scholarly journals Differential Regulation of Eotaxin-1/CCL11 and Eotaxin-3/CCL26 Production by the TNF-α and IL-4 Stimulated Human Lung Fibroblast

2006 ◽  
Vol 29 (6) ◽  
pp. 1102-1109 ◽  
Author(s):  
Akiko Rokudai ◽  
Yasuhito Terui ◽  
Ryoko Kuniyoshi ◽  
Yuji Mishima ◽  
Yuko Mishima ◽  
...  
Keyword(s):  
Human Lung ◽  
Differential Regulation ◽  
Lung Fibroblast ◽  
Human Lung Fibroblast ◽  
Tnf Α

scholarly journals Differential regulation of metalloproteinase production, proliferation and chemotaxis of human lung fibroblasts by PDGF, Interleukin-1β and TNF-α

2000 ◽  
Vol 9 (3-4) ◽  
pp. 155-160 ◽  
Author(s):  
Masahiro Sasaki ◽  
Masayuki Kashima ◽  
Takefumi Ito ◽  
Akiko Watanabe ◽  
Noriko Izumiyama ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Human Lung ◽  
Lung Fibroblast ◽  
Differential Sensitivity ◽  
Lung Fibroblasts ◽  
Type I ◽  
Dependent Manner ◽  
Human Lung Fibroblast ◽  
Human Lung Fibroblasts ◽  
Tnf Α

Fibroblast migration, proliferation, extracellular matrix protein synthesis and degradation,all of which play important roles in inflammation, are them selves induced by various growth factors and cytokines. Less is known about the interaction of these substances on lung fibroblast function in pulmonary fibrosis.The goal of this study was to investigate the effects of PDGF alone and in combination with IL–1β and TNF–α on the production of human lung fibroblast matrix metalloproteinases, proliferation, and the chemotactic response. The assay for MMPs activity against FITC labeled type I and IV collagen was based on the specificity of the enzyme cleavage of collagen. Caseinolytis and gelatinolytic activities of secreted proteinases were analyzed by zymography. Fibronectin in conditioned media was measured using human lung fibronectin enzyme immunoassay. Cell proliferation was measured by 3H-Thymidine incorporation assay. Cell culture supernatants were tested for PGE2 content by ELISA. Chemotactic activity was measured using the modified Boyden chamber.Matrix metalloproteinase assay indicated that IL–1β, TNF–α and PDGF induced intestitial collagenase (MMP-1) production. MMP assay also indicated that IL–1β and TNF–α had inhibitory effects on MMP-2,9(gelatinaseA,B) production. Casein zymography confirmed that IL–1β stimulated stromlysin (matrix metalloproteinase 3; MMP–3) and gelatin zymography demonstrated that TNF–α induced MMP–9 production in human lung fibroblast, whereas PDGF alone did not. PDGF in combination with IL–1β and TNF–α induced MMP–3 and MMP–9 activity, as demonstrated by zymography. PDGF stimulated lung fibroblast proliferation in a concentration-dependent manner, whereas IL–1β and TNF–α alone had no effect. In contrast, the proliferation of human lung fibroblasts by PDGF was inhibited in the presence of IL–1β and TNF–α, and this inhibition was not a consequence of any elevation of PGE2. PDGF stimulated fibroblast chemotaxis in a concentrationdependent manner, and this stimulation was augmented by combining PDGF with IL–1β and TNF–α.These findings suggested that PDGF differentially regulated MMPs production in combination with cytokines, and further that MMP assay and zymography had differential sensitivity for detecting MMPs. The presence of cytokines with PDGF appears to modulate the proliferation and chemotaxis of human lung fibroblasts.

Effects of silica on human lung fibroblast in culture

2001 ◽  
Vol 270 (1-3) ◽  
pp. 135-139 ◽  
Author(s):  
G Arcangeli ◽  
V Cupelli ◽  
G Giuliano
Keyword(s):  
Human Lung ◽  
Lung Fibroblast ◽  
Human Lung Fibroblast

Surfactant downregulates synthesis of DNA and inflammatory mediators in normal human lung fibroblasts

1996 ◽  
Vol 270 (1) ◽  
pp. L159-L163 ◽  
Author(s):  
M. J. Thomassen ◽  
J. M. Antal ◽  
B. P. Barna ◽  
L. T. Divis ◽  
D. P. Meeker ◽  
...  
Keyword(s):  
Inflammatory Cytokines ◽  
Inflammatory Mediators ◽  
Human Lung ◽  
Thymidine Incorporation ◽  
Interleukin 1 ◽  
S Phase ◽  
Lung Fibroblast ◽  
Lung Fibroblasts ◽  
Human Lung Fibroblast ◽  
Normal Human

The initial inflammatory event in the adult respiratory distress syndrome (ARDS) is followed by fibroproliferation and a cascade of fibroblast-derived mediators. Because lung fibroblasts may be exposed to surfactant as well as inflammatory cytokines during ARDS, we hypothesized that surfactant might modulate fibroblast activity. We previously demonstrated that surfactant inhibited production of inflammatory cytokines from endotoxin-stimulated human alveolar macrophages. In the current study the effects of surfactant on normal human lung fibroblast proliferative capacity and mediator production were examined. Both synthetic (Exosurf) and natural (Survanta) surfactant inhibited fibroblast [3H]thymidine incorporation. Examination of pre-S-phase events indicated stimulation of the immediate response gene, c-fos, and no effect on the G1/S cyclin, cyclin D1, suggesting that the surfactant block occurred elsewhere before S phase. The antioxidant N-acetyl-L-cysteine (NAC), like surfactant, inhibited [3H]thymidine incorporation. Furthermore, menadione, a generator of intracellular H2O2, stimulated fibroblast [3H]thymidine incorporation, and this was inhibited by surfactant. Interleukin-1 (IL-1)-stimulated secretion of the inflammatory mediators, IL-6 and prostaglandin E2, was also inhibited by surfactant. These data suggest that surfactant may modify lung fibroblast participation in ARDS sequelae by downregulating DNA synthesis and secondary inflammatory mediator production.

Dynamic protein hydrogels with reversibly tunable stiffness regulate human lung fibroblast spreading reversibly

2019 ◽  
Vol 55 (36) ◽  
pp. 5235-5238 ◽  
Author(s):  
Linglan Fu ◽  
Amanda Haage ◽  
Na Kong ◽  
Guy Tanentzapf ◽  
Hongbin Li
Keyword(s):  
Human Lung ◽  
Lung Fibroblast ◽  
Fibroblast Cells ◽  
Human Lung Fibroblast ◽  
Protein Hydrogels ◽  
Tunable Stiffness

Fibroblast cells change their morphology reversibly in response to changes in protein hydrogel stiffness.

Cytokine-cytokine synergy and protein kinase C in the regulation of lung fibroblast leukemia inhibitory factor

1994 ◽  
Vol 266 (4) ◽  
pp. L426-L435 ◽  
Author(s):  
J. A. Elias ◽  
T. Zheng ◽  
N. L. Whiting ◽  
A. Marcovici ◽  
T. K. Trow
Keyword(s):  
Protein Synthesis ◽  
Transforming Growth Factor Beta ◽  
Leukemia Inhibitory Factor ◽  
Transforming Growth Factor ◽  
Human Lung ◽  
Lung Fibroblast ◽  
Inhibitory Factor ◽  
Tgf Beta ◽  
Human Lung Fibroblast ◽  
Mrna Induction

Studies were undertaken to characterize the cytokines and cytokine-cytokine interactions that stimulate human lung fibroblast leukemia inhibitory factor (LIF) production and the mechanisms of these regulatory effects were investigated. Unstimulated fibroblasts did not produce significant amounts of LIF, whereas recombinant interleukin-1 alpha (rIL-1 alpha), transforming growth factor-beta (TGF-beta), and recombinant tumor necrosis factor (rTNF) were dose-dependent stimulators of LIF production. TGF-beta and rIL-1 alpha also interacted in a synergistic fashion to further increase LIF elaboration. Under all conditions alterations in LIF production were associated with comparable alterations in LIF mRNA accumulation. The kinetics of mRNA induction, however, differed with rIL-1-induced LIF mRNA being readily detected after 2 h, TGF-beta 1 induction peaking after 16-24 h, and the induction caused by rIL-1 alpha plus TGF-beta 1 being most prominent after 2-4 h and decreasing with additional incubation. Protein synthesis was not required for LIF induction. In addition, even though A23187 was an effective stimulator of LIF production, the calmodulin antagonists W-7 and trifluoperazone dichoride (TFP) did not significantly alter the LIF-stimulatory effects of IL-1 and TGF-beta. PKC did appear to play an important role in this induction, however, since LIF was induced by PMA and cytokine induction of LIF production was markedly diminished by chronic phorbol ester preincubation, staurosporine, and H-7, but not by HA1004. These studies demonstrate that 1) rIL-1, TGF-beta, TNF, agents that increase intracellular calcium and agents that activate PKC, stimulate lung fibroblast LIF production; 2) rIL-1 and TGF-beta interact in a synergistic fashion to further increase fibroblast LIF production; and 3) rIL-1 and TGF-beta stimulate lung fibroblast LIF production via a pretranslational activation pathway that is largely PKC-dependent and protein synthesis-, cyclic nucleotide-, and calmodulin-independent. Cytokine-stimulated LIF production may play an important role in homeostasis and repair in the human lung.

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