Self-renewal and Differentiation of Muscle Satellite Cells Are Regulated by the Fas-associated Death Domain

Cheng, Wei; Wang, Lu; Yang, Bo; Zhang, Rong; Yao, Chun; He, Liangqiang; Liu, Zexu; Du, Pan; Hammache, Kahina; Wen, Juan; Huang, Li; Xu, Qiang; Zhang, Hua

doi:10.1074/jbc.m113.533448

Cited by 7 publications

(9 citation statements)

References 55 publications

(58 reference statements)

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“…Knockdown of FADD impairs pancreatic cancer cell proliferation, suggesting that FADD is required for cell proliferation in the context of cancer. It has been shown that FADD translocates into the nucleus during mitosis to promote cell cycle progression, implying that FADD has apoptotic and non-apoptotic roles depending upon its cellular localization (26,27). Its nuclear localization promotes cell cycle progression and simultaneously deprives proliferative cells of apoptotic stimuli (18).…”

Section: Discussionmentioning

confidence: 99%

The role of FADD in pancreatic cancer cell proliferation and drug resistance

et al. 2017

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Abstract. Pancreatic cancer has one of the poorest patient outcomes and is highly resistant to chemotherapy. Identifying the molecular mechanisms involved in drug resistance is critical in the development of novel strategies to treat pancreatic cancer. The results of the present study demonstrate that Fas-associated death domain protein (FADD), a classical adaptor protein mediating apoptotic stimuli-induced cell death, protects pancreatic cancer cells from drug-induced apoptosis. In contrast to its classical apoptotic roles, it was observed that FADD is required for pancreatic cancer cell proliferation and that it is overexpressed to varying degrees in various types of pancreatic cancer cell. This leads to differing levels of drug resistance in pancreatic cancer cells, where drug resistance is positively correlated with FADD expression. Notably, the results of the present study demonstrate that FADD protects pancreatic cancer cells from drug-induced apoptosis, while RNA interference of FADD sensitizes drug-resistant cells to Adriamycin ® -mediated apoptosis. The results of the present study reveal unexpected roles for FADD in pancreatic cancer cell proliferation and drug resistance.

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Section: Discussionmentioning

confidence: 99%

The role of FADD in pancreatic cancer cell proliferation and drug resistance

et al. 2017

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“…We have shown that Fasassociated death domain (FADD) phosphorylation regulates conventional PKC (cPKC) signaling termination and cell migration [Cheng et al, 2012]. Moreover, we have also established the role of FADD phosphorylation in muscle stem cell self-renewal and commitment, which occurs mainly through cPKC-mediated Notch signaling [Cheng et al, 2014]. How cPKC mediates FADD-induced Notch signaling remains unknown.…”

Section: Introductionmentioning

confidence: 99%

“…Our previous studies indicated that skeletal muscles containing FADD-D exhibited a reduced myofiber size [Cheng et al, 2014]. Here, we wanted to establish whether FADD-D affected the regeneration capacity of muscles by monitoring freeze-injured TA muscle regeneration.…”

Section: Fadd-d Impairs Muscle Regenerationmentioning

confidence: 99%

“…We have shown that FADD phosphorylation promotes PKCα activation, the inhibition of which represses the increased Notch-1 protein levels in FADD-D myogenic satellite cells [Cheng et al, 2014]. We then investigated whether PKCα also modulated Notch-1 expression in myoblasts.…”

Section: Pkc Promotes Notch Signaling In Fadd-d Myoblastsmentioning

confidence: 99%

“…Primary myoblasts were isolated as described previously with minor modifications [Cheng et al, 2014]. Briefly, the mice were sacrificed by cervical dislocation.…”

Section: Myoblast Isolation and Culturementioning

confidence: 99%

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Fas-Associated Protein with Death Domain Regulates Notch Signaling during Muscle Regeneration

Zhang

Wang

et al. 2014

Cells Tissues Organs

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Notch signaling plays critical roles during myogenesis by promoting the proliferation and inhibiting the differentiation of myogenic progenitors. However, the mechanism of the temporal regulation of Notch signaling during the myogenic lineage progression remains elusive. In the present study, we show that a constitutively phosphoryl-mimicking mutation of Fas-associated death domain (FADD-D) enhances Notch-1 signaling and compromises Wnt signaling in both cultured myoblasts and regenerating muscles, which results in inhibited myogenic differentiation and muscle regeneration. Inhibition of Notch signaling recovers the regeneration ability in injured FADD-D muscles through rescuing Wnt signaling. Furthermore, we found that protein kinase Cα mediates FADD-D-induced Notch-1 signaling by stabilizing Notch-1. Collectively, these data identify a novel mechanism for the temporal regulation of Notch signaling during myogenic lineage progression and muscle regeneration.

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Effects of 7,8-Dihydroxyflavone on Lipid Isoprenoid and Rho Protein Levels in Brains of Aged C57BL/6 Mice

et al. 2020

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Synaptic impairment may be the main cause of cognitive dysfunction in brain aging that is probably due to a reduction in synaptic contact between the axonal buttons and dendritic spines. Rho proteins including the small GTPase Rac1 have become key regulators of neuronal morphogenesis that supports synaptic plasticity. Small Rho- and Ras-GTPases are post-translationally modified by the isoprenoids geranylgeranyl pyrophosphate (GGPP) and farnesyl pyrophosphate (FPP), respectively. For all GTPases, anchoring in the plasma membrane is essential for their activation by guanine nucleotide exchange factors (GEFs). Rac1-specific GEFs include the protein T lymphoma invasion and metastasis 1 (Tiam1). Tiam1 interacts with the TrkB receptor to mediate the brain-derived neurotrophic factor (BDNF)-induced activation of Rac1, resulting in cytoskeletal rearrangement and changes in cellular morphology. The flavonoid 7,8-dihydroxyflavone (7,8-DHF) acts as a highly affine-selective TrkB receptor agonist and causes the dimerization and autophosphorylation of the TrkB receptor and thus the activation of downstream signaling pathways. In the current study, we investigated the effects of 7,8-DHF on cerebral lipid isoprenoid and Rho protein levels in male C57BL/6 mice aged 3 and 23 months. Aged mice were daily treated with 100 mg/kg b.w. 7,8-DHF by oral gavage for 21 days. FPP, GGPP, and cholesterol levels were determined in brain tissue. In the same tissue, the protein content of Tiam1 and TrkB in was measured. The cellular localization of the small Rho-GTPase Rac1 and small Rab-GTPase Rab3A was studied in total brain homogenates and membrane preparations. We report the novel finding that 7,8-DHF restored levels of the Rho proteins Rac1 and Rab3A in membrane preparations isolated from brains of treated aged mice. The selective TrkB agonist 7,8-DHF did not affect BDNF and TrkB levels, but restored Tiam1 levels that were found to be reduced in brains of aged mice. FPP, GGPP, and cholesterol levels were significantly elevated in brains of aged mice but not changed by 7,8-DHF treatment. Hence, 7,8-DHF may be useful as pharmacological tool to treat age-related cognitive dysfunction although the underlying mechanisms need to be elucidated in detail.

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Self-renewal and Differentiation of Muscle Satellite Cells Are Regulated by the Fas-associated Death Domain

Cited by 7 publications

References 55 publications

The role of FADD in pancreatic cancer cell proliferation and drug resistance

The role of FADD in pancreatic cancer cell proliferation and drug resistance

Fas-Associated Protein with Death Domain Regulates Notch Signaling during Muscle Regeneration

Effects of 7,8-Dihydroxyflavone on Lipid Isoprenoid and Rho Protein Levels in Brains of Aged C57BL/6 Mice

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