The status of trypsin-like enzymes in squamous-cell carcinoma of the head and neck region.

Abstract

The activity of two proteases associated with tumour cells was studied using frozen sections of squamous-cell carcinoma and fluorescent probes for the enzymes. Four fluorescent probes were used to define the enzymic status of guanidinobenzoatase on the surface of the squamous carcinoma cells. Each of four probes demonstrated the location of cells possessing inactive guanidinobenzoatase, whereas adjacent cells of the same tumour exhibited active enzyme. It was shown that the inactive form of the enzyme was an inhibitor-enzyme complex that could be dissociated. In contrast, all of the squamous carcinoma cells possessed active trypsin-like enzymes that were recognised by fluorescent aprotinin molecules. The observed variation in enzymic status of these two tumour-associated enzyme systems is discussed in the context of a possible biological control mechanism for cell migration.

• Authors: F S Steven, L A Williams, H Maier, J Arndt, H Weidauer, A Born
• Journal: Journal of cancer research and clinical oncology (J Cancer Res Clin Oncol) Vol. 116 Issue 1 Pg. 57-64 ( 1990) ISSN: 0171-5216 [Print] Germany
• PMID: 2312606 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Rhodamines
• Aminacrine
• N-benzyloxycarbonylargininamidorhodamine
• Carboxylic Ester Hydrolases
• guanidinobenzoate esterase
• Endopeptidases
• Trypsin

Topics

• Aminacrine
• Carboxylic Ester Hydrolases (analysis, immunology)
• Carcinoma, Squamous Cell (enzymology)
• Cell Movement
• Endopeptidases
• Fluorescence
• Head and Neck Neoplasms (enzymology)
• Humans
• Rhodamines
• Trypsin (analysis)