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Human Latent PMN Leukocyte Collagenase and Regulation of Activity via Disulfide-Thiol Interchange as Catalyzed by the Glutathione Cycle

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Book cover Structural and Functional Aspects of Enzyme Catalysis

Abstract

Since the initial demonstration of collagenolytic activity in leukocytes [1], it has been shown that the enzyme exists in both active and latent forms in extracts of human leukocytes [2], The latent collagenase can be activated by other active neutral proteinases [3–5] with a concomitant decrease in molecular weight of 10,000–20,000. In previous years various proteolytic enzymes have been used by many groups to activate latent collagenases obtained from a variety of other tissues and a multistep scheme has been proposed for collagenase activation by limited proteolysis [6–9].

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Author information

Authors and Affiliations

  1. Fakultät für Chemie, Lehrstuhl für Biochemie Universität Bielefeld, Universitätsstraße, D-4800, Bielefeld 1, Germany

    H. W. Macartney

Authors
  1. H. Tschesche
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  2. H. W. Macartney
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Editor information

Editors and Affiliations

  1. Physiologisch-Chemisches Institut, Technische Universität, Biedersteiner Straße 29, D-8000, München 40, Germany

    Hermann Eggerer

  2. Max-Planck-Institut für Biochemie, Am Klopferspitz, D-8033, Martinsried, Germany

    Robert Huber

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© 1981 Springer-Verlag Berlin Heidelberg

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Tschesche, H., Macartney, H.W. (1981). Human Latent PMN Leukocyte Collagenase and Regulation of Activity via Disulfide-Thiol Interchange as Catalyzed by the Glutathione Cycle. In: Eggerer, H., Huber, R. (eds) Structural and Functional Aspects of Enzyme Catalysis. Colloquium der Gesellschaft für Biologische Chemie 23.–25. April 1981 in Mosbach/Baden, vol 32. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-81738-0_14

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  • DOI: https://doi.org/10.1007/978-3-642-81738-0_14

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-81740-3

  • Online ISBN: 978-3-642-81738-0

  • eBook Packages: Springer Book Archive

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