Implications of Proteases and Protease Inhibitors in Neurite Outgrowth

  • D. Monard
Part of the Colloquium der Gesellschaft für Biologische Chemie 18.–20. April 1985 in Mosbach/Baden book series (MOSBACH, volume 36)

Abstract

There is increasing experimental evidence that the proteolytic activity associated with cells can strongly affect their behavior. The role of cell-surface protease activity in cell migration has been stressed in many developmental systems [1,2]. Migrating cells, including cells transformed by oncogenic viruses, have more cell-associated proteolytic activity than stationary, differentiated cells [3,4]. Cell-associated proteolytic activity is usually estimated by measuring cell-derived plasminogen activators [5]. Plasminogen activators are serine proteases that convert plasminogen to plasmin, which then degrades substrates such as fibrin [6] or casein [7]. In the nervous system, an increased amount of plasminogen activator can be attributed to cultured, cerebellar granule neurons if the dissociation and the initiation of the cultures take place at the developmental stage at which these cells are migrating [8]. It was also demonstrated that, in neuroblastoma cells, plasminogen activator activity can be preferentially localized at the growth cone when neurite outgrowth is induced by treatment with dibutyryl cyclic AMP [9]. These results have suggested that such proteolytic activity is required for the migratory behavior of the growth cone during neurite outgrowth [9].

Keywords

Migration Serine Trypsin Thrombin Creatine 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1985

Authors and Affiliations

  • D. Monard
    • 1
  1. 1.Friedrich Miescher-InstitutBaselSwitzerland

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