Adiponectin increases MMP‐3 expression in human chondrocytes through adipor1 signaling pathway

Tong, Kwok-Man; Chen, Chao-Ping; Huang, Kui-Chou; Shieh, Dong-Chen; Cheng, Hsu-Chen; Tzeng, Chung‐Yuh; Chen, Kun-Hui; Chiu, Yung-Cheng; Tang, Chih‐Hsin

doi:10.1002/jcb.23059

Cited by 90 publications

(61 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…We have previously reported that leptin [Yeh et al, 2009] and GDNF [Lu et al, 2010a] enhance migration and invasion of glioma cells by increasing MMP production. Previous reports also showed that adiponectin, an adipokine, activates AMPK activation and upregulates MMP expression [Handy et al, 2010;Kang et al, 2010;Tong et al, 2011]. Here we also found that ghrelin affects the expression of MMP in human glioma cells (Suppl.…”

supporting

confidence: 77%

Ghrelin induces cell migration through GHS-R, CaMKII, AMPK, and NF-κB signaling pathway in glioma cells

Chen¹,

Huang

Chen

et al. 2011

J. Cell. Biochem.

View full text Add to dashboard Cite

Ghrelin is a newly discovered gastric peptide which stimulates food intake, energy balance, and growth hormone release. Recent reports have also shown that circulating ghrelin can efficiently reach the brain. However, the molecular mechanisms and pathophysiologic roles underlying ghrelin-induced glioma migration remain unclear. Glioma is the most common primary adult brain tumor with poor prognosis because of the spreading of tumor cell to the other regions of brain easily. In present study, we found that application of recombinant human ghrelin enhances the glioma cell migration in both rat C6 and human U251 cells. Ghrelin and its receptor GHS-R (growth hormone secretagogue receptor) are expressed in a wide variety of tissues and cell types, including various cancer cells. However, little is known about the expression of ghrelin or GHS-R in brain tumors. Here, we found that ghrelin increased GHS-R receptor up-regulation, and the enhancement of ghrelin-induced glioma cell motility markedly inhibited by a GHS-R antagonist. In addition, ghrelin-mediated migration was attenuated by treatment of CaMKII inhibitor, and AMPK inhibitors and pre-transfection with AMPK siRNA. Moreover, ghrelin stimulation also increased the phosphorylation of CaMKII and AMPK. Treatment with three different types of NF-κB inhibitors or pre-transfection with KM-IKKα, or KM-IKKβ also reduced ghrelin-induced glioma cell migration. Moreover, treatment of ghrelin also induced IKKα/β activation, IκBα phosphorylation, p65 phosphorylation at Ser(536), and increased NF-κB-DNA binding activity and κB-transcriptional activity. These results indicate that ghrelin enhances migration of glioma cells is mainly regulated by the GHS-R, CaMKII, AMPK, and NF-κB pathway.

show abstract

supporting

confidence: 77%

Ghrelin induces cell migration through GHS-R, CaMKII, AMPK, and NF-κB signaling pathway in glioma cells

Chen¹,

Huang

Chen

et al. 2011

J. Cell. Biochem.

View full text Add to dashboard Cite

show abstract

“…Besides, the upregulation of matrix metalloproteinase (MMP) -1 and -13 genes expression level in fi broblast-like cell was demonstrated by Choi et al (28). The relationship between adiponectin and other MMPs (MMP-2 and MMP-3) was also showed by other researchers (29,30). However, there is no investigation apart from our data to demonstrate the putative effect of adiponectin on ADAMTSs gene expression level in literature.…”

Section: Discussionsupporting

confidence: 50%

Dose-dependent effects of adiponectin on ADAMTS-9 gene expression in human chondrocytes

Yaykaşlı¹,

Hatipoğlu²,

Yaykaşlı³

et al. 2017

BLL

View full text Add to dashboard Cite

OBJECTIVE: A disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS), comprising of 19 members is a family of peptidases. They have several vital functions in physiological and pathological processes in organisms. ADAMTS-9 has aggrecanolytic activity and is responsible for degradation of aggrecan mainly in articular cartilage. It is known that adiponectin is the most abundantly secreted adipokine (adipocytokines), and the characteristics of adiponectin have not been elucidated yet. It was assumed that adiponectin has antiinfl ammatory effect before. However, an infl ammatory feature of adiponectin was shown in researches. In our study, the effect of adiponectin on ADAMTS-9 gene expression in primary human chondrocytes was investigated. METHODS: Primary human chondrocytes were exposed to adiponectin at 1, 4, 8 and 12 μg/ml doses for certain time period. Total RNA was isolated and reverse-transcribed by random primer after incubation. ADAMTS-9 and β-actin genes expression levels were determined using real-time polymerase chain reaction (qRT-PCR). RESULTS: The highest upregulation of ADAMTS-9 gene expression level was found at 12 μg/ml dose of adiponectin and 48 h incubation. CONCLUSION: Adiponectin is the key element in the maintenance of cartilage homeostasis. Similarly, the involvement of adiponectin in articular infl ammatory diseases was demonstrated in detail. These fi ndings bring adiponectin into central place in the research to develop adiponectin based new therapy methods for arthritic diseases. Together with these fi ndings, our results suggest that adiponectin may be involved in the degradation of articular cartilage by increasing ADAMTS-9 gene expression (Tab. 1, Fig. 3, Ref. 35). Text in PDF www.elis.sk.

show abstract

“…It can regulate the enzymatic activity of other MMPs such as MMP-1 and MMP-9, and promote collagen degradation, extracellular matrix destruction, and joint swelling, to reduce resistance to external force. With the help of the stress load, it can cause cartilage destruction (Choi et al, 2009;Tong et al, 2011). Our study showed that MMP-3 levels were significantly elevated in articular cartilage lesions.…”

Section: Discussionmentioning

confidence: 59%

“…It also causes the stagnation of the physiological metabolism of cartilage cells, causing cartilage degeneration and joint dysfunction. There are several theories about articular cartilage degeneration caused by abnormal stress (Honsawek and Chayanupatkul, 2010;Tong, 2011), which are outlined as follows:…”

Section: Discussionmentioning

confidence: 99%

Cartilage oligomeric matrix protein and matrix metalloproteinase-3 expression in the serum and joint fluid of a reversible osteoarthritis rabbit model

Xq¹,

Wang²,

Ld³

et al. 2015

Genet. Mol. Res.

View full text Add to dashboard Cite

ABSTRACT. The main pathological characteristic of osteoarthritis (OA) is cartilage damage. We explored cartilage oligomeric matrix protein (COMP) and matrix metalloproteinase-3 (MMP-3) changes during articular cartilage injury and repair. Rabbits were randomly divided into the following: a blank control group; groups M1, M2, and M3, in which breaking was performed for 2, 4, and 6 weeks, respectively; and groups L1, L2, and L3, in which breaking was discontinued for 2, 4, and 6 weeks, respectively, following a 4-week recovery period. There are 7 rabbits in each group. The degree of cartilage damage in each group was scored (OA score). An enzyme-linked immunosorbent assay was used to detect COMP and MMP-3 levels in serum and joint fluid. The OA scores were 3.89 ± 2.31, 7.21 ± 2.31, and 10.88 ± 2.08 points in groups M1, M2, and M3, respectively (P < 0.05). COMP and MMP-3 levels were significantly 14208 X.Q. Chu et al.©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 14 (4): 14207-14215 (2015) higher in groups M1, M2, and M3 than in C. The OA score improved significantly following the 4-week recovery period (P < 0.05). COMP and MMP-3 levels began to decrease as the time following discontinuation of breaking increased, but were higher than in the control (P < 0.05). MMP-3 and COMP levels were correlated with OA score (r > 0.7, P < 0.05). COMP and MMP-3 levels were correlated between joint fluid and serum (r = 0.899, r = 0.874, P < 0.05, respectively). Long-term joint breaking can cause articular cartilage damage. Doing some activites after the process can promote self-repair of articular cartilage. COMP and MMP-3 levels were associated with articular cartilage destruction and repair.

show abstract

Adiponectin increases MMP‐3 expression in human chondrocytes through adipor1 signaling pathway

Cited by 90 publications

References 33 publications

Ghrelin induces cell migration through GHS-R, CaMKII, AMPK, and NF-κB signaling pathway in glioma cells

Ghrelin induces cell migration through GHS-R, CaMKII, AMPK, and NF-κB signaling pathway in glioma cells

Dose-dependent effects of adiponectin on ADAMTS-9 gene expression in human chondrocytes

Cartilage oligomeric matrix protein and matrix metalloproteinase-3 expression in the serum and joint fluid of a reversible osteoarthritis rabbit model

Contact Info

Product

Resources

About