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Biology subjects

Chin, H. S.

Publications and source records attributed to Chin, H. S..

4 recordsLinked to original sources

IFNγ-CXCL9-CXCR3 axis links T cell recruitment to skeletal muscle remodelling in human physical frailty

Introduction: Physical frailty is increasingly prevalent in our ageing society, and results in higher morbidity and healthcare costs. Yet, targeted therapeutics are lacking because underlying mechanisms are poorly defined. Human cohort studies have linked inflammation with frailty, but do not define the mechanisms by which the ageing immune system affects skeletal muscle and physical function. Defining this immune-muscle interaction is therefore crucial for identifying therapeutics for human physical frailty. Methods: We first studied two independent human ageing cohorts (discovery n=22; validation n=33). Physical frailty was quantified with age-adjusted timed-up-and-go (TUG) residuals. Peripheral blood was analysed for plasma OLINK proteomics, high-dimensional spectral immunophenotyping and in a subset, single-cell RNA-sequencing of PBMCs with paired TCR profiling. We then examined an independent human skeletal-muscle cohort (n=340) by bulk RNA-sequencing to derive our proposed immune-muscle axis. Finally, we interrogated individual steps of this axis in primary human in vitro models using IFN{gamma}-conditioned myotube-fibroblast co-cultures, PBMC transwell migration assays with CXCL9 neutralisation (anti-CXCL9) and receptor CXCR3 antagonism (AMG487). Macrophage co-cultured with CD8 were sequentially co-cultured with myotube/fibroblast co-culture, supernatant was then analysed for fibrosis mediators. We used fixed-effect meta-analysis, multivariable models and sequential mediation for analyses. Results: Physical frailty, by single-cell analyses, was associated with a compartmentalised immune-remodelling state involving inflammatory, tissue-remodelling and trafficking programmes in myeloid and T-cells. This finding was validated with plasma proteomics of the same human cohort, where physical frailty was significantly positively associated with an interferon-gamma (IFN{gamma})/CXCR3 (IL-18R1, IFN{gamma}, CXCL9) module, within which plasma CXCL9 was the strongest correlate. CD8-TEMRA and {gamma}{delta} T-cells were most responsive to CXCL9 in physical frailty. This expanded CD8-TEMRA compartment was polyclonal, consistent with bystander IFN{gamma} production rather than a shared antigen-specific response. In human muscle, CXCL9 was significantly positively associated with T-cell module, and through this, fibrosis. Conversely, fibrosis was associated with macrophages. Sequential mediation was consistent with a CXCL9-T-cell-macrophage-fibrosis pathway. Finally, in in-vitro human primary cell experiments, IFN{gamma}-conditioned myotube-fibroblast cultures produced CXCL9 and attracted CD8-TEMRA subsets. Anti-CXCL9 and CXCR3 antagonism significantly reduced this migration, indicating that recruitment of CD8-TEMRA cells was dependent on the CXCL9-CXCR3 axis. Incubating with activated CD8 cells shifted macrophages towards mixed CD163+CD86+ and pro-inflammatory CD163-CD86+ phenotypes. These CD8-co-cultured macrophages in myotube/fibroblast co-culture were associated with increased fibrosis markers transforming growth factor beta-1 and plasminogen activator inhibitor-1. Conclusion: We identified a CD8-TEMRA T-cell migration to human muscle dependent on IFN{gamma}-CXCL9-CXCR3 axis that is associated with human TUG-defined physical frailty which presents potential therapeutic avenues.

immunology↗

FOXO-regulated Deaf1 controls muscle regeneration through autophagy

The commonality between various muscle diseases is the loss of muscle mass, function, and regeneration, which severely restricts mobility and impairs the quality of life. With muscle stem cells (MuSCs) playing a key role in facilitating muscle repair, targeting regulators of muscle regeneration has been shown to be a promising therapeutic approach to repair muscles. However, the underlying molecular mechanisms driving muscle regeneration are complex and poorly understood. Here, we identified a new regulator of muscle regeneration, Deformed epidermal autoregulatory factor 1 (Deaf1) - a transcriptional factor downstream of FOXO signaling. We showed that Deaf1 is transcriptionally repressed by FOXOs and that Deaf1 targets to PI3KC3 and Atg16l1 promoter regions and suppresses their expressions. Deaf1 depletion therefore induces autophagy, which in turn blocks MuSC survival and differentiation. In contrast, Deaf1 overexpression inactivates autophagy in MuSCs, leading to increased protein aggregation and cell death. Interestingly, Deaf1 depletion and overexpression both lead to defects in muscle regeneration, highlighting the importance of fine tuning Deaf1-regulated autophagy during muscle regeneration. We further showed that Deaf1 expression is altered in aging and cachectic MuSCs. Remarkably, manipulation of Deaf1 expression can attenuate muscle atrophy and restore muscle regeneration in aged mice or mice with cachectic cancers. Together, our findings unveil an evolutionarily conserved role for Deaf1 in muscle regeneration, providing insights into the development of new therapeutic strategies against muscle atrophy.

cell biology↗

E3 ubiquitin ligase MARCHF5 controls BAK apoptotic activity independently of BH3-only proteins

Intrinsic apoptosis is principally governed by the BCL-2 family of proteins, but some non-BCL-2 proteins are also critical to control this process. To identify novel apoptosis regulators, we performed a genome-wide CRISPR-Cas9 library screen, and it identified the mitochondrial E3 ubiquitin ligase MARCHF5/MITOL/RNF153 as an important regulator of BAK apoptotic function. Deleting MARCHF5 in diverse cell lines dependent on BAK conferred profound resistance to BH3-mimetic drugs. The loss of MARCHF5 or its E3 ubiquitin ligase activity surprisingly drove BAK to adopt an activated conformation, with resistance to BH3-mimetics afforded by the formation of inhibitory complexes with pro-survival proteins MCL-1 and BCL-XL. Importantly, these changes to BAK conformation and pro-survival association occurred independently of BH3-only proteins and influence on pro-survival proteins. This study identifies a new mechanism by which MARCHF5 regulates apoptotic cell death and provides new insight into how cancer cells respond to BH3-mimetic drugs. These data also highlight the emerging role of ubiquitin signalling in apoptosis that may be exploited therapeutically.

cell biology↗

BAX requires VDAC2 to mediate apoptosis and to limit tumor development

Intrinsic apoptosis is critical for normal physiology including the prevention of tumor formation. BAX and BAK are essential for mediating this process and for the cytotoxic action of many anticancer drugs. BAX and BAK are thought to act in a functionally redundant manner and are considered to be regulated similarly. From an unbiased genome-wide CRISPR/Cas9 screen, we identified VDAC2 (voltage-dependent anion channel 2) as essential for BAX, but not BAK, to function. The genetic deletion of VDAC2 abrogated the association of BAX and BAK with mitochondrial complexes that contain VDAC1, VDAC2 and VDAC3. By disrupting its localization to mitochondria, BAX is rendered completely ineffective. Moreover, we defined an interface unique to VDAC2 that is required to drive BAX activity. Consequently, interfering with this interaction or deleting VDAC2 phenocopied the loss of BAX, including impairing the killing of tumor cells by anti-cancer agents such as the BCL-2 inhibitor venetoclax. Furthermore, the ability of BAX to prevent tumor formation was attenuated in the absence of VDAC2. Taken together, our studies show for the first time that BAX-mediated apoptosis, but not BAK-mediated apoptosis, is critically dependent on VDAC2, hence revealing the differential regulation of BAX and BAK.

cell biology↗