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Article

Ribosomal protein S19 interacts with macrophage migration inhibitory factor and attenuates its pro-inflammatory function.

The Journal of biological chemistry - 20 Mar 2009

Filip Ana-Maria, Klug Jörg, Cayli Sevil, Fröhlich Suada, Henke Tamara, Lacher Philipp, Eickhoff Regina, Bulau Patrick, Linder Monika, Carlsson-Skwirut Christine, Leng Lin, Bucala Richard, Kraemer Sandra, Bernhagen Jürgen, Meinhardt Andreas

Abstract excerpt

Macrophage migration inhibitory factor (MIF) is a pleiotropic cytokine that has been implicated in the pathogenesis of inflammatory disorders such as infection, sepsis, and autoimmune disease. MIF exists preformed in cytoplasmic pools and exhibits an intrinsic tautomerase and oxidoreductase activity. MIF levels are elevated in the serum of animals and patients with infection or different inflammatory disorders....

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 19155217
DOI: 10.1074/jbc.M808620200
PMCID: PMC2658091

Genes

MIF
RPS19
CXCR2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Ribosomal protein S19 interacts with macrophage migration inhibitory factor and attenuates its pro-inflammatory function.PMID 19155217Read ↗

Identification of receptor-binding sites of monocyte chemotactic S19 ribosomal protein dimer.Semantic proximity Read ↗

A novel nucleolar protein interacts with ribosomal protein S19.Semantic proximity Read ↗

Macrophage migration inhibitory factor (MIF): a promising biomarker.Semantic proximity Read ↗

Identification and characterization of novel classes of macrophage migration inhibitory factor (MIF) inhibitors with distinct mechanisms of action.Semantic proximity Read ↗

Redox-dependent Structure and Dynamics of Macrophage Migration Inhibitory Factor Reveal Sites of Latent AllosterySemantic proximity Read ↗

An extraribosomal function of ribosomal protein L13a in macrophages resolves inflammation.Semantic proximity Read ↗

A tautomerase-null macrophage migration-inhibitory factor (MIF) gene knock-in mouse model reveals that protein interactions and not enzymatic activity mediate MIF-dependent growth regulation.Semantic proximity Read ↗

Mutation of the key residue for extraribosomal function of ribosomal protein S19 cause increased grooming behaviors in mice.Semantic proximity Read ↗

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MIF but not MIF-2 recruits inflammatory macrophages in an experimental polymicrobial sepsis model.Semantic proximity Read ↗

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