Linked Life Data

8766524

Source:http://linkedlifedata.com/resource/pubmed/id/8766524

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1996-9-13
pubmed:abstractText
We examined production and tissue localization of matrix metalloproteinase (MMP)-1 (tissue collagenase), MMP-2 (gelatinase A), MMP-3 (stromelysin-1), MMP-9 (gelatinase B), tissue inhibitors of metalloproteinase (TIMP)-1 and TIMP-2 in human breast carcinomas. In more than half of the cases, MMP-1, MMP-2, MMP-9, TIMP-1 and TIMP-2 were immunolocalized in carcinoma cells and MMP-2 was on the carcinoma cell membranes as well, whereas MMP-3 was positively stained in less than 15% of the cases. MMP-1 staining in carcinoma cells was significantly higher in scirrhous carcinoma than in other types of carcinoma. MMP-9 expression was remarkably higher in the carcinoma cases with lymphnode metastasis than in the non-metastatic cases. MMP-3 was mainly expressed in T-lymphocytes infiltrated in the tumor stroma. Stromal fibroblasts were positive for all these MMPs except for MMP-3. The TIMP-1 levels released into the culture media by carcinoma tissues were significantly lower than those by fibroadenoma tissues, although there were no significant differences in the levels of MMP-1, MMP-2, MMP-9 and TIMP-2. Gelatin zymographical analyses showed that the activation rate of the zymogen of MMP-2 (proMMP-2) is significantly higher in the more advanced carcinoma group with lymphnode metastasis than in the metastasis-negative and fibroadenoma groups. These data indicate that MMP-1, MMP-2 and MMP-9 are highly expressed in human breast carcinoma tissue and suggest that activation of proMMP-2 may be an indicator of lymphnode metastasis of the breast carcinoma.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0910-5050
pubmed:author
pubmed:issnType
Print
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
602-11
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8766524-Breast Neoplasms, pubmed-meshheading:8766524-Collagenases, pubmed-meshheading:8766524-Culture Techniques, pubmed-meshheading:8766524-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8766524-Female, pubmed-meshheading:8766524-Gelatinases, pubmed-meshheading:8766524-Glycoproteins, pubmed-meshheading:8766524-Humans, pubmed-meshheading:8766524-Immunoenzyme Techniques, pubmed-meshheading:8766524-Immunohistochemistry, pubmed-meshheading:8766524-Lymphatic Metastasis, pubmed-meshheading:8766524-Matrix Metalloproteinase 2, pubmed-meshheading:8766524-Matrix Metalloproteinase 3, pubmed-meshheading:8766524-Matrix Metalloproteinase 9, pubmed-meshheading:8766524-Metalloendopeptidases, pubmed-meshheading:8766524-Protease Inhibitors, pubmed-meshheading:8766524-Protein Biosynthesis, pubmed-meshheading:8766524-Tissue Inhibitor of Metalloproteinase-2, pubmed-meshheading:8766524-Tissue Inhibitor of Metalloproteinases
pubmed:year
1996
pubmed:articleTitle
Production of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human breast carcinomas.
pubmed:affiliation
The Second Department of Surgery, Nagoya City University Medical School, Nagoya, Japan.
pubmed:publicationType
Journal Article