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Tumor Cysteine Proteinases, Platelet Aggregation and Metastasis

  • Chapter
Hemostatic Mechanisms and Metastasis

Part of the book series: Developments in Oncology ((DION,volume 22))

Abstract

Cysteine proteinases are a subclass of endopeptidases which require activation by thiol reagents (1). This group of enzymes includes the plant proteinase papain, the lysosomal cysteine proteinases (cathepsins B, H and L) and the cytosolic calcium-activated neutral proteinases (CANP). Sequence homologies among the cysteine proteinases suggest that they may have a common evolutionary origin. Takio et al. (2) compared the amino acid sequences of papain and of rat liver cathepsins B and H and found substantial sequence homologies among the three. Surrounding the active site cysteine, cathepsin B has 10 of 11 and cathepsin H 9 of 11 amino acids found in papain. Overall, however, cathepsin H is more closely homologous to papain than to cathepsin B. A peptide containing the active site cysteine residue of chicken skeletal muscle CANP was isolated and found to consist of 7 residues of which 3 are common to the active sites of papain and cathepsin B (3) and cathepsin H (2). Bajkowski and Frankfater (4, 5) have provided evidence that there are functional homologies as well as structural homologies between the active sites of cathepsin B and papain.

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  1. Bonnie F. Sloane
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  2. Philip G. Cavanaugh
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  3. Kenneth V. Honn
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Editors and Affiliations

  1. Department of Radiation Oncology, Wayne State University, 210 Science Hall, Detroit, 48202, MI, USA

    Kenneth V. Honn

  2. Department of Pharmacology, Wayne State University, 540 East Canfield, Detroit, 48201, MI, USA

    Bonnie F. Sloane

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Sloane, B.F., Cavanaugh, P.G., Honn, K.V. (1984). Tumor Cysteine Proteinases, Platelet Aggregation and Metastasis. In: Honn, K.V., Sloane, B.F. (eds) Hemostatic Mechanisms and Metastasis. Developments in Oncology, vol 22. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-3831-4_12

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