ArticleEndocrine pathology2026
The Proteome of Bilateral Macronodular Adrenocortical Disease (BMAD) Shows Different Profiles Correlating with the Genetic Causes and Reveals Specific Dysregulation of RNA Polymerase II and Cholesterol Biosynthesis Enzymes.
Article in Endocrine pathology, 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
14 authors.
Funding
Abstract
Bilateral macronodular adrenocortical disease (BMAD) is currently described as composed of 4 microscopic subtypes (subtype 1 to 4) and 3 molecular groups (ARMC5-altered, KDM1A-altered, and unknown). Little is known about protein heterogeneity and its links with BMAD characteristics. The aim of this work is to study the protein signatures of BMADs and their correlations with microscopy and genetics. Liquid chromatography and tandem mass spectrometry (LC-MS/MS) was performed on 24 BMADs: 7 ARMC5, 4 KDM1A, 13 non-KDM1A, non-ARMC5 BMADs and 2 normal adrenal glands and 10 adrenal adenomas as control. Unsupervised clustering divided BMAD samples into 3 proteomic groups. The first group is composed of ARMC5-altered BMADs (subtype 1) and is characterized by an accumulation of RNA polymerase II (Pol II) subunits. The second, composed of KDM1A-altered (subtype 2) patients and subtype 4 BMADs (oncocytic), is characterized by an accumulation of cholesterol biosynthesis enzymes (such as FDFT1). The last group has no specific signature detected and is composed of subtypes 1 and 3 BMAD without ARMC5 alteration. Immunohistochemical analyses with anti Pol II subunits and cholesterol biosynthesis enzymes correlate with the three proteomic groups. Proteins specifically accumulated in ARMC5-altered BMADS such as POLR2A could be used as biomarkers to detect ARMC5 alterations. Data are available via ProteomeXchange with identifier PXD070500. Our study explores BMAD proteome using LC-MS/MS. The 3 proteomic groups mostly overlap the 4 microscopic and 3 molecular groups of BMAD. Accumulation of Pol II subunits consistent with the described role of ARMC5 could play a role in the pathogenesis of these BMADs. KDM1A-altered (subtype 2) and subtype 4 BMADs showed an accumulation of proteins involved in lipid metabolism that could contribute to hypercortisolism. These results reveal specific protein patterns pointing to various cellular processes opening new perspectives to understand BMAD pathophysiology and provide new tools for the pathologists.
Indexed as
Identifiers
41524866What 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.