Recombinant ADAMTS1 promotes muscle cell differentiation and alleviates muscle atrophy by repressing NOTCH1
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
A disintegrin and metalloproteinase with thrombospondin motifs1 (ADAMTS1) plays crucial roles in various biological processes,including myogenesis, by modulating the neurogeniclocus notch homolog protein 1 (NOTCH1) signaling pathway. However, the mechanisms through which ADAMTS1 regulatesmyogenesis remain unclear. In this study, we generated recombinantADAMTS1 mutants and determined their effects onmuscle cell differentiation, focusing on the regulation ofNOTCH1 signaling. Treatment of C2C12 cells with recombinantADAMTS1 protein enhanced muscle cell differentiation. Meanwhile,ADAM10 treatment inhibited muscle differentiationthrough the activation of NOTCH1 cleavage. RecombinantADAMTS1 reversed ADAM10-induced muscle cell atrophy bysuppressing NOTCH1 activation and downregulating its targetgene. Recombinant ADAMTS1 also alleviated dexamethasoneinducedmuscle atrophy in a mouse model. In summary, ourfindings suggest that recombinant ADAMTS1 promotes muscleregeneration by suppressing NOTCH1 and highlight the potentialof recombinant ADAMTS1 proteins in the treatment ofmuscle wasting disease.
Abstract
A disintegrin and metalloproteinase with thrombospondin motifs1 (ADAMTS1) plays crucial roles in various biological processes,including myogenesis, by modulating the neurogeniclocus notch homolog protein 1 (NOTCH1) signaling pathway. However, the mechanisms through which ADAMTS1 regulatesmyogenesis remain unclear. In this study, we generated recombinantADAMTS1 mutants and determined their effects onmuscle cell differentiation, focusing on the regulation ofNOTCH1 signaling. Treatment of C2C12 cells with recombinantADAMTS1 protein enhanced muscle cell differentiation. Meanwhile,ADAM10 treatment inhibited muscle differentiationthrough the activation of NOTCH1 cleavage. RecombinantADAMTS1 reversed ADAM10-induced muscle cell atrophy bysuppressing NOTCH1 activation and downregulating its targetgene. Recombinant ADAMTS1 also alleviated dexamethasoneinducedmuscle atrophy in a mouse model. In summary, ourfindings suggest that recombinant ADAMTS1 promotes muscleregeneration by suppressing NOTCH1 and highlight the potentialof recombinant ADAMTS1 proteins in the treatment ofmuscle wasting disease.
참고문헌 (26)
- Apte SS, "A disintegrin-like and metalloprotease(reprolysin-type)with thrombospondin type 1 motif(ADAMTS)superfamily : functions and mechanisms", J Biol Chem, 284, pp.31493~31497 (2009)
- Zhang X, "The potential prognostic values of the ADAMTS-like protein family : an integrative pan-cancer analysis", Ann Transl Med, 9, pp.1562~ (2021)
- Minns AF, "The C-terminal domains of ADAMTS1contain exosites involved in its proteoglycanase activity", J Biol Chem, 299, pp.103048~ (2023)
- Du H, "Macrophagereleased ADAMTS1 promotes muscle stem cell activation", Nat Commun, 8, pp.669~ (2017)
- Gioftsidi S, "The Notch signaling network in muscle stem cells during development, homeostasis, and disease", Skelet Muscle, 12, pp.9~ (2022)
- Steinbuck MP, "A review of Notch processing with new insights into ligand-independent Notch signaling in T-Cells", Front Immunol, 9, pp.1230~ (2018)
- Brown MS, "Regulated intramembrane proteolysis : a control mechanism conserved from bacteria to humans", Cell, 100, pp.391~398 (2000)
- Struhl G, "Requirements for presenilindependent cleavage of notch and other transmembrane proteins", Mol Cell, 6, pp.625~636 (2000)
- Vargas-Franco D, "The Notch signaling pathway in skeletal muscle health and disease", Muscle Nerve, 66, pp.530~544 (2022)
- Fujimaki S, "Notch1 and Notch2 coordinately regulate stem cell function in the quiescent and activated states of muscle satellite cells", Stem Cells, 36, pp.278~285 (2018)
- Kitamoto T, "Notch3 null mutation in mice causes muscle hyperplasia by repetitive muscle regeneration", Stem Cells, 28, pp.2205~2216 (2010)
- Zhang Y, "Oscillations of Delta-like1 regulate the balance between differentiation and maintenance of muscle stem cells", Nat Commun, 12, pp.1318~ (2021)
- Bjornson CRR, "Notch signaling is necessary to maintain quiescence in adult muscle stem cells", Stem Cells, 30, pp.232~242 (2012)
- Mourikis P, "A critical requirement for notch signaling in maintenance of the quiescent skeletal muscle stem cell state", Stem Cells, 30, pp.243~252 (2012)
- Wehling M, "A nitric oxide synthase transgene ameliorates muscular dystrophy in mdx mice", J Cell Biol, 155, pp.123~131 (2001)
- Arnold L, "Inflammatory monocytes recruited after skeletal muscle injury switch into antiinflammatory macrophages to support myogenesis", J Exp Med, 204, pp.1057~1069 (2007)
- Summan M, "Macrophages and skeletal muscle regeneration : a clodronatecontaining liposome depletion study", Am J Physiol Regul Integr Comp Physiol, 290, pp.R1488~1495 (2006)
- Nagase H, "Matrix metalloproteinases", J Biol Chem, 274, pp.21491~21494 (1999)
- Porter S, "The ADAMTS metalloproteinases", Biochem J, 386, pp.15~27 (2005)
- Mizuno S, "Inhibition of ADAM10 in satellite cells accelerates muscle regeneration following muscle injury", J Orthop Res, 36, pp.2259~2265 (2018)
- Wang BYH, "Is dexamethasone-induced muscle atrophy an alternative model for naturally aged sarcopenia model?", J Orthop Translat, 39, pp.12~20 (2022)
- Bodine SC, "Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx", atrogin-1, 2014, pp.307, E469~E484
- Yoon JH, "Alverine citrate promotes myogenic differentiation and ameliorates muscle atrophy", Biochem Biophys Res Commun, 586, pp.157~162 (2022)
- Huang L, "Potential therapeutic strategies for skeletal muscle atrophy", Antioxidants, 12, pp.44~ (2023)
- Pronsato L, "Testosterone modulates FoxO3a and p53-related genes to protect c2c12 skeletal muscle cells against apoptosis", Steroids, 124, pp.35~45 (2017)
- Lahmann I, "Oscillations of MyoD and Hes1 proteins regulate the maintenance of activated muscle stem cells", Genes Dev, 33, pp.524~535 (2019)