Linked Life Data

10403463

Source:http://linkedlifedata.com/resource/pubmed/id/10403463

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1999-7-29
pubmed:abstractText
Previous studies have shown a correlation between the production of certain matrix metalloproteinases (MMPs), especially the gelatinases, by malignant tumors and the progression of these cancers as they invade and metastasize through the extracellular matrix and basement membranes. However, very few of these studies examined this relationship in human oral cancer in vivo, and none addressed the issue of how combinations of the MMPs may further enhance tumor progression. To determine which MMPs are produced in vivo by human oral cancers, we used specific anti-human-MMP antibodies and immunocytochemistry (ICC) methods to examine oral cancer tissue specimens from 20 surgery patients. The ICC data indicated that 72-kDa (72K-GL) and 92-kDa gelatinases (92K-GL) were produced in vivo by discreet clusters of tumor cells and by stromal fibroblasts, vascular endothelial cells (72K-GL), and PMNs (92K-GL). Some stromal fibroblasts near the tumors also appeared to produce fibroblast-type collagenase (FIB-CL), a finding confirmed by Western blot analysis of media conditioned by oral tumor explant cultures. ICC results indicated that 5 of the 20 tumors coincidentally produced all three MMPs. To examine how the two gelatinases and FIB-CL may interact in vitro to degrade fibrillar type I collagen, a major structural component of the extracellular matrix, we used a modified FIB-CL activity assay. Combinations of the gelatinases and FIB-CL were incubated with a 3H-collagen substrate, with the results compared with the combination of stromelysin-1 (SL-1, a superactivator of FIB-CL) and FIB-CL. 92K-GL caused a nine-fold increase in collagenase activity, equivalent to SL-1, while 72K-GL produced a four-fold increase. These results indicate that human oral cancers produce 92K-GL, 72K-GL, and FIB-CL in vivo and that the gelatinases and FIB-CL cooperate to enhance collagen degradation greatly in vitro.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-0345
pubmed:author
pubmed:issnType
Print
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1354-61
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10403463-Antibodies, pubmed-meshheading:10403463-Basement Membrane, pubmed-meshheading:10403463-Blotting, Western, pubmed-meshheading:10403463-Carcinoma, Squamous Cell, pubmed-meshheading:10403463-Collagen, pubmed-meshheading:10403463-Collagenases, pubmed-meshheading:10403463-Disease Progression, pubmed-meshheading:10403463-Endothelium, Vascular, pubmed-meshheading:10403463-Extracellular Matrix, pubmed-meshheading:10403463-Fibroblasts, pubmed-meshheading:10403463-Gelatinases, pubmed-meshheading:10403463-Humans, pubmed-meshheading:10403463-Immunohistochemistry, pubmed-meshheading:10403463-Matrix Metalloproteinase 1, pubmed-meshheading:10403463-Matrix Metalloproteinase 2, pubmed-meshheading:10403463-Matrix Metalloproteinase 3, pubmed-meshheading:10403463-Matrix Metalloproteinase 9, pubmed-meshheading:10403463-Metalloendopeptidases, pubmed-meshheading:10403463-Mouth Neoplasms, pubmed-meshheading:10403463-Neoplasm Invasiveness, pubmed-meshheading:10403463-Neutrophils, pubmed-meshheading:10403463-Radiopharmaceuticals, pubmed-meshheading:10403463-Tritium
pubmed:year
1999
pubmed:articleTitle
92K-GL (MMP-9) and 72K-GL (MMP-2) are produced in vivo by human oral squamous cell carcinomas and can enhance FIB-CL (MMP-1) activity in vitro.
pubmed:affiliation
Department of Orthodontics, University of Alabama at Birmingham, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't