Evidence for the Participation of Poly(ADPribosyl)ation in Collagenase Gene Expression in Rabbit Synovial Fibroblasts after Treatment with Active Oxygen Released by Xanthin/Xanthinoxidase

1992 ◽  
pp. 199-202
Author(s):  
Wilhelm Ehrlich ◽  
Hans Huser ◽  
Hans Kröger
Keyword(s):  
Gene Expression ◽  
Synovial Fibroblasts ◽  
Active Oxygen ◽  
Collagenase Gene

Regulation of Collagenase Gene Expression in Synovial Fibroblasts

1990 ◽  
Vol 580 (1 Structure, Mo) ◽  
pp. 355-374 ◽  
Author(s):  
CONSTANCE E. BRINCKERHOFF ◽  
DAVID T. AUBLE
Keyword(s):  
Gene Expression ◽  
Synovial Fibroblasts ◽  
Collagenase Gene

scholarly journals Components of the nuclear signaling cascade that regulate collagenase gene expression in response to integrin-derived signals.

1995 ◽  
Vol 129 (6) ◽  
pp. 1707-1720 ◽  
Author(s):  
P Tremble ◽  
C H Damsky ◽  
Z Werb
Keyword(s):  
Gene Expression ◽  
Synovial Fibroblasts ◽  
Plasma Fibronectin ◽  
Reporter Construct ◽  
Fibronectin Receptor ◽  
Receptor Antibody ◽  
Fibronectin Fragment ◽  
Integrin Fibronectin Receptor ◽  
Collagenase Gene ◽  
In Cells

We have shown previously that the expression of collagenase is upregulated in rabbit synovial fibroblasts cultured on a substrate of antibody to the alpha 5 chain of the alpha 5 beta 1 integrin fibronectin receptor or on the 120-kD cell-binding chymotryptic fragment of plasma fibronectin, but remains at basal levels in cells plated on intact plasma fibronectin. We now have identified some of the components of a signaling pathway that couples the fibronectin receptor to the induction of collagenase transcription. We studied the control of collagenase gene expression in cells adhering to the 120-kD fragment of fibronectin, to antifibronectin receptor antibody, or to plasma fibronectin by transiently introducing promoter-reporter constructs into rabbit synovial fibroblasts before plating cells on these matrices. The constructs contained segments of the human collagenase promoter regulating transcription of chloramphenicol acyl transferase. Expression of constructs containing the -1200/-42-bp segment or the -139/-42-bp segment of the collagenase promoter inserted upstream from the reporter gene was induced to similar extents in cells plated on the 120-kD fragment of fibronectin or on anti-fibronectin receptor antibody, relative to that in fibroblasts plated on fibronectin. The expression of the construct containing the -66/-42-bp segment of the promoter was not regulated and was similar to that of the parent pBLCAT2 plasmid, suggesting that the -139/-67 region of the collagenase promoter, which contains PEA3- and AP1-binding sites, regulates the transcription of collagenase caused by integrin-derived signals. Expression of a reporter construct containing only the PEA3 and AP1 sites in the collagenase promoter (-90/-67) also increased in cells plated on the 120-kD fragment of fibronectin or on anti-fibronectin receptor antibody, relative to that in cells plated on fibronectin. Mutations in either the AP1 or PEA3 site of this minimal promoter abrogated its activity in cells plated on these inductive ligands. Expression of c-fos mRNA increased within 1 h of plating cells on the 120-kD fibronectin fragment or on anti-fibronectin receptor antibody, relative to that in cells plated on fibronectin. c-Fos protein accumulated in the nuclei of fibroblasts within 10 min of plating on the 120-kD fibronectin fragment. The increase in c-Fos was required for the increase in collagenase in cells plated on the 120-kD fibronectin fragment: incubation of cells with antisense, but not sense, c-fos oligonucleotides diminished both basal and induced expression of the -139/-42 collagenase promoter-reporter construct and decreased expression of the endogenous collagenase gene.(ABSTRACT TRUNCATED AT 400 WORDS)

scholarly journals Changes in cell shape correlate with collagenase gene expression in rabbit synovial fibroblasts.

1984 ◽  
Vol 98 (5) ◽  
pp. 1662-1671 ◽  
Author(s):  
J Aggeler ◽  
S M Frisch ◽  
Z Werb
Keyword(s):  
Gene Expression ◽  
Cell Morphology ◽  
Cell Shape ◽  
Shape Change ◽  
Synovial Fibroblasts ◽  
Matrix Proteins ◽  
Duration Of Treatment ◽  
Neutral Proteinase ◽  
Altered Cell ◽  
Collagenase Gene

Induction of the neutral proteinase, collagenase, is a marker for a specific switch in gene expression observed in rabbit synovial fibroblasts. A variety of agents, including 12-O-tetradecanoylphorbol-13-acetate, cytochalasins B and D, trypsin, chymotrypsin, poly(2-hydroxyethylmethacrylate), and trifluoperazine induced this change in gene expression. Induction of collagenase by these agents was always correlated with a marked alteration in cell morphology, although the cells remained adherent to the culture dishes. The amount of collagenase induced was positively correlated with the degree of shape change produced by a given concentration and, to some extent, with the duration of treatment. Altered cell morphology was required only during the first few hours of treatment with inducing agents; after this time collagenase synthesis continued for up to 6 d even when agents were removed and normal flattened cell morphology was regained. All agents that altered cell morphology also produced a characteristic switch in protein secretion phenotype, characterized by the induction of procollagenase (Mr 53,000 and 57,000) and a neutral metalloproteinase (Mr 51,000), which accounted for approximately 25% and 15% of the protein secreted, respectively. Secretion of another neutral proteinase, plasminogen activator, did not correlate with increased collagenase secretion. In contrast, synthesis and secretion of a number of other polypeptides, including the extracellular matrix proteins, collagen and fibronectin, were concomitantly decreased. That changes in cell shape correlated with a program of gene expression manifested by both degradation and synthesis of extracellular macromolecules may have broad implications in development, repair, and pathologic conditions.

scholarly journals The extracellular matrix ligands fibronectin and tenascin collaborate in regulating collagenase gene expression in fibroblasts.

1994 ◽  
Vol 5 (4) ◽  
pp. 439-453 ◽  
Author(s):  
P Tremble ◽  
R Chiquet-Ehrismann ◽  
Z Werb
Keyword(s):  
Gene Expression ◽  
Extracellular Matrix ◽  
Type I Collagen ◽  
Serum Proteins ◽  
Synovial Fibroblasts ◽  
Type I ◽  
Mixed Substrate ◽  
Amino Terminal ◽  
Collagenase Gene ◽  
In Cells

Tenascin (TN) is a large oligomeric glycoprotein that is present transiently in the extracellular matrix (ECM) of cells and is involved in morphogenetic movements, tissue patterning, and tissue repair. It has multiple domains, both adhesive and anti-adhesive, that interact with cells and with fibronectin (FN) and other ECM macromolecules. We have studied the consequences of the interaction of TN with a FN matrix on gene expression in rabbit synovial fibroblasts. Fibroblasts plated on a mixed substrate of FN and TN, but not on FN alone, upregulated synthesis of four genes: collagenase, stromelysin, the 92-kDa gelatinase, and c-fos. Although the fibroblasts spread well on both FN and FN/TN substrates, nuclear c-Fos increased within 1 h only in cells that were plated on FN/TN. TN did not induce the expression of collagenase in cells plated on substrates of type I collagen or vitronectin (VN). Moreover, soluble TN added to cells adhering to a FN substrate or to serum proteins had no effect, suggesting that TN has an effect only in the context of mixed substrates of FN and TN. Collagenase increased within 4 h of plating on a FN/TN substrate and exhibited kinetics similar to those for induction of collagenase gene expression by signaling through the integrin FN receptor. Arg-Gly-Asp peptide ligands that recognize either the FN receptor or the VN receptor and function-perturbing anti-integrin monoclonal antibodies diminished the interaction of fibroblasts with a mixed substrate of FN, TN, and VN, but had no effect on the adhesion of fibroblasts to a substrate of FN and VN, suggesting that both receptors recognize the complex. Anti-TN68, an antibody that recognizes an epitope in the carboxyl-terminal type III repeats involved in the interaction of TN with both FN and cells, blocked the inductive effect of the FN/TN substrate, whereas anti-TNM1, an antibody that recognizes an epitope in the amino-terminal anti-adhesive region of epidermal growth factor-like repeats, had no effect. These data suggest that transient alteration of the composition of ECM by addition of proteins like TN may regulate the expression of genes involved in cell migration, tissue remodeling, and tissue invasion, in regions of tissue undergoing phenotypic changes.

scholarly journals THU0003 Altered gene expression in rheumatoid arthritis synovial fibroblasts after few culture passages

2001 ◽  
Author(s):  
U Müller-Ladner ◽  
E Neumann ◽  
M Judex ◽  
F Kullmann ◽  
J Grifka ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Gene Expression ◽  
Synovial Fibroblasts ◽  
Altered Gene Expression ◽  
Altered Gene

Suppression of collagenase gene expression by all-trans and 9-cis retinoic acid is ligand dependent and requires both RARs and RXRs

1995 ◽  
Vol 57 (4) ◽  
pp. 575-589 ◽  
Author(s):  
Luying Pan ◽  
Christian Eckhoff ◽  
Constance E. Brinckerhoff
Keyword(s):  
Gene Expression ◽  
Retinoic Acid ◽  
Collagenase Gene

scholarly journals Cell culture and passaging alters gene expression pattern and proliferation rate in rheumatoid arthritis synovial fibroblasts

2010 ◽  
Vol 12 (3) ◽  
pp. R83 ◽  
Author(s):  
Elena Neumann ◽  
Birgit Riepl ◽  
Anette Knedla ◽  
Stephanie Lefèvre ◽  
Ingo H Tarner ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Gene Expression ◽  
Cell Culture ◽  
Expression Pattern ◽  
Gene Expression Pattern ◽  
Synovial Fibroblasts ◽  
Proliferation Rate
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