Red blood cells increase secretion of matrix metalloproteinases from human lung fibroblasts in vitro

Fredriksson, Karin; Liu, X. D.; Lundahl, Joachim; Klominek, Julius; Rennard, Stephen I.; Sköld, C. Magnus

doi:10.1152/ajplung.00057.2005

Cited by 27 publications

(29 citation statements)

References 51 publications

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“…Zymography revealed constitutive expression of the proform of MMP-2 (gelatinase) in cultures of HFL-1 cells, as has been previously reported for this cell type (19,20,34). Trace levels of processed MMP-2 were also detectable in the presence of HMC-1 cells, and higher levels in the presence of pHMC.…”

Section: Discussionsupporting

confidence: 79%

MMP dependence of fibroblast contraction and collagen production induced by human mast cell activation in a three-dimensional collagen lattice

Margulis¹,

Nocka²,

Wood³

et al. 2009

American Journal of Physiology-Lung Cellular and Molecular Phys

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Mast cell-fibroblast interactions may contribute to fibrosis in asthma and other disease states. Fibroblast contraction is known to be stimulated by coculture with the human mast cell line, HMC-1, or by mast cell-derived agents. Matrix metalloproteinases (MMPs) can also mediate contraction, but the MMP-dependence of mast cell-induced fibroblast contractility is not established, and the consequences of mast cell activation within the coculture system have not been fully explored. We demonstrate that activation of primary human mast cells (pHMC) with IgE receptor cross-linking, or activation of HMC-1 with C5a, enhanced contractility of human lung fibroblasts in a three-dimensional collagen lattice system. This enhanced contractility was inhibited by the pan-MMP antagonist, batimastat, and was transferrable in the conditioned medium of activated mast cells. Exogenously added MMPs promoted gel contraction by mediating the proteolytic activation of latent transforming growth factor-beta (TGF-beta). Consistent with this, fibroblast contraction induced by mast cell activation was enhanced by addition of excess latent TGF-beta to the cultures. Batimastat inhibited this response, suggesting that MMPs capable of activating latent TGF-beta were released following mast cell activation in coculture with fibroblasts. Collagen production was also stimulated by activated mast cells in an MMP-dependent manner. MMP-2 and MMP-3 content of the gels increased in the presence of activated mast cells, and inhibition of these enzymes blocked the contractile response. These findings demonstrate the MMP dependence of mast cell-induced fibroblast contraction and collagen production.

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Section: Discussionsupporting

confidence: 79%

MMP dependence of fibroblast contraction and collagen production induced by human mast cell activation in a three-dimensional collagen lattice

Margulis¹,

Nocka²,

Wood³

et al. 2009

American Journal of Physiology-Lung Cellular and Molecular Phys

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“…39 We now showed that TGF-b2-induced a-SMA expression and MLC phosphorylation in RPE cells are inhibited by both 17b-estradiol and progesterone. Moreover, both TGF-b2-induced fibronectin production and expression of MMPs, which mediate remodeling of the ECM and contribute to collagen gel contraction, 40 were also attenuated by these female sex hormones in RPE cells. These various effects of female sex hormones may thus give rise to inhibition of the contraction of proliferative fibrocellular membranes stimulated by TGF-b in PVR.…”

Section: Discussionmentioning

confidence: 99%

Inhibition by Female Sex Hormones of Collagen Gel Contraction Mediated by Retinal Pigment Epithelial Cells

Kimura¹,

Orita²,

Fujitsu³

et al. 2014

Invest. Ophthalmol. Vis. Sci.

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“…However, co-culture of fibroblasts and monocytes results in the activation of pro-MMP-2 [17,55]. Among other factors, neutrophil elastase is also known to augment the conversion of the 72-kDa form of MMP-2 to the 66-kDa form in lung fibroblasts [55,56]. …”

Section: Discussionmentioning

confidence: 99%

Macrophage migration inhibitory factor: a mediator of matrix metalloproteinase-2 production in rheumatoid arthritis

et al. 2006

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Rheumatoid arthritis (RA) is a chronic inflammatory disease characterized by destruction of bone and cartilage, which is mediated, in part, by synovial fibroblasts. Matrix metalloproteinases (MMPs) are a large family of proteolytic enzymes responsible for matrix degradation. Macrophage migration inhibitory factor (MIF) is a cytokine that induces the production of a large number of proinflammatory molecules and has an important role in the pathogenesis of RA by promoting inflammation and angiogenesis.In the present study, we determined the role of MIF in RA synovial fibroblast MMP production and the underlying signaling mechanisms. We found that MIF induces RA synovial fibroblast MMP-2 expression in a time-dependent and concentrationdependent manner. To elucidate the role of MIF in MMP-2 production, we produced zymosan-induced arthritis (ZIA) in MIF gene-deficient and wild-type mice. We found that MMP-2 protein levels were significantly decreased in MIF gene-deficient compared with wild-type mice joint homogenates. The expression of MMP-2 in ZIA was evaluated by immunohistochemistry (IHC). IHC revealed that MMP-2 is highly expressed in wild-type compared with MIF gene-deficient mice ZIA joints. Interestingly, synovial lining cells, endothelial cells, and sublining nonlymphoid mononuclear cells expressed MMP-2 in the ZIA synovium. Consistent with these results, in methylated BSA (mBSA) antigen-induced arthritis (AIA), a model of RA, enhanced MMP-2 expression was also observed in wild-type compared with MIF gene-deficient mice joints. To elucidate the signaling mechanisms in MIF-induced MMP-2 upregulation, RA synovial fibroblasts were stimulated with MIF in the presence of signaling inhibitors. We found that MIF-induced RA synovial fibroblast MMP-2 upregulation required the protein kinase C (PKC), c-jun N-terminal kinase (JNK), and Src signaling pathways. We studied the expression of MMP-2 in the presence of PKC isoform-specific inhibitors and found that the PKCδ inhibitor rottlerin inhibits MIF-induced RA synovial fibroblast MMP-2 production. Consistent with these results, MIF induced phosphorylation of JNK, PKCδ, and c-jun. These results indicate a potential novel role for MIF in tissue destruction in RA. AIA = antigen-induced arthritis; BCA = bicinchoninic acid; CO 2 = carbon dioxide; COX2 = cyclo-oxygenase 2; DAPI = 4',6-diamidino-2-phenylindole dihydrochloride; DMSO = dimethyl sulfoxide; ECL = enhanced chemiluminescence; ED 50 = Median Effective Dose; ELISA = enzyme-linked immunosorbent assay; FBS = fetal bovine serum; IFN-γ; = interferon-γ; IHC = immunohistochemistry; IL-1β; = interleukin-1β; Jak = janus kinase; JNK = cjun N-terminal kinase; MAPK/ERK = mitogen-activated protein kinase extracellular-signal-regulated kinase; mBSA = methylated bovine serum albumin; MIF = macrophage migration inhibitory factor; MMP = matrix metalloproteinase; MT-MMP = membrane-type matrix metalloproteinase; NF-κB = nuclear factor-κB; OCT = optimal cutting temperature compound; PAGE = polyacrylamide gel electrophoresis; PB...

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Red blood cells increase secretion of matrix metalloproteinases from human lung fibroblasts in vitro

Abstract: . Red blood cells increase secretion of matrix metalloproteinases from human lung fibroblasts in vitro.

Cited by 27 publications

References 51 publications

MMP dependence of fibroblast contraction and collagen production induced by human mast cell activation in a three-dimensional collagen lattice

MMP dependence of fibroblast contraction and collagen production induced by human mast cell activation in a three-dimensional collagen lattice

Inhibition by Female Sex Hormones of Collagen Gel Contraction Mediated by Retinal Pigment Epithelial Cells

Macrophage migration inhibitory factor: a mediator of matrix metalloproteinase-2 production in rheumatoid arthritis

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