Stimulation of TIMP‐1 production by oncostatin m in human articular cartilage

Nemoto, Osamu; Yamada, Harumoto; Mukaida, Masahiro; Shimmei, Masayuki

doi:10.1002/art.1780390404

Cited by 45 publications

(30 citation statements)

References 39 publications

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“…In extrapulmonary stromal cells, OSM stimulation in vitro induced the secretion of TIMP-1, a major inhibitor of MMP [42], suggesting that it might prevent ECM degradation. However, the effects of monocyte-derived OSM secretion on pulmonary stroma in a cytokine-rich milieu such as that of the tuberculous granuloma may be very different to data obtained in simple tissue-culture systems.…”

Section: Discussionmentioning

confidence: 99%

“…Although p38 was constitutively phosphorylated in monocytes, inhibition of p38 signalling reduced OSM secretion, suggesting that this pathway is necessary although not sufficient for maximal Mtb-induced OSM secretion. Although JNK phosphorylation occurred in response to both Mtb and CoMTb, inhibition did not affect OSM secretion.In extrapulmonary stromal cells, OSM stimulation in vitro induced the secretion of TIMP-1, a major inhibitor of MMP [42], suggesting that it might prevent ECM degradation. However, the effects of monocyte-derived OSM secretion on pulmonary stroma in a cytokine-rich milieu such as that of the tuberculous granuloma may be very different to data obtained in simple tissue-culture systems.…”

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confidence: 99%

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Monocyte‐dependent oncostatin M and TNF‐α synergize to stimulate unopposed matrix metalloproteinase‐1/3 secretion from human lung fibroblasts in tuberculosis

2008

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Leukocyte-derived matrix metalloproteinases (MMP) are implicated in the tissue destruction characteristic of tuberculosis (TB). The contribution of lung stromal cells to MMP activity in TB is unknown. Oncostatin M (OSM) is an important stimulus to extrapulmonary stromal MMP induction, but its role in regulation of pulmonary MMP secretion or pathophysiology of TB is unknown. We investigated OSM secretion from Mycobacterium tuberculosis (Mtb)-infected human monocytes/macrophages and the networking effects of such OSM on lung fibroblast MMP secretion. Mtb increased monocyte OSM secretion dose dependently in vitro. In vivo tuberculous granulomas immunostained positively for OSM. Further, conditioned media from Mtb-infected monocytes (CoMTb) induced monocyte OSM secretion (670 AE 55 versus 166 AE 14 pg/mL in controls), implicating an autocrine loop. Mtbinduced OSM secretion was prostaglandin (PG) sensitive, and required activation of surface G-protein coupled receptors. OSM induction was ERK MAP kinase dependent, p38-requiring but JNK-independent. OSM synergized with TNF-a, a key cytokine in TB granuloma formation, to stimulate pulmonary fibroblast MMP-1/-3 secretion, while suppressing secretion of tissue inhibitors of metalloproteinases-1/-2. In summary, Mtb infection of monocytes results in PG-dependent OSM secretion, which synergizes with TNF-a to drive functionally unopposed fibroblast MMP-1/-3 secretion, demonstrating a previously unrecognized role for OSM in TB.Key words: Human Á Inflammation Á Monocytes/macrophages Á Stromal cells Introduction Tuberculosis (TB) remains a major global health problem with over 8 million cases of overt clinical infection, and 2 million deaths annually. The pathological response to Mycobacterium tuberculosis (Mtb) infection is characterised by extensive tissue breakdown including caseous necrosis, and later fibrosis. Tissue destruction in TB requires degradation of matrix proteins including collagen and elastin, and several studies have implicated matrix metalloproteinases (MMP) in pathogenesis [1][2][3]. MMP are a group of 23 related zinc-dependent enzymes that together are capable of degrading all components of the extracellular matrix (ECM) [4]. MMP are inhibited in vivo by the tissue inhibitors of metalloproteinases (TIMP), and in general, overall proteolytic activity is determined by the molar ratio of MMP:TIMP. MMP secretion is induced by inflammatory cytokines, physical stimuli, or directly by some bacterial components [5]. Direct infection of mononuclear cells with Mtb has been shown to induce MMP-9 (gelatinase B), a process that depends in part on 6].In the lung, the principal structural supporting collagen is type I [7,8]. MMP-1 (interstitial collagenase) is the most abundant pulmonary enzyme capable of degrading type I collagen [5]. Several cell types secrete MMP-1 in TB [9,10] but there are no data on the role of fibroblast-derived MMP-1 in TB. However, stimulated fibroblasts are the most potent source of MMP-1 in the lung [11] and may cause type IV collagen and prote...

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Monocyte‐dependent oncostatin M and TNF‐α synergize to stimulate unopposed matrix metalloproteinase‐1/3 secretion from human lung fibroblasts in tuberculosis

2008

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“…Activation of one of the two pathways may depend on the physiological condition or, alternatively, distinct pathways may be used in different FS cell subpopulations (80,99). A similar complexity is reflected in the expression of tissue-inhibitors of metalloproteinases (TIMPs) in pituitary cells: constitutive TIMP-II expression was observed in the FS cell line TtT/GF (83), whereas several of the cytokines produced by pituitary cells (IL-6, IL-10, LIF) -which are probably also produced within the FS cell compartment -were found to induce TIMP-I expression but not TIMP-II expression in various cell types including mononuclear phagocytes (100,101). The expression of TIMPs has generally been related to the preservation of extracellular matrix (ECM) components in various tissues (101).…”

Section: New Perspectives In Fs Cell Physiologymentioning

confidence: 99%

History and perspectives of pituitary folliculo-stellate cell research

Allaerts¹,

Vankelecom²

2005

eur j endocrinol

157

129

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Historically, the study of folliculo-stellate (FS) cells of the anterior pituitary dates back to the onset of electron microscopical observation of the pituitary gland. The morphological and electrophysiological characteristics, topographical distribution and contribution to intercellular junctions of these FS cells have been instrumental to the understanding of their putative function. Moreover, many studies have documented the role of FS cells as a source of newly discovered peptides, growth factors and cytokines. Quantitative immunohistochemical observation of FS cells in situ and functional in vitro studies, using either cultured FS cells or cells from an immortalized FS cell line, forwarded the notion of immunophenotypical and functional heterogeneity of the FS cell group. Double immunolabeling with a classical FS cell marker (S-100 protein) and with major histocompatibility complex class II markers characteristic for dendritic cells (DC) have shown a considerable overlap of FS cells with DC. The latter cells are immunocompetent cells belonging to the mononuclear phagocyte system. In this review, the FS cell heterogeneity is discussed with respect to the question of their embryological origin and developmental fate and with respect to the physiological relevance of functionally heterogeneous subpopulations. Recent findings of a myeloid origin of part of the interstitial cells of the anterior pituitary are confronted by other developmental paradigms of pituitary cell differentiation. The possibility that FS cells represent an adult stem cell population of the pituitary is critically examined. Also the physiological role of FS cells in the interferon-g-and nitric oxide-mediated effects on pituitary hormone secretion is discussed. New approaches for the study of this enigmatic cell group using immortalized cell lines and new markers for an hitherto unrecognized pituitary cell population, the so-called 'side population', are evaluated.

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“…In addition, OSM has shown functions that are distinct from those of other members of the group. OSM stimulates tissue inhibitor of metalloproteinases 1 (TIMP-1) in synovial fibroblasts (25) and in human chondrocytes (26). We have recently shown that OSM can regulate the expression of IL-8, IL-6, and granulocyte-macrophage colonystimulating factor in cell culture (27) while other IL-6/ LIF cytokines do not.…”

mentioning

confidence: 99%

Oncostatin M stimulates monocyte chemoattractant protein‐1‐ and interleukin‐1‐induced matrix metalloproteinase‐1 production by human synovial fibroblasts in vitro

Langdon

Leith

Smith

et al. 1997

Arthritis & Rheumatism

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Objective. To measure levels of oncostatin M (OSM) in the synovial fluid of rheumatoid arthritis (FU) patients and to examine the activities of human OSM in the regulation of human synovial fibroblast (HSF) production of chemokines and matrix metalloproteinases (MMP-1 and MMP-3) in vitro.Methods. We examined the levels of OSM in the synovial fluids of patients with arthritis by an enzymelinked immunosorbent assay (ELISA). ELISA of cell culture supernatants and Northern blots were used to assess responses of HSF to interleukin-la (IL-la), OSM, and other members of the IL-6/leukemia inhibitory factor (IL-6/LIF) family of cytokines.Results. We detected variable levels of OSM antigen in 9 of 10 RA patient synovial fluids, but levelswere not detectable in 9 of 10 osteoarthritis (OA) patient fluids. Upon examining the responses of HSF in culture, OSM stimulated monocyte chemoattractant protein 1 (MCP-l), whereas RANTES secretion (regulated upon activation, normal T expressed and presumably secreted) was not altered by OSM alone. In IL-lainduced cells, OSM costimulation further enhanced MCP-1 release, but inhibited the release of RANTES and IL-8. Other members of the IL-6/LIF family of cytokines did not show these effects. OSM induced a small elevation of MMP-1 production over 2 and 3 days of stimulation (2-fold), and acted significantly to enhance IL-la-induced production of MMP-1 (to 8-fold Submitted for publication December 20, 1096; acccptcd in revised form July 15, 1097. and 9-fold at 48 and 72 hours, respectively). No effect of OSM was seen on MMP-3 secretion, either alone or in IL-la-costimulated cells.Conclusion. These results suggest that OSM has potentially important functions in the modulation of chemokine and metalloproteinase production by synovial cells of the joint.

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Stimulation of TIMP‐1 production by oncostatin m in human articular cartilage

Cited by 45 publications

References 39 publications

Monocyte‐dependent oncostatin M and TNF‐α synergize to stimulate unopposed matrix metalloproteinase‐1/3 secretion from human lung fibroblasts in tuberculosis

Monocyte‐dependent oncostatin M and TNF‐α synergize to stimulate unopposed matrix metalloproteinase‐1/3 secretion from human lung fibroblasts in tuberculosis

History and perspectives of pituitary folliculo-stellate cell research

Oncostatin M stimulates monocyte chemoattractant protein‐1‐ and interleukin‐1‐induced matrix metalloproteinase‐1 production by human synovial fibroblasts in vitro

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