Document Detail


Induction of M(r) 92,000 type IV collagenase expression in a squamous cell carcinoma cell line by fibroblasts.
MedLine Citation:
PMID:  7850814     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A previous investigation (Matsumoto et al., J. Oral Pathol. Med., 18: 498-501, 1989) has shown that the in vitro invasion of a collagen gel by squamous cell carcinoma can be substantially augmented in the presence of fibroblasts. Therefore, we undertook a study to determine if the production of collagenase(s) by a squamous cell carcinoma cell line, UM-SCC-1, was up-regulated by fibroblasts. Cocultivation of UM-SCC-1 cells with MDA-TU-138 fibroblasts, both established from the oral cavity, resulted in a dose-dependent increase in the activity of a M(r) 92,000 gelatinase as shown by zymography. Augmented M(r) 92,000 gelatinase activity was a consequence of the stimulation of the UM-SCC-1 cells by a soluble, fibroblast-derived factor since this effect could be reproduced with fibroblast-conditioned medium but not with glutaraldehyde-fixed fibroblasts. The increased M(r) 92,000 gelatinolytic activity could be accounted for by an increase in M(r) 92,000 type IV collagenase (MMP-9) protein, as demonstrated by Western blotting for this metalloproteinase. Trypsin treatment of the fibroblast-conditioned medium abolished its ability to increase MMP-9 secretion by UM-SCC-1 cells. Furthermore, fractionation of the fibroblast-conditioned medium revealed a M(r) 3,000-10,000 soluble factor(s) which was responsible for the augmented production of MMP-9 by UM-SCC-1 cells. To determine if the increased production of MMP-9, in response to the fibroblasts, was a consequence of increased promoter activity, UM-SCC-1 cells were transiently transfected with a chloramphenicol acetyltransferase reporter driven by the MMP-9 promoter and plated on plastic or on a monolayer of MDA-TU-138 fibroblasts. A 4-5-fold stimulation of MMP-9 promoter activity was observed with UM-SCC-1 cells plated with the MDA-TU-138 fibroblasts, when compared with similarly transfected cells recultured on plastic. In conclusion, we have demonstrated that MMP-9 expression in a squamous cell carcinoma cell line is augmented by a fibroblast-derived protein(s). This finding indicates a role for stromal cells in the regulation of MMP-9 expression in squamous cell carcinoma. The ability of fibroblasts to regulate MMP-9 expression in tumor cells in vitro may explain the observation that the amount of M(r) 92,000 type IV collagenase mRNA in tumor cells is highest at the tumor:stromal interface of resected squamous cell carcinoma.
Authors:
E Lengyel; R Gum; J Juarez; G Clayman; M Seiki; H Sato; D Boyd
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Cancer research     Volume:  55     ISSN:  0008-5472     ISO Abbreviation:  Cancer Res.     Publication Date:  1995 Feb 
Date Detail:
Created Date:  1995-03-14     Completed Date:  1995-03-14     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2984705R     Medline TA:  Cancer Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  963-7     Citation Subset:  IM    
Affiliation:
Department of Tumor Biology, Anderson Cancer Center, Houston, Texas 77030.
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MeSH Terms
Descriptor/Qualifier:
Carcinoma, Squamous Cell / enzymology*
Collagenases / biosynthesis*,  metabolism
Enzyme Induction
Fibroblasts / physiology*
Humans
Matrix Metalloproteinase 9
Molecular Weight
Sensitivity and Specificity
Solubility
Trypsin / pharmacology
Tumor Cells, Cultured
Grant Support
ID/Acronym/Agency:
R01CA58311/CA/NCI NIH HHS; R01DE10845/DE/NIDCR NIH HHS; R29CA5159/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
EC 3.4.21.4/Trypsin; EC 3.4.24.-/Collagenases; EC 3.4.24.35/Matrix Metalloproteinase 9

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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