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Your search keyword '"Jiang, Lu"' showing total 408 results
Start Over Author "Jiang, Lu" Publication Type Periodicals Publisher elsevier b.v.
408 results on '"Jiang, Lu"'

47. When pyro(ptosis) meets palm(itoylation).

Author

Jiang, Lu, Wang, Zirui, Xu, Ting, and Zhang, Leiliang

Subjects
*APOPTOSIS, *TYPE I interferons, *PALMITOYLATION, *PYROPTOSIS, *VENOM
Abstract

Pyroptosis, a programmed cell death process, is vital for the immune response against microbial infections and internal danger signals. Recent studies have highlighted the importance of protein palmitoylation, a modification that involves attaching palmitate to cysteine residues, in regulating key proteins involved in pyroptosis. Palmitoylation of cGAS at residue C474 by ZDHHC18 affects its enzymatic activity and DNA binding ability. Similarly, ZDHHC9 promotes cGAS activity through palmitoylation at residues C404/405. NLRP3 palmitoylation at residue C844, mediated by ZDHHC12, impacts its stability and interactions with other proteins, crucial for activating the NLRP3 inflammasome and triggering inflammation. However, the role of ZDHHC5 in NLRP3 palmitoylation remains uncertain due to conflicting findings. Palmitoylation at C88/91 is essential for STING activation and induction of type I interferons. It modulates the formation of multimeric complexes and downstream signaling pathways. GSDMD palmitoylation at C191 is necessary for pore formation and membrane translocation, while GSDME palmitoylation at C407/408 is associated with drug-induced pyroptosis. Moreover, palmitoylation of NOD1 and NOD2 influences their membrane recruitment and immune signaling pathways in response to bacterial peptidoglycans, acting as upstream regulators of pyroptosis. This review summarizes the important roles for palmitoylation in regulating the function of key pyroptosis-related proteins, shedding light on the intricate mechanisms governing immune responses and inflammation. • cGAS undergoes palmitoylation. • STING palmitoylation is crucial for pyroptosis. • NLRP3 palmitoylation is important for pyroptosis. • ZDHHC5-mediated palmitoylation of NOD1/2 is crucial for pyroptosis. • Palmitoylation of GSDMD and GSDME is essential for pyroptosis. [ABSTRACT FROM AUTHOR]

Published
2024
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48. Targeting GPX4-mediated Ferroptosis Alleviates Liver Steatosis in a Rat Model of Total Parenteral Nutrition.

Author

Cheng, Siyang, Wang, Ying, Zhao, Yuling, Wang, Nan, Yan, Junkai, Jiang, Lu, and Cai, Wei

Abstract

Parenteral nutrition-associated liver disease (PNALD) is a common hepatobiliary complication resulting from long-term parenteral nutrition (PN) that is associated with significant morbidity and mortality. Ferroptosis plays a significant role in the pathogenesis of various liver diseases. This study aims to explore the role of ferroptosis in PNALD and to uncover its underlying mechanisms. Ferroptosis was evaluated in pediatric patients with PNALD and in rats administered with total parenteral nutrition (TPN) as an animal model of PNALD. In TPN-fed rats, we applied liproxstatin-1 (Lip-1) to inhibit ferroptosis for 7 days and assessed its impact on liver steatosis. We performed RNA-seq analysis to profile the alterations in miRNAs in livers from TPN-fed rats. The ferroptosis-promoting effects of miR-431 were evaluated in HepG2 cells and the direct targeting effects on glutathione peroxidase 4 (GPX4) were evaluated in HEK293T cells. RNA-seq analysis and experimental validation suggested that ferroptosis was increased in the livers of pediatric patients and rats with PNALD. Inhibiting ferroptosis with Lip-1 attenuated liver steatosis by regulating PPARα expression. RNA-seq analysis uncovered miR-431 as the most upregulated miRNA in the livers of TPN-fed rats, showing a negative correlation with hepatic GPX4 expression. In vitro studies demonstrated that miR-431 promoted ferroptosis by directly binding to the 3′UTR of GPX4 mRNA, resulting in the suppression of its expression. Our study demonstrates that TPN induces the upregulation of miR-431 in rats, leading to activation of ferroptosis through downregulation of GPX4. Inhibition of ferroptosis attenuates TPN-induced liver steatosis by regulating PPARα expression. [Display omitted] [ABSTRACT FROM AUTHOR]

Published
2024
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