Abstract
The ability to invade normal tissues which surround primary tumors and to subsequently metastasize to distant sites are the distinguishing features of malignant neoplasms [1–5]. In order to invade and metastasize, tumor cells must overcome several structural barriers presented by host tissues [2, 3, 5]. In most mammalian tissues, structural barriers consist of a meshwork of tightly packed and highly cross-linked collagen fibrils. These fibrils are embedded in a viscoelastic ground substance whose major components are structural macromolecular complexes, i.e. proteoglycans, glycoproteins, and elastin [6–11]. The normal packing of these macro-molecules may leave little or no space for the free movement of tumor cells. Cleavage by proteinases may therefore provide a mechanism by which tumor cells invade [12–20]. Numerous reports of increased proteolytic (collagenolytic) activity associated with various tumors, obtained either by extraction or tissue culture techniques, have strengthened the concept of a primary involvement of proteinases in tumor invasion [16–36]. Considerable progress has since been achieved in analyzing the role of matrix-degrading enzymes in the invasion of tumors. Despite this, the cellular origin and the local regulation (synthesis, secretion, activation, inhibition) of most of these enzymes remain in doubt, mainly because of the heterogeneity of tumor specimens used by the various investigators [16–36].
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Pauli, B.U., Kuettner, K.E. (1982). The regulation of invasion by a cartilage-derived anti-invasion factor. In: Liotta, L.A., Hart, I.R. (eds) Tumor Invasion and Metastasis. Developments in Oncology, vol 7. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-7511-8_16
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DOI: https://doi.org/10.1007/978-94-009-7511-8_16
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