Linked Life Data

9354769

Source:http://linkedlifedata.com/resource/pubmed/id/9354769

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-11-21
pubmed:abstractText
Matrix metalloprotease-9 (MMP-9; 92-kd type IV collagenase, gelatinase B) is regarded as important for degradation of the basement membrane and extracellular matrix during cancer invasion and other tissue-remodeling events. Expression of MMP-9 was analyzed in 22 cases of human ductal breast cancer by immunohistochemistry and in 8 of these cases also by in situ hybridization. For immunohistochemistry we used affinity-purified polyclonal antibodies as well as a MMP-9-specific monoclonal antibody (clone 6-6B). Three different stromal cell types with a positive MMP-9 immunoreaction were identified morphologically: neutrophils and macrophage-like cells in all cases and vascular cells in 16 of 22 cases. Double immunofluorescence with antibodies to CD68 conclusively demonstrated MMP-9 expression in macrophages. To identify the positive vascular cells, we employed antibodies to von Willebrand factor and PAL-E for identification of endothelial cells, high molecular weight melanoma-associated antigen for pericytes, and alpha-smooth muscle actin for vascular smooth muscle cells. Using conventional and confocal double immunofluorescence microscopy, colocalization of MMP-9 was seen with high molecular weight melanoma-associated antigen, the pericyte marker, whereas little or no coexpression was seen with alpha-smooth muscle actin. Virtually no coexpression was seen with the endothelial cell markers PAL-E and von Willebrand factor. In situ hybridization showed that MMP-9 mRNA colocalized with MMP-9 immunoreactivity in macrophages and vascular structures, whereas no MMP-9 mRNA was detected in neutrophils. No MMP-9 immunostaining or in situ hybridization signal was detected in cancer cells in any of the cases. Based on these results, it is concluded that MMP-9 in human breast cancer is located in tumor-infiltrating stromal cells, including neutrophils, macrophages, and vascular pericytes, and that the latter two cell types also produce this metalloprotease. We suggest that the MMP-9 produced in pericytes may play a role in extracellular matrix degradation during tumor angiogenesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0023-6837
pubmed:author
pubmed:issnType
Print
pubmed:volume
77
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
345-55
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9354769-Actins, pubmed-meshheading:9354769-Antibodies, Monoclonal, pubmed-meshheading:9354769-Antigens, CD, pubmed-meshheading:9354769-Antigens, CD31, pubmed-meshheading:9354769-Antigens, Differentiation, Myelomonocytic, pubmed-meshheading:9354769-Breast Neoplasms, pubmed-meshheading:9354769-Carcinoma, Ductal, Breast, pubmed-meshheading:9354769-Collagenases, pubmed-meshheading:9354769-Connective Tissue Cells, pubmed-meshheading:9354769-Fluorescent Antibody Technique, Indirect, pubmed-meshheading:9354769-Humans, pubmed-meshheading:9354769-Immunohistochemistry, pubmed-meshheading:9354769-In Situ Hybridization, pubmed-meshheading:9354769-Macrophages, pubmed-meshheading:9354769-Matrix Metalloproteinase 9, pubmed-meshheading:9354769-Melanoma, pubmed-meshheading:9354769-Muscle, Smooth, Vascular, pubmed-meshheading:9354769-RNA, Messenger, pubmed-meshheading:9354769-von Willebrand Factor
pubmed:year
1997
pubmed:articleTitle
Expression of matrix metalloprotease-9 in vascular pericytes in human breast cancer.
pubmed:affiliation
Department of Pathology, Rigshospitalet, Copenhagen, Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't