p38 kinase mediates nitric oxide-induced apoptosis of chondrocytes through the inhibition of protein kinase C ζ by blocking autophosphorylation

Js, Kim; Zy, Park; Yj, Yoo; Yu, Shiying; Js, Chun

doi:10.1038/sj.cdd.4401511

Cited by 26 publications

(22 citation statements)

References 33 publications

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“…Effectively, there is evidence that SNP induces chondrocyte apoptosis through the activation of p38MAPK, the nuclear translocation of NK-κB, the increase in p53 protein phosphorylation and finally, the increase in caspase-3 activation [35,39]. The observation that chondroitin sulfate reduces SNP-induced apoptosis is in agreement with a report showing that chondroitin sulfate and heparan sulfate diminished the apoptosis of lung fibroblasts by abolishing caspase-3 and caspase-7 cleavage [40].…”

Section: Discussionsupporting

confidence: 86%

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Chondroitin Sulfate Inhibits the Nuclear Translocation of Nuclear Factor‐κB in Interleukin‐1β‐Stimulated Chondrocytes

Jomphe

Gabriac

Hale

et al. 2007

Basic Clin Pharma Tox

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Chondroitin sulfate is referred as a symptomatic slow-acting drug for osteoarthritis because it improves articular function, and reduces joint swelling and effusion. In addition, chondroitin sulfate prevents joint space narrowing of the knee. We hypothesized that the anti-inflammatory effect of chondroitin sulfate is associated to a decrease in the activation of mitogen-activated protein kinases (MAPK) and of the transcription factors nuclear factor-κ B (NF-κ B) and activator protein-1 (AP-1). Cultured rabbit chondrocytes were stimulated with interleukin-1 β (IL-1 β ) in presence of chondroitin sulfate. Nuclear translocation of NF-κ B and AP-1, and nitrite concentrations (as an index for nitric oxide) was assessed 48 hr later. The effect of chondroitin sulfate on IL-1 β activation of extracellular signal-regulated kinase 1/2 (Erk1/2) and p38MAPK was documented by immunoblot. The effect of chondroitin sulfate on sodium nitroprusside-induced apoptosis was evaluated with the terminal deoxynucleotidyl transferase-mediated dUTP-biotin nick end labelling assay. Chondroitin sulfate reduced IL-1 β -induced NF-κ B nuclear translocation, but not AP-1 translocation, it decreased IL-1 β -induced phosphorylation of Erk1/2 and abrogated p38MAPK phosphorylation, but did not prevent IL-1 β -induced increase in nitrite. Finally, chondroitin sulfate decreased nitroprusside-induced apoptosis of the chondrocytes. These results suggest that some of the biological activities of chondroitin sulfate may be associated to the reduction in Erk1/2 and p38MAPK phosphorylation and nuclear transactivation of NF-κ B.

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Section: Discussionsupporting

confidence: 86%

“…There is evidence that SNP-induced apoptosis is closely associated to the activation of p38MAPK [35]. As a consequence, Fig.…”

Section: Effect Of Chondroitin Sulfate On Chondrocytes Proliferation mentioning

confidence: 87%

Chondroitin Sulfate Inhibits the Nuclear Translocation of Nuclear Factor‐κB in Interleukin‐1β‐Stimulated Chondrocytes

Jomphe

Gabriac

Hale

et al. 2007

Basic Clin Pharma Tox

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“…Immunoprecipitation was conducted as previously described (20). Briefly, cells were lysed by NP-40 lysis buffer and the lysates were then precipitated with negative control mouse antibody (Santa Cruz Biotechnology, Inc.) or mouse monoclonal antibody against either CIP2A or Plk1 (Santa Cruz Biotechnology, Inc.).…”

Section: Immunoprecipitation and Strep Pull-downmentioning

confidence: 99%

CIP2A Modulates Cell-Cycle Progression in Human Cancer Cells by Regulating the Stability and Activity of Plk1

Kim

et al. 2013

Cancer Research

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Abnormal cell-cycle control can lead to aberrant cell proliferation and cancer. The oncoprotein cancerous inhibitor of protein phosphatase 2A (CIP2A) is an inhibitor of protein phosphatase 2A (PP2A) that stabilizes c-Myc. However, the precise role of CIP2A in cell division is not understood. Herein, we show that CIP2A is required for mitotic progression by regulating the polo-like kinase (Plk1). With mitotic entry, CIP2A translocated from the cytoplasm to the nucleus, where it was enriched at spindle poles. CIP2A depletion delayed mitotic progression, resulting in mitotic abnormalities independent of PP2A activity. Unexpectedly, CIP2A interacted directly with the polo-box domain of Plk1 during mitosis. This interaction was required to maintain Plk1 stability by blocking APC/C-Cdh1-dependent proteolysis, thereby enhancing the kinase activity of Plk1 during mitosis. We observed strong correlation and in vivo interactions between these two proteins in multiple human cancer specimens. Overall, our results established a novel function for CIP2A in facilitating the stability and activity of the pivotal mitotic kinase Plk1 in cell-cycle progression and tumor development. Cancer Res; 73(22); 6667-78. Ó2013 AACR.

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“…After growth to 90% confluency, chondrocytes were washed and maintained in serum-free DMEM for 48 h. Supernatant fractions prepared from chondrocytes were precipitated using the trichloroacetic acid/acetone method. Proteins from the precipitated supernatant were reduced, alkylated, and trypsin-digested, as described previously (19). Briefly, digested proteins were loaded onto fused silica capillary columns, and placed in line with an Agilent HP1100 quaternary LC pump.…”

Section: Rt-pcr Analysis and Quantitative Real Time Pcr (Qrt-pcr)-totalmentioning

confidence: 99%

Cytokine-like 1 (CYTL1) Regulates the Chondrogenesis of Mesenchymal Cells

Kim

Ryoo

Chun

2007

Journal of Biological Chemistry

100

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To identify novel molecules regulating chondrogenesis and cartilage development, we screened a cartilage-specific expressed sequence tag data base. Cytokine-like 1 (Cytl1), a possible cytokine candidate with unknown function that was originally identified in bone marrow-derived CD34-positive cells, was selected for functional characterization. In view of the initial observation that Cytl1 is predominantly expressed in chondrocytes and cartilage, we investigated its possible role in chondrogenesis and hypertrophic maturation of chondrocytes. Cytl1 expression was very low in mesenchymal cells, dramatically increased during chondrogenesis, and decreased during hypertrophic maturation, both in vivo and in vitro. The role of Cytl1 in chondrogenesis and hypertrophic maturation was examined by treating chondrifying mesenchymal cells with exogenous Cytl1 or ectopic expression of Cytl1. Notably, exogenous Cytl1 caused chondrogenic differentiation of mouse limb bud mesenchymal cells during micromass culture. Lentivirus-mediated overexpression of Cytl1 additionally induced chondrogenic differentiation of mesenchymal cells. However, Cytl1 did not affect the hypertrophic maturation of chondrocytes. Cytl1 exerted its chondrogenic effect via stimulation of Sox9 transcriptional activity. In addition, Cytl1 caused expression of insulin-like growth factor 1, which has a capacity to induce chondrogenesis. Thus, our results collectively suggest that chondrocyte-specific Cytl1 regulates chondrogenesis as a novel autocrine factor, but not hypertrophic maturation of chondrocytes during cartilage development.Cartilage formation during embryonic development begins with the aggregation of mesenchymal cells, which ultimately differentiate into chondrocytes. Differentiated chondrocytes proliferate rapidly and secrete a cartilage-specific extracellular matrix such as type II collagen and sulfated proteoglycan to form cartilage. The cartilage serves as a template for endochondral ossification, which requires the maturation of hypertrophic chondrocytes (1-4). These sequential events during chondrogenesis and cartilage formation are precisely regulated by various growth factors released from cartilage elements and perichondrium. Secreted growth factors exert their effects by modulating intracellular signaling (1, 2). Although several regulatory growth factors have been identified, including bone morphogenetic proteins, fibroblast growth factors, insulin-like growth factor-1 (IGF-1), 2 transforming growth factor-␤, and parathyroid hormone-related peptide, the precise mechanisms of regulation of chondrogenesis and cartilage development remain to be elucidated. In this study, we analyze a cartilagespecific expressed sequence tag (EST) data base in an attempt to identify novel molecules that modulate chondrogenesis and cartilage development.The EST data base provides important information on novel genes displaying tissue-specific expression profiles (5-7). We analyzed the human cartilage UniGene library (8), and selected Cytl1 as a possible candid...

show abstract

p38 kinase mediates nitric oxide-induced apoptosis of chondrocytes through the inhibition of protein kinase C ζ by blocking autophosphorylation

Cited by 26 publications

References 33 publications

Chondroitin Sulfate Inhibits the Nuclear Translocation of Nuclear Factor‐κB in Interleukin‐1β‐Stimulated Chondrocytes

Chondroitin Sulfate Inhibits the Nuclear Translocation of Nuclear Factor‐κB in Interleukin‐1β‐Stimulated Chondrocytes

CIP2A Modulates Cell-Cycle Progression in Human Cancer Cells by Regulating the Stability and Activity of Plk1

Cytokine-like 1 (CYTL1) Regulates the Chondrogenesis of Mesenchymal Cells

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