Advertisement

Plasminogen Activator (PA) in Muscle, Its Activation Post-Denervation

  • B. W. Festoff
  • D. Hantaï
  • C. Soria
  • J. Soria
  • M. Fardeau
Conference paper
Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)

Abstract

Following injury skeletal muscle undergoes a form of tissue remodelling that can result in relatively complete regeneration (Allbrook 1981). Although the molecular mechanisms underlying this remodelling are not yet understood, the cellular basis resides in the muscle tissue itself. Mammalian skeletal muscle regenerates from activation of quiescent “satellite” cells interposed between plasma and basement membrane (BM) of the muscle fiber. After denervation of mammalian muscle a number of changes also occur. Early events include loss of end-plate specific A12 (16 S) acetylcholinesterase (AChE), reduction in fibronectin (Fn) and, invasion of the end-plate by Schwann cells, all within 1–3 days, before muscle atrophy occurs. The possible release of neutral proteases early in denervation may account for the reduction and release of A12 AChE (Fernandez et al. 1979), internalization and partial degradation of AChR (Hatzfeld et al. 1982; Romstedt et al. 1983) and of sarcolemmal Fn (Festoff et al. 1977). These changes may be necessary for the re-innervation of denervated muscle fibers, a specialized form of remodelling in this system. Regeneration following muscle freegrafting has been shown to involve changes of Fn, collagen type IV and laminin (Gulati et al. 1983). Remodelling in other systems has been associated with increased activity of serine proteases such as plasminogen activator (PA; Danø et al. 1985), so we were interested in studying PA in skeletal muscle following denervation.

Keywords

Plasminogen Activator Neutral Protease Skeletal Muscle Regeneration Fibrin Monomer Injury Skeletal Muscle 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Allbrook D (1981) Skeletal muscle regeneration. Muscle and nerve 4: 234–245PubMedCrossRefGoogle Scholar
  2. Danø K, Andreasen PA, Grøndahl-Hansen J, Kristensen P, Nielsen LS, Skriver L (1985) Plasminogen activators, tissue degradation and cancer. Adv Cancer Res 44: 139–266PubMedCrossRefGoogle Scholar
  3. Eaton DL, Baker JB (1984) Evidence that a variety of cultured cells secrete protease nexin and produce a distinct cytoplasmic serine protease-binding factor. J Cell Physiol 117: 175–182CrossRefGoogle Scholar
  4. Fernandez HL, Duell MJ, Festoff BW (1979) Neurotrophic regulation of 16 S acetylcholinesterase at the vertebrate neuromuscular junction. J Neurobiol 10: 442–454CrossRefGoogle Scholar
  5. Festoff BW, Oliver KL, Reddi AB (1977) In vitro studies of skeletal muscle membranes. Effects of denervation on macromolecular components of cation transport in red and white muscle. J Membr Biol 32: 345–360PubMedCrossRefGoogle Scholar
  6. Festoff BW, Patterson MR, Romstedt K (1982) Plasminogen activator: the major secreted neutral protease of cultured skeletal muscle cells. J Cell Physiol 110: 190–195PubMedCrossRefGoogle Scholar
  7. Granelli-Piperno A, Reich E (1978) A study of protease and protease-inhibitor complexes in biological fluids. J Exp Med 148: 223–234PubMedCrossRefGoogle Scholar
  8. Gulati AK, Reddi AH, Zalewski AA (1983) Changes in the basement membrane zone components during skeletal muscle fiber degeneration and regeneration. J Cell Biol 97: 957–962PubMedCrossRefGoogle Scholar
  9. Hatzfeld J, Miskin R, Reich E (1982) Acetylcholine receptor: effects of proteolysis on receptor metabolism. J Cell Biol 92: 176–182PubMedCrossRefGoogle Scholar
  10. Ranby M, Norman B, Wallen P (1982) A sensitive assay for tissue plasminogen activator. Throm Res 27: 743–748CrossRefGoogle Scholar
  11. Romstedt K, Beach RL, Festoff BW (1983) Studies of acetylcholine receptor turn-over in clonal muscle cells: role of plasmin and effects of protease inhibitors. Muscle and nerve 6: 283–290PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1986

Authors and Affiliations

  • B. W. Festoff
  • D. Hantaï
  • C. Soria
  • J. Soria
  • M. Fardeau
    • 1
    • 2
  1. 1.University of Kansas/V.A. Medical CenterKansas CityUSA
  2. 2.Hôpital Lariboisière, Hôtel Dieu and INSERM UParisFrance

Personalised recommendations