ACSL1 (Acyl-CoA Synthetase Long Chain Family Member 1)

Clinically, higher CD36 expression correlated with the luminal androgen receptor (LAR) subtype of TNBC, known to exhibit a higher sensitivity to ferroptosis. Altogether, these data provide evidence for an essential role of the CD36 protein in the ferroptotic process induced by the saturated fatty acid PA, opening potential new therapeutic approaches promoting ferroptosis in the most aggressive breast cancers.

Combining ibrutinib with the GPX4 inhibitor RSL3 enhances ferroptosis and improves antileukemic efficacy in vivo. Notably, ACSL1 is selectively upregulated in U-CLL cells and represents a targetable metabolic enhancer of ferroptosis sensitivity, as shown in vivo. Our findings reveal that TFRC and ACSL1 are functionally distinct yet targetable nodes that govern ferroptosis vulnerability in CLL patients and may guide novel therapeutic strategies for high-risk patients.

CONCLUSIONS Our findings suggest multi-omic switch-like regulation may underlie differential COPD/IPF etiology. Future investigation of LPCAT1 and ATP11A could provide new mechanistic understanding and therapeutic avenues.

We demonstrate that the mitochondrial network changes in human oligodendrocyte development resemble those reported in mouse tissue. Our findings point to MCL-1 as a critical factor essential for proper oligodendrocyte morphogenesis.

In vitro mechanistic studies revealed that CPT1A may promote mitochondrial damage and induce cardiomyocyte injury by interacting with Parkin. This study underscores the utility of multi-omics integration in elucidating TIC mechanisms and paves the way for personalized cardioprotective strategies in HER2-targeted therapy.

We demonstrate that TAG in peri-mitochondrial LDs functions as a ROS scavenger, enabling CSCs to survive in hyperoxidative environments. Targeting the signaling pathways involved in TAG synthesis presents a potential strategy for eradicating CSCs.

The present review seeks to fill this gap by summarizing recent advances in understanding the roles of the ACSL family across diverse diseases, with a focus on emerging therapeutic strategies that target these enzymes. This work provides critical insights that may inform future preclinical and clinical investigations of the ACSL family.

AC is characterized by distinct metabolic reprogramming, with preferential upregulation of peroxisomal β-oxidation rather than mitochondrial pathways. These metabolic features are accompanied by a high prevalence of activating PIK3CA mutations, suggesting a link between genomic alterations and metabolic phenotype. These findings provide new insights into the pathobiology of AC and may assist in its histopathological differentiation from other breast cancer subtypes.

We describe the mechanisms of action, effects, regulation, association with cancer progression, and their potential as pharmacological targets of the steroid acute regulatory protein (StAR), translocator protein (TSPO), acetyl-CoA carboxylase β (ACCβ), acyl-CoA synthetases long chain family member 1 and 6 (ACSL1 and ACSL6), and carnitine palmitoyl transferases 1A and 1B (CPT1A and CPT1B). Overall, we provide a comprehensive view of these OMM enzymes in non-cancerous and cancer cells as well as their potential as targets for developing novel chemotherapies.

Collectively, these findings indicate that ACSL1 is highly expressed in CRC tissues and is correlated with poor prognosis. Importantly, our study provides the first evidence that the ACSL1-JAK2-STAT3 pathway facilitates CRC cell proliferation and migration, highlighting its potential as a therapeutic target.

Our findings establish EZH2 as a critical regulator of lenvatinib resistance in HCC through ACSL1-mediated ferroptosis suppression. The EZH2-H3K27me3-ACSL1 axis represents a promising therapeutic target for overcoming drug resistance, offering new strategies to improve HCC treatment outcomes.

Felodipine and GSK2033 treatment eliminated the differential effects on TG concentration between wild-type and Ces1d-deficient hepatocytes. The results suggest that CES1/Ces1d activates PPARγ, LXR and SREBP1c pathways, thereby increasing TG synthesis and LD storage by augmenting fatty acid esterification.