Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1992-10-8
pubmed:abstractText
The increased expression of proteolytic systems is one of the characteristics of transformed and malignant cells and their evaluations in whole tumor homogenates were considered as possible diagnostic and/or prognostic factors. Abnormal intracellular distribution, increased activities and secretion of cysteine proteinases (CPs) cathepsin B (Cat B) and L (Cat L), were associated with tumor progression. In the present study of matched pairs of breast carcinoma and normal breast tissue, the activities of Cat B and Cat L in breast carcinoma homogenates were found to be 20 and 50 fold higher, respectively, than in normal tissues. In contrast, a decrease in total inhibitory activity of cysteine proteinase inhibitors (CPIs) was observed but an average ratio between tumor and normal tissues was only 0.75. One of the CPIs, stefin A, was also determined immunochemically. The activities of CPs and CPIs were compared to the increased levels of cathepsin D (Cat D) activities in individual patients, but no statistically significant correlations were found. We correlated CPs and CPIs with morphological and receptor data as well as the axillary lymph node metastases. There was no statistical correlation of CP and CPIs with the number of lymph node metastases. However, highly elevated levels of Cat B and Cat L and lowered CPI activities in tumor cytosols were often associated with poorly differentiated carcinomas and those with negative ER and PR values. We conclude that cysteine-dependent proteolysis may play an important role in breast tumors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CSTA protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CTSL1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin B, http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin L, http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins, http://linkedlifedata.com/resource/pubmed/chemical/Cystatin A, http://linkedlifedata.com/resource/pubmed/chemical/Cystatins, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Estrogen, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Progesterone
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0177-3593
pubmed:author
pubmed:issnType
Print
pubmed:volume
373
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
595-604
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:1515089-Amino Acid Sequence, pubmed-meshheading:1515089-Breast Neoplasms, pubmed-meshheading:1515089-Cathepsin B, pubmed-meshheading:1515089-Cathepsin L, pubmed-meshheading:1515089-Cathepsins, pubmed-meshheading:1515089-Cystatin A, pubmed-meshheading:1515089-Cystatins, pubmed-meshheading:1515089-Cysteine Endopeptidases, pubmed-meshheading:1515089-Cysteine Proteinase Inhibitors, pubmed-meshheading:1515089-Cytosol, pubmed-meshheading:1515089-Endopeptidases, pubmed-meshheading:1515089-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:1515089-Female, pubmed-meshheading:1515089-Humans, pubmed-meshheading:1515089-Molecular Sequence Data, pubmed-meshheading:1515089-Neoplasm Metastasis, pubmed-meshheading:1515089-Receptors, Estrogen, pubmed-meshheading:1515089-Receptors, Progesterone
pubmed:year
1992
pubmed:articleTitle
Cystatins and cathepsins in breast carcinoma.
pubmed:affiliation
Department of Biochemistry, J. Stefan Institute, Ljubljana, Slovenia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't