bioRxiv Science⌕ Search

Biology subjects

Mimche, P. N.

Publications and source records attributed to Mimche, P. N..

3 recordsLinked to original sources

Developmental IL7/IL7R signaling in fetal resident tissue macrophages regulates adaptive responses to liver injury

Resident tissue macrophages (RTMs) originate from multiple fetal hematopoietic waves and seed organs during the prenatal window where they acquire tissue-specific homeostatic functions. Several growth factors within the fetal niche are required for RTM development, but knowledge of how these signals program tissue-specific RTM survival, identity, and function during the prenatal window is limited. Here, we investigated the functional role of developmental IL7/IL7R signaling on fetal RTM survival and function. IL7 deficiency impaired neonatal RTM establishment, similar to IL7R deficiency, and IL7 was broadly expressed in fetal tissues and co-localized with IL7R+ macrophages. IL7/IL7R signaling regulated cell cycle, apoptotic, and inflammatory transcriptional pathways and activated phospho-AKT signaling in fetal liver myeloid cells. IL7R deletion impaired proliferation of fetal liver monocyte precursors and increased fetal liver macrophage apoptosis. Specific Cre-mediated IL7R deletion in fetal definitive HSC-derived, but not EMP- derived, macrophages caused irrecoverable postnatal loss of IL7R-expressing macrophages in specific tissues, including the liver, demonstrating a specific temporal requirement for IL7R expression during fetal myelopoiesis. Prenatal IL7R blockade subsequently impaired adaptive responses to chronic fibrotic liver injury in adulthood, associated with increased monocyte infiltration and upregulation of pro-inflammatory signaling pathways. These findings redefine IL7 as a developmental myeloid niche factor and demonstrate that IL7/IL7R signaling is co-opted during fetal development to imprint durable RTM programs that shape postnatal tissue immunity and adaptive responses to injury.

immunology↗

Excessive Ca2+-dependent ER-mitochondrial contact stabilization by EFHD1 drives liver injury

Metabolic-associated steatohepatitis (MASH) involves hepatocyte damage that cannot be explained solely by lipid accumulation. Here, to discover injury-specific pathways, we focused on a gene of uncertain function, EF-Hand Domain Family Member D1 (EFHD1), identified in human genome-wide association studies of liver injury but not liver fat. We show that EFHD1, a Ca2+-dependent actin crosslinker, stabilizes endoplasmic reticulum-mitochondria contact sites (ERMCS), detecting spatiotemporal coincidence of inter-organellar proximity and ER Ca2+ release. During MASH, EFHD1 upregulation drives pathological mitochondrial fragmentation via excessive contact persistence. This structural failure promotes mitochondrial double-stranded RNA escape and activation of a maladaptive antiviral PKR-dependent stress response, a causal relationship also supported by Mendelian randomization in humans. Consequently, inhibiting EFHD1 in human and mouse models blunts hepatocyte damage. These findings identify EFHD1 as a Ca2+-dependent ERMCS stabilizer, reveal a hepatocyte-intrinsic injury pathway, and suggest EFHD1 inhibition as a therapeutic strategy.

cell biology↗

Cardiolipin deficiency disrupts CoQ redox state and induces steatohepatitis

Metabolic dysfunction-associated steatotic liver disease (MASLD) is a progressive disorder marked by lipid accumulation, leading to metabolic dysfunction-associated steatohepatitis (MASH). A key feature of the transition to MASH involves oxidative stress resulting from defects in mitochondrial oxidative phosphorylation (OXPHOS). Here, we show that pathological alterations in the lipid composition of the inner mitochondrial membrane (IMM) directly instigate electron transfer inefficiency to promote oxidative stress. Specifically, mitochondrial cardiolipin (CL) was downregulated with MASLD/MASH in humans and in mice. Hepatocyte-specific CL synthase knockout (CLS-LKO) led to spontaneous and robust MASH with extensive steatotic and fibrotic phenotype. Loss of CL paradoxically increased mitochondrial respiratory capacity but also promoted electron leak primarily at sites IIIQO and IIF of the electron transport chain, reduced the formation of I+III2+IV respiratory supercomplex, and disrupted the propensity of coenzyme Q (CoQ) to become reduced. Thus, low mitochondrial CL disrupts electron transport chain to promote oxidative stress and contributes to pathogenesis of MASH.

biochemistry↗