reformed meat products – fundamental concepts and new developments. In: Mitchell J, Blanshard JMV (Eds.) Food Structure – Its Creationand Evaluation. Butterworths, London 231–264.Google Scholar
  41. Kieseier BC, Schneider C, Clements JM, Gearing AJH, Gold R, Tokya KV, Hartung H-P (2001) Expression of specific matrix metalloproteinases in inflammatory myopathies. Brain 124: 341–351.CrossRefGoogle Scholar
  42. Kjær, M (2004) Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading. Physiol. Rev. 84: 649–698.CrossRefGoogle Scholar
  43. Kjær M, Magnusson P, Krogsgaard M, Moller JB, Olesen J, Heinemeier K, Hansen M, Haraldsson B, Koskinen S, Esmarck B, Langberg H (2006) Extracellular matrix adaptation of tendon and skeletal muscle to exercise. J. Anat. 208: 445–450.CrossRefGoogle Scholar
  44. Krenchel. H. (1964) Fibre Reinforcement. Akademisk Forlag, Copenhagen.Google Scholar
  45. Lawson MA, Purslow PP (2001) Development of components of the extracellular matrix, basal lamina and sarcomere in chick quadriceps and pectoralis muscles. Br. Poult. Sci. 42: 315–320.CrossRefGoogle Scholar
  46. Lepetit J (1991) Theoretical strain ranges in raw meat. Meat Sci. 29: 271–283.CrossRefGoogle Scholar
  47. Lewis GJ, Purslow PP (1989) The strength and stiffness of perimysial connective-tissue isolated from cooked beef muscle. Meat Sci. 26: 255–269.CrossRefGoogle Scholar
  48. Lewis GJ, Purslow PP (1991) The effect of marination and cooking on the mechanical properties of intramuscular connective tissue. J. Muscle Foods 2: 177–195.CrossRefGoogle Scholar
  49. Lewis GJ, Purslow PP, Rice AE (1991) The effect of conditioning on the strength of perimysial connective-tissue dissected from cooked meat. Meat Sci. 30: 1–12CrossRefGoogle Scholar
  50. Liao J, Yang L, Grashow J, Sacks MS (2007) The relation between collagen fibril kinematics and mechanical properties in the mitral valve anterior leaflet J. Biomech. Eng. (Trans ASME) 129: 78–87.CrossRefGoogle Scholar
  51. Light ND (1987) The role of collagen in determining the texture of meat. In Pearson AM, Dutson TR, Bailet AJ (Eds.) Advances in Meat Research Vol. 4: Collagen as a Food. Van Nostrand Reinhold, NY 87–107.Google Scholar
  52. Light N, Champion AE, Voyle C, Bailey AJ (1985) The role of epimysial, perimysial and endomysial collagen in determining texture in six bovine muscles. Meat Sci. 13: 137–149.CrossRefGoogle Scholar
  53. Lis Y, Burleigh MC, Parker DJ, Child AH, Hogg J, Davies MJ (1987) Biochemical-characterization of individual normal, floppy and rheumatic human mitral-valves. Biochem. J. 244: 597–603.Google Scholar
  54. Listrat A, Picard B, Geay Y (1999) Age-related changes and location of type I, III, IV, V and VI collagens during development of four foetal skeletal muscles of double muscles and normal bovine muscles. Tissue Cell 31: 17–27.CrossRefGoogle Scholar
  55. Listrat A, Lethias C, Hocquette JF, Renand G, Menissier F, Geay Y, Picard B (2000). Age related changes and location of types I, III, XII and XIV collagen during development of skeletal muscles from genetically different animals. Histochem. J. 32: 349–356.Google Scholar
  56. Lunkenheimer PP, Redmann K, Westermann P, Rothaus K, Cryer CW, Niederer P, Anderson RH (2006) The myocardium and its fibrous matrix working in concert as a spatially netted mesh: a critical review of the purported tertiary structure of the ventricular mass. Eur. J. Cardio-thoracic Surg. 295: 541–549.Google Scholar
  57. Macchiarelli G, Ohtani O (2001). Endomysium in left ventricle. Heart 86: 416–416.CrossRefGoogle Scholar
  58. Macchiarelli G, Ohtani O, Nottola SA, Stallone T, Camboni A, Prado IM, Motta PM (2002) A micro-anatomical model of the distribution of myocardial endomysial collagen. Histol. Histopath. 17: 699–706.Google Scholar
  59. Magid A, Law DJ (1985) Myofibrils bear most of the resting tension in frog skeletal muscle. Science 230: 1280–1282.CrossRefGoogle Scholar
  60. Mayne R, Sanderson RD (1985) The extracellular matrix of skeletal muscle. Collagen Relat. Res. 5: 449–468.Google Scholar
  61. McCormick RJ (1994) The flexibility of the collagen compartment of muscle. Meat Sci. 36: 79–91.CrossRefGoogle Scholar
  62. Merryman WD, Engelmayr GC, Liao J, Sacks MS (2006) Defining biomechanical endpoints for tissue engineered heart valve leaflets from native leaflet properties. Progress Pediatric Cardiol. 21: 153–160.CrossRefGoogle Scholar
  63. Miner EC, Miller WL (2006) A look between the cardiomyocytes: the extracellular matrix in heart failure. Mayo Clin. Proc. 81: 71–76.Google Scholar
  64. Mutungi G, Purslow P, Warkup C (1995) Structural and mechanical changes in raw and cooked single porcine muscle-fibers extended to fracture. Meat Sci. 40: 217–234.CrossRefGoogle Scholar
  65. Nakano T, Li X, Sunwoo HH, Sim JS (1997) Immunohistochemical localization of proteoglycans in bovine skeletal muscle and adipose connective tissues. Can. J. Anim. Sci. 77: 169–172.CrossRefGoogle Scholar
  66. Natori R. (1954) The role of myofibrils, sarcoplasma and sarcolemma in muscle contraction. Jikeikai Med. J. 1, 18–28.Google Scholar
  67. Nishimura T, Hattori A, Takahashi K (1996) Arrangement and identification of proteoglycans in basement membrane and intramuscular connective tissue of bovine semitendinousus muscle. Acta Anat. 155: 257–265.CrossRefGoogle Scholar
  68. Passerieux E, Rossignol R, Chopard A, Carnino A, Marini JF, Letellier T, Delage JP (2006) Structural organization of the perimysium in bovine skeletal muscle: Junctional plates and associated intracellular subsomains. J. Struct. Biol. 154: 206–216.CrossRefGoogle Scholar
  69. Passerieux E, Rossignol R, Letellier T, Delage JP (2007) Physical continuity of the perimysium from myofibers to tendons: Involvement in lateral force transmission in skeletal muscle. J. Struct. Biol. 159: 19–28.CrossRefGoogle Scholar
  70. Peterson JT (2006) The importance of estimating the therapeutic index in the development of matrix metalloproteinase inhibitors. Cardiovasc. Res. 69: 677–687.CrossRefGoogle Scholar
  71. Podolsky RJ (1964) The maximum sarcomere length for contraction of isolated myofibrils. J. Physiol. 170, 110–123.Google Scholar
  72. Purslow PP (1989) Strain-induced reorientation of an intramuscularconnective tissue network: Implications for passive muscle elasticity. J. Biomech. 22: 21–31.CrossRefGoogle Scholar
  73. Purslow PP (1999) The intramuscular connective tissue matrix and cell-matrix interactions in relation to meat toughness. Proceedings of the 45th International Congress Meat Science And Technology. Yokohama, Japan 210–219.Google Scholar
  74. Purslow PP (2002) The structure and functional significance of variations in the connective tissue within muscle. Comp. Biochem. Physiol. Part A 133: 947–966.Google Scholar
  75. Purslow PP (2005) Intramuscular connective tissue and its role in meat quality. Meat Sci. 70: 435–447.CrossRefGoogle Scholar
  76. Purslow PP, Duance VC (1990) The structure and function of intramuscular connective tissue. In Hukins DWL (Ed.) Connective Tissue Matrix Vol 2. MacMillan, London 127–166.Google Scholar
  77. Purslow PP, Trotter JA, (1994) The morphology and mechanical properties of endomysium in series-fibred muscles; variations with muscle length. J. Muscle Res. Cell Motil. 15: 299–304.CrossRefGoogle Scholar
  78. Purslow PP, Wess TJ, Hukins DWL (1998). Collagen orientation and molecular spacing during creep and stress–relaxation in soft connective tissues. J. Exp. Biol. 201: 135–142.Google Scholar
  79. Ramsay RW, Street SF (1940) The isometric length-tension diagram of isolated skeletal fibers of the frog. J. Cell Comp. Physiol. 15: 11–34.CrossRefGoogle Scholar
  80. Rhodes JM, Simons M (2007) The extracellular matrix and blood vessel formation: not just a scaffold. J. Cell. Molec. Med. 11: 176–205.CrossRefGoogle Scholar
  81. Robinson TF, Geraci MA, Sonnenblick EH, Factor SM (1988). Coiled perimysioal fibres of papillary muscle in rat heart: morphology, distribution and changes in configuration. Circ. Res. 63: 577–592.Google Scholar
  82. Rowe RWD (1981) Morphology of perimysial and endomysial connective tissue in skeletal muscle. Tissue Cell 13: 681–690.CrossRefGoogle Scholar
  83. Sacks MS, Smith DB, Hiester ED (1998) The aortic valve microstructure: Effects of transvalvular pressure. J. Biomed. Mats. Res. 41: 131–141.CrossRefGoogle Scholar
  84. Sanes JR (2003) The basement membrane/basal lamina of skeletal muscle. J. Biol. Chem. 278: 12601–12604.CrossRefGoogle Scholar
  85. Sato K, Ohashi C, Muraki M, Itsuda H, Yokoyama Y, Kanamori M, Ohtsuki K, Kawabata M (1998) Isolation of intact type V collagen from fish intramuscular connective tissue. J. Food Biochem. 22: 213–225.CrossRefGoogle Scholar
  86. Schmalbruch H. (1985) Skeletal Muscle. Springer. Berlin.Google Scholar
  87. Schmid H, Nash MP, Young AA, Hunter PJ (2006) Myocardial material parameter estimation – a comparative study for simple shear. J. Biomech. Eng. (Trans. ASME) 128: 742–750.CrossRefGoogle Scholar
  88. Schwartz SM (Ed) (1995). The Vascular Smooth Muscle Cell: Molecular and Biological Responses to the Extracellular Matrix. Academic Press, NY. ISBN-10: 0126323100.Google Scholar
  89. Scott JE (1990) Proteoglycan: collagen interactions and subfibrillar structure in collagen fibrils. Implications in the development and ageing of connective tissues. J. Anat. 169: 23–35.Google Scholar
  90. Street SF (1983) Lateral transmission of tension in frog myofibers: A myofibrillar network and transverse cytoskeletal connections are possible transmitters. J. Cell. Physiol. 114: 346–364.CrossRefGoogle Scholar
  91. Stegemann JP, Hong H, Nerem RM (2005) Mechanical, biochemical, and extracellular matrix effects on vascular smooth muscle cell phenotype. J. Appl. Physiol. 98: 2321–2327.CrossRefGoogle Scholar
  92. Sun W, Sacks MS, Sellaro TL, Slaughter WS, Scott MJ (2003) Biaxial mechanical response of bioprosthetic heart valve biomaterials to high in-plane shear. J. Biomech. Eng. (Trans ASME) 125: 372–380.CrossRefGoogle Scholar
  93. Torrent-Guasp F, Ballester M, Buckberg GD, Carreras F, Flotats A, Carrio I, Ferreira A, Samuels LE, Narula J (2001) Spatial orientation of the ventricular muscle band: Physiologic contribution and surgical implications. J. Thorac. Cardiovasc. Surg 122: 389–392.CrossRefGoogle Scholar
  94. Torrent-Guasp F, Kocica MJ, Corno AF, Komeda M, Carreras-Costa F, Flotats A, Cosin-Aguillar J, Wen H (2005) Towards new understanding of the heart structure and function. Eur. J. Cardio-thoracic Surg. 27: 191–201.CrossRefGoogle Scholar
  95. Trotter JA (1993) Functional morphology of force transmission n skeletal muscle. Acta Anat. 146: 205–222.CrossRefGoogle Scholar
  96. Trotter JA, Purslow PP, (1992) Functional morphology of the endomysium in series fibered muscles. J. Morphol. 212: 109–122.CrossRefGoogle Scholar
  97. Trotter JA, Richmond FJR, Purslow PP (1995). Functional morphology and motor control of series fibred muscles. In: Holloszy, JO (Ed.), Exercise and Sports Sciences Reviews Vol 23. Williams and Watkins, Baltimore, 167–213. ISBN 0-683-00037-3.Google Scholar
  98. Velleman SG, Liu XS, Eggen KH, Nestor KE (1999) Developmental downregulation of proteoglycan synthesis and decorin expression during turkey embryonic skeletal muscle formation. Poult. Sci. 78, 1619–1626.Google Scholar
  99. Willems MET, Purslow PP (1997) Mechanical and structural characteristics of single muscle fibres and fibre groups from raw and cooked pork Longissimus muscle. Meat. Sci. 46: 285–301.CrossRefGoogle Scholar
  100. Young M, Paul A, Rodda J, Duxson M, Sheard P (2000) Examination of Intrafascicular Muscle fiber terminations: Implications for tension delivery in series-fibered muscles. J. Morphol. 245:130–145.CrossRefGoogle Scholar

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