Irisin Recovers Osteoarthritic Chondrocytes In Vitro
Physical exercise favors weight loss and ameliorates articular pain and function in patients suffering from osteoarthritis. Irisin, a myokine released upon muscle contraction, has demonstrated to yield anabolic effects on different cell types. This study aimed to investigate the effect of irisin on...
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| Format: | Article |
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MDPI AG
2020-06-01
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| Series: | Cells |
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| Online Access: | https://www.mdpi.com/2073-4409/9/6/1478 |
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| author | Gianluca Vadalà Giuseppina Di Giacomo Luca Ambrosio Francesca Cannata Claudia Cicione Rocco Papalia Vincenzo Denaro |
| author_facet | Gianluca Vadalà Giuseppina Di Giacomo Luca Ambrosio Francesca Cannata Claudia Cicione Rocco Papalia Vincenzo Denaro |
| author_sort | Gianluca Vadalà |
| collection | DOAJ |
| description | Physical exercise favors weight loss and ameliorates articular pain and function in patients suffering from osteoarthritis. Irisin, a myokine released upon muscle contraction, has demonstrated to yield anabolic effects on different cell types. This study aimed to investigate the effect of irisin on human osteoarthritic chondrocytes (hOAC) in vitro. Our hypothesis was that irisin would improve hOAC metabolism and proliferation. Cells were cultured in growing media and then exposed to either phosphate-buffered saline (control group) or human recombinant irisin (experimental group). Cell proliferation, glycosaminoglycan content, type II/X collagen gene expression and protein quantification as well as p38/extracellular signal-regulated kinase (ERK) mitogen-activated protein kinase (MAPK), protein kinase B (Akt), c-Jun N-terminal kinase (JNK), and nuclear factor kappa-light-chain-enhancer of activated B cells (NFκB) involvement were evaluated. Furthermore, gene expression of interleukin (IL)-1 and -6, matrix metalloproteinase (MMP)-1 and -13, inducible nitric oxide synthase (iNOS), and tissue inhibitor of matrix metalloproteinases (TIMP)-1 and -3 were investigated following irisin exposure. Irisin increased hOAC cell content and both type II collagen gene expression and protein levels, while decreased type X collagen gene expression and protein levels. Moreover, irisin decreased IL-1, IL-6, MMP-1, MMP-13 and iNOS gene expression, while increased TIMP-1 and TIMP-3 levels. These effects seemed to be mediated by inhibition of p38, Akt, JNK and NFκB signaling pathways. The present study suggested that irisin may stimulate hOAC proliferation and anabolism inhibiting catabolism through p38, Akt, JNK, and NFκB inactivation in vitro, demonstrating the existence of a cross-talk between muscle and cartilage. |
| first_indexed | 2024-03-10T19:07:10Z |
| format | Article |
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| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-10T19:07:10Z |
| publishDate | 2020-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-799f54f9f0f748738b7ebd1d59b2e3292023-11-20T04:05:26ZengMDPI AGCells2073-44092020-06-0196147810.3390/cells9061478Irisin Recovers Osteoarthritic Chondrocytes In VitroGianluca Vadalà0Giuseppina Di Giacomo1Luca Ambrosio2Francesca Cannata3Claudia Cicione4Rocco Papalia5Vincenzo Denaro6Laboratory of Regenerative Orthopaedics, Department of Orthopaedic and Trauma Surgery, Campus Bio-Medico University of Rome, Via Alvaro del Portillo 200, 00128 Rome, ItalyLaboratory of Regenerative Orthopaedics, Department of Orthopaedic and Trauma Surgery, Campus Bio-Medico University of Rome, Via Alvaro del Portillo 200, 00128 Rome, ItalyLaboratory of Regenerative Orthopaedics, Department of Orthopaedic and Trauma Surgery, Campus Bio-Medico University of Rome, Via Alvaro del Portillo 200, 00128 Rome, ItalyDepartment of Endocrinology and Diabetes, Campus Bio-Medico University of Rome, Via Alvaro del Portillo 200, 00128 Rome, ItalyLaboratory of Regenerative Orthopaedics, Department of Orthopaedic and Trauma Surgery, Campus Bio-Medico University of Rome, Via Alvaro del Portillo 200, 00128 Rome, ItalyLaboratory of Regenerative Orthopaedics, Department of Orthopaedic and Trauma Surgery, Campus Bio-Medico University of Rome, Via Alvaro del Portillo 200, 00128 Rome, ItalyLaboratory of Regenerative Orthopaedics, Department of Orthopaedic and Trauma Surgery, Campus Bio-Medico University of Rome, Via Alvaro del Portillo 200, 00128 Rome, ItalyPhysical exercise favors weight loss and ameliorates articular pain and function in patients suffering from osteoarthritis. Irisin, a myokine released upon muscle contraction, has demonstrated to yield anabolic effects on different cell types. This study aimed to investigate the effect of irisin on human osteoarthritic chondrocytes (hOAC) in vitro. Our hypothesis was that irisin would improve hOAC metabolism and proliferation. Cells were cultured in growing media and then exposed to either phosphate-buffered saline (control group) or human recombinant irisin (experimental group). Cell proliferation, glycosaminoglycan content, type II/X collagen gene expression and protein quantification as well as p38/extracellular signal-regulated kinase (ERK) mitogen-activated protein kinase (MAPK), protein kinase B (Akt), c-Jun N-terminal kinase (JNK), and nuclear factor kappa-light-chain-enhancer of activated B cells (NFκB) involvement were evaluated. Furthermore, gene expression of interleukin (IL)-1 and -6, matrix metalloproteinase (MMP)-1 and -13, inducible nitric oxide synthase (iNOS), and tissue inhibitor of matrix metalloproteinases (TIMP)-1 and -3 were investigated following irisin exposure. Irisin increased hOAC cell content and both type II collagen gene expression and protein levels, while decreased type X collagen gene expression and protein levels. Moreover, irisin decreased IL-1, IL-6, MMP-1, MMP-13 and iNOS gene expression, while increased TIMP-1 and TIMP-3 levels. These effects seemed to be mediated by inhibition of p38, Akt, JNK and NFκB signaling pathways. The present study suggested that irisin may stimulate hOAC proliferation and anabolism inhibiting catabolism through p38, Akt, JNK, and NFκB inactivation in vitro, demonstrating the existence of a cross-talk between muscle and cartilage.https://www.mdpi.com/2073-4409/9/6/1478irisinosteoarthritiscartilagephysical exercisechondrocyte |
| spellingShingle | Gianluca Vadalà Giuseppina Di Giacomo Luca Ambrosio Francesca Cannata Claudia Cicione Rocco Papalia Vincenzo Denaro Irisin Recovers Osteoarthritic Chondrocytes In Vitro Cells irisin osteoarthritis cartilage physical exercise chondrocyte |
| title | Irisin Recovers Osteoarthritic Chondrocytes In Vitro |
| title_full | Irisin Recovers Osteoarthritic Chondrocytes In Vitro |
| title_fullStr | Irisin Recovers Osteoarthritic Chondrocytes In Vitro |
| title_full_unstemmed | Irisin Recovers Osteoarthritic Chondrocytes In Vitro |
| title_short | Irisin Recovers Osteoarthritic Chondrocytes In Vitro |
| title_sort | irisin recovers osteoarthritic chondrocytes in vitro |
| topic | irisin osteoarthritis cartilage physical exercise chondrocyte |
| url | https://www.mdpi.com/2073-4409/9/6/1478 |
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