ArticleThe Journal of biological chemistry2012
Negative regulation of AMP-activated protein kinase (AMPK) activity by macrophage migration inhibitory factor (MIF) family members in non-small cell lung carcinomas.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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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.
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Who cites it
27 citing papers in PubMed, 42 citations in OpenAlex.
- Multi-omics integration reveals that pyrimidine metabolism in lung adenocarcinoma drives an immunosuppressive microenvironment.iScience · 2026Article
- Anticancer Mechanism ofPharmaceuticals (Basel, Switzerland) · 2024Review
- CD74 Promotes Cyst Growth and Renal Fibrosis in Autosomal Dominant Polycystic Kidney Disease.Cells · 2024Article
- The roles of macrophage migration inhibitory factor in retinal diseases.Neural regeneration research · 2024Review
- MIF contribution to progressive brain diseases.Journal of neuroinflammation · 2024Review
- Enhanced tumor control and survival in preclinical models with adoptive cell therapy preceded by low-dose radiotherapy.Frontiers in oncology · 2024Article
- Emerging Role of the Macrophage Migration Inhibitory Factor Family of Cytokines in Neuroblastoma. Pathogenic Effectors and Novel Therapeutic Targets?Molecules (Basel, Switzerland) · 2020Review
- MIF-Dependent Control of Tumor Immunity.Frontiers in immunology · 2020Review
- A selective small-molecule inhibitor of macrophage migration inhibitory factor-2 (MIF-2), a MIF cytokine superfamily member, inhibits MIF-2 biological activity.The Journal of biological chemistry · 2019Article
- AMPKα2 knockout enhances tumour inflammation through exacerbated liver injury and energy deprivation-associated AMPKα1 activation.Journal of cellular and molecular medicine · 2019Article
- Autophagic flux is essential for the downregulation of D-dopachrome tautomerase by atractylenolide I to ameliorate intestinal adenoma formation.Journal of cell communication and signaling · 2018Article
- Structural Plasticity in the C-Terminal Region of Macrophage Migration Inhibitory Factor-2 Is Associated with an Induced Fit Mechanism for a Selective Inhibitor.Biochemistry · 2018Article
- Review
- Crosstalk between calcium and reactive oxygen species signaling in cancer.Cell calcium · 2017Review
- 25 Years On: A Retrospective on Migration Inhibitory Factor in Tumor Angiogenesis.Molecular medicine (Cambridge, Mass.) · 2015Review
- Prognostic value of several biomarkers for the patients with malignant pleural mesothelioma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015Review
- Role of macrophage migration inhibitory factor in age-related lung disease.American journal of physiology. Lung cellular and molecular physiology · 2015Review
- Macrophage migration inhibitory factor promotes cyst growth in polycystic kidney disease.The Journal of clinical investigation · 2015Article
- Macrophage migration inhibitory factor (MIF) enzymatic activity and lung cancer.Molecular medicine (Cambridge, Mass.) · 2015Article
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
AMP-activated protein kinase (AMPK) is a nutrient- and metabolic stress-sensing enzyme activated by the tumor suppressor kinase, LKB1. Because macrophage migration inhibitory factor (MIF) and its functional homolog, d-dopachrome tautomerase (d-DT), have protumorigenic functions in non-small cell lung carcinomas (NSCLCs) but have AMPK-activating properties in nonmalignant cell types, we set out to investigate this apparent paradox. Our data now suggest that, in contrast to MIF and d-DTs AMPK-activating properties in nontransformed cells, MIF and d-DT act cooperatively to inhibit steady-state phosphorylation and activation of AMPK in LKB1 wild type and LKB1 mutant human NSCLC cell lines. Our data further indicate that MIF and d-DT, acting through their shared cell surface receptor, CD74, antagonize NSCLC AMPK activation by maintaining glucose uptake, ATP production, and redox balance, resulting in reduced Ca(2+)/calmodulin-dependent kinase kinase β-dependent AMPK activation. Combined, these studies indicate that MIF and d-DT cooperate to inhibit AMPK activation in an LKB1-independent manner.
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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.