Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1988-2-2
pubmed:abstractText
The proteolytic activity of serum against two synthetic polypeptide substrates conjugated with 7-amino-4-methylcoumarine which are known to be highly specific substrates for lysosomal cathepsin B-like cysteine proteinase, was studied in normal individuals and in patients with breast and colorectal cancer. The results showed that both substrates are cleaved in different ways and their hydrolysis is very poorly sensitive to inhibitors of cysteine proteinases. On the other hand, cleavage is intensively inhibited by disodium-EDTA which is known as an activator of cysteine proteinases. This indicates that lysosomal conditions are quite different from serum which is an unstable mixture of various enzymes and their substrates. It was also demonstrated that hydrolysis of the tested substrates is not probably realized by cysteine proteinases but it can be performed by cooperation of other serum proteinases. Moreover, our results confirmed that serum activity of these enzymes can be significantly higher in patients with breast cancer, particularly with metastasis, than in healthy women. A slight insignificant increase was observed also in patients with colorectal cancer.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0028-2685
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
601-8
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Clinical experience with the testing of serum proteinase activity by cathepsin B-like sensitive amino acid derivatives of 7-amino-4-methylcoumarine.
pubmed:affiliation
Department of Pathology, Faculty of Medicine, Palacký University, Olomouc, Czechoslovakia.
pubmed:publicationType
Journal Article