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  • Title: Proteolytic enzymes and catabolism: enhanced release of granulocyte proteinases in uremic intoxication and during hemodialysis.
    Author: Heidland A, Hörl WH, Heller N, Heine H, Neumann S, Heidbreder E.
    Journal: Kidney Int Suppl; 1983 Dec; 16():S27-36. PubMed ID: 6376917.
    Abstract:
    Proteinases are classified into four groups according to their catalytic mechanisms: the serine, cysteine (thiol), aspartic (carboxyl), and metallo-proteinases. Neutrophil granulocytes contain a variety of neutral proteinases and two acid proteinases. Lysosomal proteinases are released from cells during phagocytosis, cell death, or exposure to antigen-antibody complexes, complement factors, and toxins. Under pathological conditions, massive proteinase release may cause tissue injury and degradation of plasma proteins. Plasma proteolytic activity is controlled by inhibitors of blood systems (antithrombin III, C1 inhibitor, and plasmin inhibitor) and by inhibitors against proteinases of various body cells (alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, beta 1-collagenase inhibitor, and inter-alpha-trypsin inhibitor). Intracellular proteinases are controlled by different cytosolic inhibitors. In hypercatabolic states (septicemia, trauma, burns), the concentrations of many plasma proteins, including proteinase inhibitors, are decreased. Kallikrein-kinin, complement, and fibrinolytic systems may be activated, probably due to enhanced proteinase activity. In acute renal failure, there is a release of granulocyte neutral proteinases. The plasma concentration of the elastase-alpha 1-proteinase inhibitor complex is simultaneously increased. Granulocytes of chronically uremic patients treated with diet or regular dialysis have a slightly to markedly reduced proteinase content as compared with normal controls. There is a dramatic rise of the plasma elastase alpha 1-proteinase inhibitor complex during hemodialysis treatment.
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