Interleukin 1 alpha mediates collagenase synthesis stimulated by phorbol 12-myristate 13-acetate

Fini, M. Elizabeth; Strissel, Katherine J.; Girard, M T; Mays, Jacqueline W.; Rinehart, William B.

doi:10.1016/s0021-9258(19)78124-1

Cited by 63 publications

(7 citation statements)

References 45 publications

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“…We were not able to measure the concentration of IL-1 in neutrophil-CM because of the lack of appropriate antibodies to the rabbit protein. We thus chose to block the action of endogenous IL-1 with IL-1ra, given that this protein was previously shown to antagonize IL-1 activity in rabbit fibroblasts including those from the cornea [39]. IL-1ra is a member of the IL-1 family of proteins [40], shares 30% amino acid sequence identity with IL-1␤, and binds to IL-1 receptor types I and II without inducing apparent cellular activation.…”

Section: Discussionmentioning

confidence: 99%

Enhancement by neutrophils of collagen degradation by corneal fibroblasts

Fukuda

Lü

et al. 2003

Journal of Leukocyte Biology

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Activated corneal fibroblasts and infiltrated leukocytes are thought to contribute to corneal ulceration. The potential roles of neutrophil-fibroblast and cell-matrix interactions in the degradation of stromal collagen associated with corneal ulceration have now been investigated with the use of three-dimensional cultures of rabbit cells in collagen gels. Degradation of collagen fibrils during culture was measured by spectrophotometric determination of released hydroxyproline. Whereas corneal fibroblasts alone degraded collagen fibrils to a small extent, neutrophils did not. However, the addition of neutrophils or neutrophil-conditioned medium (CM) to cultures of corneal fibroblasts resulted in a marked increase in the amount of collagen degraded by the fibroblasts. The effect of CM from neutrophils cultured in collagen gels on collagen degradation by corneal fibroblasts was greater than that of medium conditioned by neutrophils in monolayer culture. Immunoblot as well as reverse transcription and real-time polymerase chain reaction analyses revealed that neutrophil-CM stimulated the synthesis of matrix metalloproteinase (MMP)-1 and MMP-3 by corneal fibroblasts. The stimulatory effect of neutrophils on collagen degradation by corneal fibroblasts was inhibited by the synthetic MMP inhibitor ilomastat and by interleukin-1 (IL-1) receptor antagonist. These results suggest that factors secreted by collagen-stimulated neutrophils augment collagen degradation by corneal fibroblasts through a stimulatory effect on MMP synthesis and that IL-1 released by neutrophils may contribute to this effect.

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Section: Discussionmentioning

confidence: 99%

Enhancement by neutrophils of collagen degradation by corneal fibroblasts

Fukuda

Lü

et al. 2003

Journal of Leukocyte Biology

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“…Incubation of cultures with SOF-OLIGO also diminished the basal expression of collagenase in RSF cultured on FN. This may be explained by the fact that in some cases, interleukin-1 acts in an autocrine manner to increase the basal level of collagenase synthesized by synovial cells (Fini et al, 1994;Tremble, P., and Z. Werb, unpublished observations). Interleukin-1 increases transcrip-tion of collagenase at several sites in the promoter, one of which is the AP1 site at (or equivalent to) -72 to -66 (Lafyatis et al, 1990;Sirum-Connolly et al, 1991), so a decrease in the expression of c-Fos would also diminish the baseline synthesis of collagenase.…”

Section: Integrin-mediated Signaling Cascades Regulate Components Of the Api Complexmentioning

confidence: 99%

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

Tremble

Damsky

Werb

1995

The Journal of Cell Biology

112

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Abstract. We have shown previously that the expression of collagenase is upregulated in rabbit synovial fibroblasts cultured on a substrate of antibody to the o~5 chain of the et5131 integrin fibronectin receptor or on the 120-kD cellbinding 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 APl-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-los oligonucleotides diminished both basal and induced expression of the -139/ -42 collagenase promoter-reporter construct and decreased expression of the endogenous collagenase gene. Therefore, one of the pathways that transduce signals activated by the a5131 integrin fibronectin receptor propagates its response through promoters that contain AP1-and PEA3-responsive DNA sequences.

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“…Both IL-1α and IL-1β bind to the same IL-1 receptor and show identical biological activities [73]. The proinflammatory cytokine IL-1 has been shown to regulate the expression of MMPs in several cell types including dermal fibroblasts [74], cardiac fibroblasts [75], chondrocytes [76], mesenchymal stem cells [77], and corneal fibroblasts [78]. IL-1β was thus found to stimulate the production of MMP1, MMP3, and MMP9 by corneal fibroblasts cultured in a collagen gel as well as to increase collagen degradation by corneal fibroblasts in this culture system [58,79].…”

Section: Collagen Degradation Resulting From Exposure Of Corneal Fibroblasts To Alarminsmentioning

confidence: 99%

Pivotal Role of Corneal Fibroblasts in Progression to Corneal Ulcer in Bacterial Keratitis

Nishida

Sugioka

Fukuda

et al. 2021

IJMS

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The shape and transparency of the cornea are essential for clear vision. However, its location at the ocular surface renders the cornea vulnerable to pathogenic microorganisms in the external environment. Pseudomonas aeruginosa and Staphylococcus aureus are two such microorganisms and are responsible for most cases of bacterial keratitis. The development of antimicrobial agents has allowed the successful treatment of bacterial keratitis if the infection is diagnosed promptly. However, no effective medical treatment is available after progression to corneal ulcer, which is characterized by excessive degradation of collagen in the corneal stroma and can lead to corneal perforation and corneal blindness. This collagen degradation is mediated by both infecting bacteria and corneal fibroblasts themselves, with a urokinase-type plasminogen activator (uPA)-plasmin-matrix metalloproteinase (MMP) cascade playing a central role in collagen destruction by the host cells. Bacterial factors stimulate the production by corneal fibroblasts of both uPA and pro-MMPs, released uPA mediates the conversion of plasminogen in the extracellular environment to plasmin, and plasmin mediates the conversion of secreted pro-MMPs to the active form of these enzymes, which then degrade stromal collagen. Bacterial factors also stimulate expression by corneal fibroblasts of the chemokine interleukin-8 and the adhesion molecule ICAM-1, both of which contribute to recruitment and activation of polymorphonuclear neutrophils, and these cells then further stimulate corneal fibroblasts via the secretion of interleukin-1. At this stage of the disease, bacteria are no longer necessary for collagen degradation. In this review, we discuss the pivotal role of corneal fibroblasts in corneal ulcer associated with infection by P. aeruginosa or S. aureus as well as the development of potential new modes of treatment for this condition.

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Interleukin 1 alpha mediates collagenase synthesis stimulated by phorbol 12-myristate 13-acetate

Cited by 63 publications

References 45 publications

Enhancement by neutrophils of collagen degradation by corneal fibroblasts

Enhancement by neutrophils of collagen degradation by corneal fibroblasts

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

Pivotal Role of Corneal Fibroblasts in Progression to Corneal Ulcer in Bacterial Keratitis

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