Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 3 complete abstracts (607 words), 9 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
A butyl-diphenyl-pyrazolidinedione that has anti-inflammatory, antipyretic, and analgesic activities. It has been used in ankylosing spondylitis; rheumatoid arthritis; and reactive arthritis.
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Diphenylbutazone; Butacote; Butazolidin; Butadione; Butadion; Butapyrazole; Butapirazol; Fenilbutazon.
Where it fits in the MeSH classification
- Broader topics
- Pyrazolones
- Narrower topics
- Feprazone; Oxyphenbutazone; Sulfinpyrazone
Related concepts
- Ankylosing Spondylitis
- Rheumatoid Arthritis
- Reactive Arthritis
Research landscape
PubMed indexes 8,001 records tagged with the MeSH heading “Phenylbutazone” (counts retrieved 2026-10-31). 53 of them (0.7%) were published from 2020 onward, and the busiest period so far is through 1999 with 7,659 records.
Reviews account for 401 records (5.0%) and meta-analyses for 3. Randomized controlled trials number 187 (2.3%) as a share of all records on the topic.
Show the data
| Period | Records |
|---|---|
| through 1999 | 7,659 |
| 2000-2009 | 184 |
| 2010-2019 | 105 |
| 2020 onward | 53 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 401 | 5.0% |
| Meta-analyses | 3 | 0.0% |
| Randomized controlled trials | 187 | 2.3% |
Method: PubMed query "Phenylbutazone"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-31.
Reading the evidence in drugs and chemicals
Studies of a chemical or drug can answer very different questions: what it is and how it behaves in cells and animals, how the body handles it, and whether it changes outcomes in people. Laboratory and animal findings often do not carry over to patients, and observational studies of exposures are confounded by who uses a substance and why. Nothing on this page is a recommendation to use, avoid, start or stop any substance or medicine; talk to a qualified clinician or pharmacist about your own situation. Check the dose, the species, the comparison group and whether a patient-relevant outcome was measured.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| Vinblastine and sulfinpyrazone export by the multidrug resistance protein MRP2 is associated with glutathione export | 2000 | Research article Design not recorded in structured metadata | 158 | cc by PMID 10917554 · DOI · PMC2374564 |
| Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding | 2020 | Research article Design not recorded in structured metadata | 52 | cc by PMID 32023900 · DOI · PMC7038104 |
| Phenylbutazone induces expression of MBNL1 and suppresses formation of MBNL1-CUG RNA foci in a mouse model of myotonic dystrophy | 2016 | Research article Design not recorded in structured metadata | 39 | cc by PMID 27126921 · DOI · PMC4850456 |
Vinblastine and sulfinpyrazone export by the multidrug resistance protein MRP2 is associated with glutathione export [1]
Abstract reading summary — source excerpts
- Opening excerpt
- The multidrug resistance proteins MRP1 and MRP2 are members of the same subfamily of ATP-binding cassette transporters.
- Closing excerpt
- Models of MRP action are discussed that could explain these results.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (207 words)
The multidrug resistance proteins MRP1 and MRP2 are members of the same subfamily of ATP-binding cassette transporters. Besides organic molecules conjugated to negatively charged ligands, these proteins also transport cytotoxic drugs for which no negatively charged conjugates are known to exist. In polarized MDCKII cells, MRP1 routes to the lateral plasma membrane, and MRP2 to the apical plasma membrane. In these cells MRP1 transports daunorubicin, and MRP2 vinblastine; both transporters export reduced glutathione (GSH) into the medium. We demonstrate that glutathione transport in MDCKII-MRP1 cells is inhibited by the inhibitors of organic anion transporters sulfinpyrazone, indomethacin, probenecid and benzbromarone. In MDCKII-MRP2 cells, GSH export is stimulated by low concentrations of sulfinpyrazone or indomethacin, whereas export is inhibited down to control levels at high concentrations. We find that unmodified sulfinpyrazone is a substrate for MRP2, also at concentrations where GSH export is inhibited. We also show that GSH export in MDCKII-MRP2 cells increases in the presence of vinblastine, and that the stoichiometry between drug and GSH exported is between two and three. Our data indicate that transport of sulfinpyrazone and vinblastine is associated with GSH export. However, at high sulfinpyrazone concentrations this compound is transported without GSH. Models of MRP action are discussed that could explain these results.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 10917554 · DOI · PMC2374564
Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding [2]
Abstract reading summary — source excerpts
- Opening excerpt
- Human serum albumin (HSA) is a protein that transports neutral and acid ligands in the organism.
- Closing excerpt
- Whereas, using fluorescence spectroscopy, the association constants differing for fresh and incubated HSA solutions in the presence of dansyl-amino acids and markers for binding sites were calculated and allowed observation of the conformational changes in HSA molecule.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (201 words)
Human serum albumin (HSA) is a protein that transports neutral and acid ligands in the organism. Depending on the environment's pH conditions, HSA can take one of the five isomeric forms that change its conformation. HSA can form aggregates resembling those in vitro formed from amyloid at physiological pH (neutral and acidic). Not surprisingly, the main goal of the research was aggregation/fibrillation of HSA, the study of the physicochemical properties of formed amyloid fibrils using thioflavin T (ThT) and the analysis of ligand binding to aggregated/fibrillated albumin in the presence of dansyl-l-glutamine (dGlu), dansyl-l-proline (dPro), phenylbutazone (Phb) and ketoprofen (Ket). Solutions of human serum albumin, both non-modified and modified, were examined with the use of fluorescence, absorption and circular dichroism (CD) spectroscopy. The experiments conducted allowed observation of changes in the structure of incubated HSA (HSAINC) in relation to nonmodified HSA (HSAFR). The formed aggregates/fibrillation differed in structure from HSA monomers and dimers. Based on CD spectroscopy, previously absent βstructural constructs have been registered. Whereas, using fluorescence spectroscopy, the association constants differing for fresh and incubated HSA solutions in the presence of dansyl-amino acids and markers for binding sites were calculated and allowed observation of the conformational changes in HSA molecule.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 32023900 · DOI · PMC7038104
Phenylbutazone induces expression of MBNL1 and suppresses formation of MBNL1-CUG RNA foci in a mouse model of myotonic dystrophy [3]
Abstract reading summary — source excerpts
- Opening excerpt
- Myotonic dystrophy type 1 (DM1) is caused by abnormal expansion of CTG repeats in the 3' untranslated region of the DMPK gene.
- Closing excerpt
- Our studies suggest that PBZ is a potent therapeutic agent for DM1 that upregulates availability of MBNL1.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (199 words)
Myotonic dystrophy type 1 (DM1) is caused by abnormal expansion of CTG repeats in the 3' untranslated region of the DMPK gene. Expanded CTG repeats are transcribed into RNA and make an aggregate with a splicing regulator, MBNL1, in the nucleus, which is called the nuclear foci. The nuclear foci sequestrates and downregulates availability of MBNL1. Symptomatic treatments are available for DM1, but no rational therapy is available. In this study, we found that a nonsteroidal anti-inflammatory drug (NSAID), phenylbutazone (PBZ), upregulated the expression of MBNL1 in C2C12 myoblasts as well as in the HSA(LR) mouse model for DM1. In the DM1 mice model, PBZ ameliorated aberrant splicing of Clcn1, Nfix, and Rpn2. PBZ increased expression of skeletal muscle chloride channel, decreased abnormal central nuclei of muscle fibers, and improved wheel-running activity in HSA(LR) mice. We found that the effect of PBZ was conferred by two distinct mechanisms. First, PBZ suppressed methylation of an enhancer region in Mbnl1 intron 1, and enhanced transcription of Mbnl1 mRNA. Second, PBZ attenuated binding of MBNL1 to abnormally expanded CUG repeats in cellulo and in vitro. Our studies suggest that PBZ is a potent therapeutic agent for DM1 that upregulates availability of MBNL1.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 27126921 · DOI · PMC4850456
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article Ornithine transcarbamylase deficiency: a urea cycle defect [4]
- Research article Phenylbutazone in the horse: a review [5]
- Research article PAGET'S DISEASE OF BONE: CLINICAL AND METABOLIC OBSERVATIONS [6]
- Research article Does platelet antiaggregant therapy lessen the severity of stroke? [7]
- Research article Role of blood platelets in coronary artery disease [8]
- Research article Pharmacokinetics, pharmacodynamics, metabolism, toxicology and residues of phenylbutazone in humans and horses [9]
References
- Evers R, de Haas M, Sparidans R, Beijnen J, Wielinga PR, Lankelma J, et al.. Vinblastine and sulfinpyrazone export by the multidrug resistance protein MRP2 is associated with glutathione export. . 2000. PMID 10917554 · DOI · PMC2374564
- Maciążek-Jurczyk M, Janas K, Pożycka J, Szkudlarek A, Rogóż W, Owczarzy A, et al.. Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding. . 2020. PMID 32023900 · DOI · PMC7038104
- Chen G, Masuda A, Konishi H, Ohkawara B, Ito M, Kinoshita M, et al.. Phenylbutazone induces expression of MBNL1 and suppresses formation of MBNL1-CUG RNA foci in a mouse model of myotonic dystrophy. . 2016. PMID 27126921 · DOI · PMC4850456
- Gordon N. Ornithine transcarbamylase deficiency: a urea cycle defect. Eur J Paediatr Neurol. 2003. PMID 12788037 · DOI
- Tobin T, Chay S, Kamerling S, Woods WE, Weckman TJ, Blake JW, et al.. Phenylbutazone in the horse: a review. J Vet Pharmacol Ther. 1986. PMID 3517382 · DOI
- DE DEUXCHAISNES CN, KRANE SM. PAGET'S DISEASE OF BONE: CLINICAL AND METABOLIC OBSERVATIONS. Medicine (Baltimore). 1964. PMID 14170787
- Grotta JC, Lemak NA, Gary H, Fields WS, Vital D. Does platelet antiaggregant therapy lessen the severity of stroke?. Neurology. 1985. PMID 3887210 · DOI
- Haft JI. Role of blood platelets in coronary artery disease. Am J Cardiol. 1979. PMID 35967 · DOI
- Lees P, Toutain PL. Pharmacokinetics, pharmacodynamics, metabolism, toxicology and residues of phenylbutazone in humans and horses. Vet J. 2013. PMID 23721873 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-31.
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Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.