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Abstract

Serine proteases initiate several complex biochemical responses to sudden, life-threatening situations. The immediate and localized activation of coagulant serine proteases prevents mammals from bleeding to death. The immediate activation of complement serine proteases kills common bacteria and prevents bacterial sepsis. The granules of cytotoxic lymphocytes (CTL) are packages which contain a unique subfamily of serine proteases and the pore-forming protein, perforin. These sequestered serine proteases are induced during the differentiation of lymphocytes to become competent killer cells (Lobe et al., 1986; Gershenfeld and Weisman, 1986). In vivo, lymphocytes laden with toxic granules accumulate at sites of graft rejection (Mueller et al., 1988). Exocytosis exposes the granule contents to high extracellular concentrations of calcium, the cation required for cell lysis. In vitro, freshly isolated natural killer (NK) lymphocytes and lymphokine-activated T lymphocytes release these protease-packed granules during killing. Proteases alone do not mediate lysis. Perform is necessary for cell lysis. The proteases undoubtably perform significant functions immediately associated with cytolysis.

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© 1993 Birkhäuser Boston

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Hudig, D. et al. (1993). Serine Protease Control of Lymphocyte-Mediated Cytolysis. In: Sitkovsky, M.V., Henkart, P.A. (eds) Cytotoxic Cells: Recognition, Effector Function, Generation, and Methods. Birkhäuser Boston. https://doi.org/10.1007/978-1-4684-6814-4_27

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  • DOI: https://doi.org/10.1007/978-1-4684-6814-4_27

  • Publisher Name: Birkhäuser Boston

  • Print ISBN: 978-1-4684-6816-8

  • Online ISBN: 978-1-4684-6814-4

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