ArticleMolecular & cellular proteomics : MCP2026
Long-Chain S-Acylation Is a Key Modulator During the Macrophage Inflammatory Response.
Article in Molecular & cellular proteomics : MCP, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Long-chain S-acylation is a reversible lipid modification critical for regulating protein localization, stability, and signaling, yet its role in macrophage-mediated inflammation remains incompletely understood. Here, we combine stable isotope labeling by amino acids in cell culture (SILAC) with site-specific acyl-biotin exchange (ssABE) to generate a comprehensive map of the long-chain S-acylation landscape in THP-1 macrophages polarized to M0 and M(LPS + IFNɣ) states. Our quantitative proteomics reveal polarization-specific S-acylation patterns and uncover numerous inflammation-related modification sites, including novel S-acyl-peptidoforms, which are distinct S-acylated variants of the same peptide such as WARS (C305/C309), highlighting their potential relevance in macrophage activation. Pharmacological inhibition of S-acylation with the broad-spectrum inhibitor 2-bromopalmitate suppresses secretion of key pro-inflammatory chemokines (CXCL9, CXCL10, and CCL4) and disrupts IDO1-mediated tryptophan catabolism, while Palmostatin B mainly stabilizes S-acylation on GPCR signaling proteins. Together, these findings position long-chain S-acylation as a key regulatory mechanism during macrophage activation and a promising target for therapeutic intervention in inflammatory disease.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.