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p38β MAPK mediates ULK1-dependent induction of autophagy in skeletal muscle of tumor-bearing mice

Liu, Zhelong, Sin, Ka Wai Thomas, Ding, Hui, Doan, HoangAnh Amy, Gao, Song, Miao, Hongyu, Wei, Yahui, Wang, Yiman, Zhang, Guohua, Li, Yi-Ping·2018·Cell Stress
DOI 10.15698/cst2018.11.163PMC PMC6551802
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Figure 1 FIGURE 1: p38β MAPK activation is necessary and sufficient for autophagy activation by tumor in skeletal muscle cells. (A) Inhibition of p38 MAPK attenuates LLC-conditioned medium (LCM)-induced autophagy activation in C2C12 myotubes. C2C12 myotubes were pretreated with SB202190 (SB, 10 (M) or vehicle (0.1% DMSO) for 30 min prior to treatment with LCM or control medium (NL20) for 8 h. Autophagy activation was evaluated by Western blotting analysis of LC3 in cell lysate. (B) Inhibition of p38 MAPK attenuates autophagy activation in skeletal muscle of LLC tumor-bearing mice. In 7 days of LLC implant to mice, SB202190 was i.p. injected (5 mg/kg) daily with DMSO (50%) as vehicle control for 14 days. Lysate of TA collected on 21 days of LLC implant was analyzed by Western blotting for LC3 (samples from 3 mice per group were loaded on each gel). (C) LCM-induced autophagy activation in myotubes is dependent on p38β MAPK. C2C12 myoblasts were transfected with control, p38α MAPK or p38β MAPK-specific siRNA. After differentiation, myotubes were treated with LCM or control medium for 8 h. Autophagy activation was evaluated by Western blotting analysis of LC3. (D) Expression of constitutively active p38β MAPK stimulates autophagy flux in C2C12 myotubes. Plasmids encoding a constitutively active mutant of p38α MAPK or p38β MAPK with the HA tag were transfected into C2C12 myoblasts, with empty vector as control. After differentiation, myotubes were treated with chloroquine (CQ, 20 (M) for 8 h. LC3, p62 and expression of the p38 MAPK mutants were monitored by Western blotting. (E) Constitutively active p38β MAPK activates autophagy in mouse muscle. Plasmids encoding the constitutively active mutant of p38α MAPK or p38β MAPK fused with the HA tag were transfected into the TA of mice. Empty vector was transfected into the contralateral TA. On day 14 expression of the p38 MAPK mutants and autophagy activation was analyzed by Western blotting (data from two mice per group are shown). Data were analyzed by one way ANOVA. * denotes a difference between bracketed groups or from controls (p < 0.05). (F) Constitutively active p38β MAPK stimulates autophagosome formation in mouse muscle. A plasmid encoding GFP-LC3 was transfected into mouse TA muscle, and co-transfected with the plasmid encoding the constitutively active mutant of p38α MAPK or p38β MAPK in the contralateral TA. In 7 days, TA muscle was collected. Frozen sections were prepared and stained with DAPI. Autophagosome formation was evaluated by confocal microscopy. Bars represent 50 μm.
Figure 1 FIGURE 1: p38β MAPK activation is necessary and sufficient for autophagy activation by tumor in skeletal muscle cells. (A) Inhibition of p38 MAPK attenuates LLC-conditioned medium (LCM)-induced autophagy activation in C2C12 myotubes. C2C12 myotubes were pretreated with SB202190 (SB, 10 (M) or vehicle (0.1% DMSO) for 30 min prior to treatment with LCM or control medium (NL20) for 8 h. Autophagy activation was evaluated by Western blotting analysis of LC3 in cell lysate. (B) Inhibition of p38 MAPK attenuates autophagy activation in skeletal muscle of LLC tumor-bearing mice. In 7 days of LLC implant to mice, SB202190 was i.p. injected (5 mg/kg) daily with DMSO (50%) as vehicle control for 14 days. Lysate of TA collected on 21 days of LLC implant was analyzed by Western blotting for LC3 (samples from 3 mice per group were loaded on each gel). (C) LCM-induced autophagy activation in myotubes is dependent on p38β MAPK. C2C12 myoblasts were transfected with control, p38α MAPK or p38β MAPK-specific siRNA. After differentiation, myotubes were treated with LCM or control medium for 8 h. Autophagy activation was evaluated by Western blotting analysis of LC3. (D) Expression of constitutively active p38β MAPK stimulates autophagy flux in C2C12 myotubes. Plasmids encoding a constitutively active mutant of p38α MAPK or p38β MAPK with the HA tag were transfected into C2C12 myoblasts, with empty vector as control. After differentiation, myotubes were treated with chloroquine (CQ, 20 (M) for 8 h. LC3, p62 and expression of the p38 MAPK mutants were monitored by Western blotting. (E) Constitutively active p38β MAPK activates autophagy in mouse muscle. Plasmids encoding the constitutively active mutant of p38α MAPK or p38β MAPK fused with the HA tag were transfected into the TA of mice. Empty vector was transfected into the contralateral TA. On day 14 expression of the p38 MAPK mutants and autophagy activation was analyzed by Western blotting (data from two mice per group are shown). Data were analyzed by one way ANOVA. * denotes a difference between bracketed groups or from controls (p < 0.05). (F) Constitutively active p38β MAPK stimulates autophagosome formation in mouse muscle. A plasmid encoding GFP-LC3 was transfected into mouse TA muscle, and co-transfected with the plasmid encoding the constitutively active mutant of p38α MAPK or p38β MAPK in the contralateral TA. In 7 days, TA muscle was collected. Frozen sections were prepared and stained with DAPI. Autophagosome formation was evaluated by confocal microscopy. Bars represent 50 μm.CC BY · PubMed Central
Figure 2 FIGURE 2: Muscle-specific knockout of p38β MAPK abrogates activation of autophagy, UPP and muscle wasting in tumor-bearing mice. Mice with muscle-specific knockout of p38β MAPK and control mice (p38β MAPKf/f) were implanted with LLC cells. In 21 days, mice were euthanized for analysis of muscle wasting. Lysate of TA collected from the mice was analyzed by Western blotting for LC3 and p62 to evaluate autophagy activity (A) and UBR2, atrogin1 and MHC to evaluate UPP activity (B). Muscle wasting in the mice was analyzed by examining tumor weight, body and muscle weight, tyrosine release and grip strength (C). Muscle mass was measured as muscle fiber cross sectional area (D). Data in A to C were analyzed by one way ANOVA. Data in D were analyzed by Chi-square analysis. * denotes a difference (p < 0.05).
Figure 2 FIGURE 2: Muscle-specific knockout of p38β MAPK abrogates activation of autophagy, UPP and muscle wasting in tumor-bearing mice. Mice with muscle-specific knockout of p38β MAPK and control mice (p38β MAPKf/f) were implanted with LLC cells. In 21 days, mice were euthanized for analysis of muscle wasting. Lysate of TA collected from the mice was analyzed by Western blotting for LC3 and p62 to evaluate autophagy activity (A) and UBR2, atrogin1 and MHC to evaluate UPP activity (B). Muscle wasting in the mice was analyzed by examining tumor weight, body and muscle weight, tyrosine release and grip strength (C). Muscle mass was measured as muscle fiber cross sectional area (D). Data in A to C were analyzed by one way ANOVA. Data in D were analyzed by Chi-square analysis. * denotes a difference (p < 0.05).CC BY · PubMed Central
Figure 3 FIGURE 3: The p38β MAPK → C/EBPβ signaling pathway mediates autophagy activation by tumor in skeletal muscle cells. (A) C/EBPβ activation in skeletal muscle of LLC tumor-bearing mice is dependent on p38β MAPK. Lysate of TA collected from p38β MAPKf/f and p38β MAPK muscle-specific knockout mice on day 21 of LLC implant was analyzed by Western blotting for C/EBPβ activation (phosphorylation of Thr-188). (B) C/EBPβ is critical to LCM-induced autophagy activation in myotubes. C2C12 myoblasts transfected with control or C/EBPβ-specific siRNA were treated with LCM or control medium for 8 h. C/EBPβ and LC3 were analyzed by Western blotting. (C) Autophagy activation in skeletal muscle of LLC tumor-bearing mice is dependent on C/EBPβ. Lysate of TA collected from wild type and C/EBPβ knockout mice on day 21 of LLC implant was analyzed by Western blotting for LC3.
Figure 3 FIGURE 3: The p38β MAPK → C/EBPβ signaling pathway mediates autophagy activation by tumor in skeletal muscle cells. (A) C/EBPβ activation in skeletal muscle of LLC tumor-bearing mice is dependent on p38β MAPK. Lysate of TA collected from p38β MAPKf/f and p38β MAPK muscle-specific knockout mice on day 21 of LLC implant was analyzed by Western blotting for C/EBPβ activation (phosphorylation of Thr-188). (B) C/EBPβ is critical to LCM-induced autophagy activation in myotubes. C2C12 myoblasts transfected with control or C/EBPβ-specific siRNA were treated with LCM or control medium for 8 h. C/EBPβ and LC3 were analyzed by Western blotting. (C) Autophagy activation in skeletal muscle of LLC tumor-bearing mice is dependent on C/EBPβ. Lysate of TA collected from wild type and C/EBPβ knockout mice on day 21 of LLC implant was analyzed by Western blotting for LC3.CC BY · PubMed Central
Figure 4 FIGURE 4. C/EBPβ mediates tumor induction of autophagy-related genes in skeletal muscle cells. (A) Potential C/EBPβ-binding cites are identified in autophagy-related genes. Data base search identified multiple potential biding sites of C/EBPβ in the 5’ promoter region of listed autophagy-related genes. (B) LC3b and Gabarapl1 are upregulated in skeletal muscle of LLC tumor-bearing mice in a C/EBPβ-dependent manner. Total RNA was extracted from the TA of wild type and C/EBPβ knockout mice implanted with LLC cells for 21 days, and analyzed for the mRNA of above identified autophagy-related genes by real-time PCR. (C) LC3b and Gabarapl1 are upregulated in LCM-treated myotubes in a C/EBPβ-dependent manner. Total RNA was extracted from C2C12 myotubes transfected with C/EBPβ-specific or control siRNA. The mRNA of C/EBPβ, LC3b and Gabarapl1 was determined by real-time PCR. Data from panel B and C were analyzed by one way ANOVA. * denotes a difference (p < 0.05). (D) LCM activates C/EBPβ binding to the LC3b and Gabarapl1 promoters in myotubes. C/EBPβ binding to the LC3b and Gabarapl1 promoters in C2C12 myotubes treated with LCM or the control NL20 cell-conditioned medium (NCM) was analyzed by the ChIP assay. Pre-immune IgG was used as control for C/EBPβ-specific antibody.
Figure 4 FIGURE 4. C/EBPβ mediates tumor induction of autophagy-related genes in skeletal muscle cells. (A) Potential C/EBPβ-binding cites are identified in autophagy-related genes. Data base search identified multiple potential biding sites of C/EBPβ in the 5’ promoter region of listed autophagy-related genes. (B) LC3b and Gabarapl1 are upregulated in skeletal muscle of LLC tumor-bearing mice in a C/EBPβ-dependent manner. Total RNA was extracted from the TA of wild type and C/EBPβ knockout mice implanted with LLC cells for 21 days, and analyzed for the mRNA of above identified autophagy-related genes by real-time PCR. (C) LC3b and Gabarapl1 are upregulated in LCM-treated myotubes in a C/EBPβ-dependent manner. Total RNA was extracted from C2C12 myotubes transfected with C/EBPβ-specific or control siRNA. The mRNA of C/EBPβ, LC3b and Gabarapl1 was determined by real-time PCR. Data from panel B and C were analyzed by one way ANOVA. * denotes a difference (p < 0.05). (D) LCM activates C/EBPβ binding to the LC3b and Gabarapl1 promoters in myotubes. C/EBPβ binding to the LC3b and Gabarapl1 promoters in C2C12 myotubes treated with LCM or the control NL20 cell-conditioned medium (NCM) was analyzed by the ChIP assay. Pre-immune IgG was used as control for C/EBPβ-specific antibody.CC BY · PubMed Central
Figure 5 FIGURE 5: p38β MAPK is required for upregulation of C/EBPβ-responsive autophagy-related genes in cachectic muscle of tumor-bearing mice. (A) Inhibition of p38 MAPK attenuates LC3b and Gabarapl1 upregulation in cachectic muscle of LLC tumor-bearing mice. On day 7 of LLC cells implant to mice, SB202190 was i.p. injected (5 mg/kg) daily with DMSO (50%) as vehicle control. Lysate of TA collected on day 21 was analyzed by qPCR for LC3b and Gabarapl1 mRNA levels. (B) LC3b and Gabarapl1 upregulation in the muscle of LLC tumor-bearing mice is dependent on p38β MAPK. Mice with muscle-specific knockout of p38β MAPK (p38β MAPK MKO) or control mice (p38β MAPKf/f) were implanted with LLC cells. On day 21, total RNA was extracted from TA of the mice and analyzed by qPCR for LC3b and Gabarapl1 mRNA levels. Data were analyzed by one way ANOVA. * denotes a difference (p < 0.05).
Figure 5 FIGURE 5: p38β MAPK is required for upregulation of C/EBPβ-responsive autophagy-related genes in cachectic muscle of tumor-bearing mice. (A) Inhibition of p38 MAPK attenuates LC3b and Gabarapl1 upregulation in cachectic muscle of LLC tumor-bearing mice. On day 7 of LLC cells implant to mice, SB202190 was i.p. injected (5 mg/kg) daily with DMSO (50%) as vehicle control. Lysate of TA collected on day 21 was analyzed by qPCR for LC3b and Gabarapl1 mRNA levels. (B) LC3b and Gabarapl1 upregulation in the muscle of LLC tumor-bearing mice is dependent on p38β MAPK. Mice with muscle-specific knockout of p38β MAPK (p38β MAPK MKO) or control mice (p38β MAPKf/f) were implanted with LLC cells. On day 21, total RNA was extracted from TA of the mice and analyzed by qPCR for LC3b and Gabarapl1 mRNA levels. Data were analyzed by one way ANOVA. * denotes a difference (p < 0.05).CC BY · PubMed Central
Figure 6 FIGURE 6: p38β MAPK activates ULK1 in skeletal muscle cells in response to tumor. (A) LCM stimulates ULK1 phosphorylation on Ser-555 in myotubes through p38 MAPK. C2C12 myotubes were pretreated with DMSO (0.1%, vehicle), compound C (CC, 10 (M) or SB202190 (SB, 10 (M) for 30 min, and then treated with LCM for 1 h. ULK1 phosphorylation state on Ser-555 and AMPK phosphorylation on Thr-172 in cell lysate were analyzed by Western blotting. (B) LCM stimulates p38 MAPK interaction with ULK1 in myotubes. C2C12 myotubes were treated with LCM for 1 h. Cell lysate was subjected to immunoprecipitation with pre-immune IgG or p38 MAPK-specific antibody. Precipitate was analyzed by Western blotting for p38 MAPK and pSer-555 ULK1. (C) LCM stimulation of ULK1 phosphorylation on Ser-555 in myotubes is mediated by p38β MAPK specifically. C2C12 myoblasts were transfected with control, p38β MAPK or p38β MAPK-specific siRNA. After differentiation for 96 h, myotubes were treated with LCM or control medium for 1 h. Knockdown of p38 MAPKs and phosphorylation of ULK1 on Ser-555 were analyzed by Western blotting. (D) p38β MAPK is required for ULK1 activation in cachectic muscle of LLC tumor-bearing mice. Mice with muscle-specific knockout of p38β MAPK and control mice were implanted with LLC cells. Lysate of TA collected from these mice on day 21 was analyzed by Western blotting for ULK1 phosphorylation on Ser-555 and AMPK phosphorylation on Thr-172. Data were analyzed by one way AVOVA. * denotes a difference (p < 0.05).
Figure 6 FIGURE 6: p38β MAPK activates ULK1 in skeletal muscle cells in response to tumor. (A) LCM stimulates ULK1 phosphorylation on Ser-555 in myotubes through p38 MAPK. C2C12 myotubes were pretreated with DMSO (0.1%, vehicle), compound C (CC, 10 (M) or SB202190 (SB, 10 (M) for 30 min, and then treated with LCM for 1 h. ULK1 phosphorylation state on Ser-555 and AMPK phosphorylation on Thr-172 in cell lysate were analyzed by Western blotting. (B) LCM stimulates p38 MAPK interaction with ULK1 in myotubes. C2C12 myotubes were treated with LCM for 1 h. Cell lysate was subjected to immunoprecipitation with pre-immune IgG or p38 MAPK-specific antibody. Precipitate was analyzed by Western blotting for p38 MAPK and pSer-555 ULK1. (C) LCM stimulation of ULK1 phosphorylation on Ser-555 in myotubes is mediated by p38β MAPK specifically. C2C12 myoblasts were transfected with control, p38β MAPK or p38β MAPK-specific siRNA. After differentiation for 96 h, myotubes were treated with LCM or control medium for 1 h. Knockdown of p38 MAPKs and phosphorylation of ULK1 on Ser-555 were analyzed by Western blotting. (D) p38β MAPK is required for ULK1 activation in cachectic muscle of LLC tumor-bearing mice. Mice with muscle-specific knockout of p38β MAPK and control mice were implanted with LLC cells. Lysate of TA collected from these mice on day 21 was analyzed by Western blotting for ULK1 phosphorylation on Ser-555 and AMPK phosphorylation on Thr-172. Data were analyzed by one way AVOVA. * denotes a difference (p < 0.05).CC BY · PubMed Central

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Metadata

Authors
Liu, Z., Sin, K. W. T., Ding, H., Doan, H. A., Gao, S., Miao, H., Wei, Y., Wang, Y., Zhang, G., & Li, Y.-P.
Venue
Cell Stress
Publisher
Shared Science Publishers OG
Published
2018-11-12
Volume
2
Issue
11
Pages
311-324
ISSN
2523-0204
DOI
10.15698/cst2018.11.163
PMC
PMC6551802
Cited by
46
References
7

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