Literature DB >> 3236068

Inhibition of guanidinobenzoatase: evidence for multiple forms of this protease on different tumour cells.

F S Steven1, M M Griffin, A J Freemont, J Johnson.   

Abstract

Guanidinobenzoatase is a proteolytic enzyme capable of degrading fibronectin and is a tumour associated enzyme. 9-Aminoacridine is a competitive inhibitor of this enzyme and has been used to locate cells possessing this enzyme in wax embedded sections by means of fluorescent microscopy. Naturally occurring inhibitors of guanidinobenzoatase can be extracted from different tissues. These inhibitors show selectivity in their ability to inhibit the binding of 9-aminoacridine to different types of tumour cells which have invaded human liver tissue. Inhibition is non-competitive and reversible. The results indicate that guanidinobenzoatase exists in a number of different forms on the surface of different tumour cells. These different forms of the enzyme were recognised by inhibitors obtained from different organs. It is suggested that these inhibitors may have a regulatory role in tumour cell migration.

Entities:  

Mesh:

Substances:

Year:  1988        PMID: 3236068     DOI: 10.3109/14756368809040717

Source DB:  PubMed          Journal:  J Enzyme Inhib        ISSN: 1026-5457


  2 in total

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

Authors:  F S Steven; L A Williams; H Maier; J Arndt; H Weidauer; A Born
Journal:  J Cancer Res Clin Oncol       Date:  1990       Impact factor: 4.553

2.  Studies on the activity of a protease associated with cells at the advancing edge of human tumour masses in frozen sections.

Authors:  F S Steven; M M Griffin; H Maier; H Weidauer; W F Mangel; M Altmannsberger
Journal:  Br J Cancer       Date:  1988-07       Impact factor: 7.640

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.