Clinical and Molecular Characteristics of PRKACA L206R Mutant Cortisol-Producing Adenomas in Korean Patients.


Journal

Endocrinology and metabolism (Seoul, Korea)
ISSN: 2093-5978
Titre abrégé: Endocrinol Metab (Seoul)
Pays: Korea (South)
ID NLM: 101554139

Informations de publication

Date de publication:
12 2021
Historique:
received: 30 07 2021
accepted: 14 10 2021
pubmed: 3 12 2021
medline: 16 3 2022
entrez: 2 12 2021
Statut: ppublish

Résumé

An activating mutation (c.617A>C/p.Lys206Arg, L206R) in protein kinase cAMP-activated catalytic subunit alpha (PRKACA) has been reported in 35% to 65% of cases of cortisol-producing adenomas (CPAs). We aimed to compare the clinical characteristics and transcriptome analysis between PRKACA L206R mutants and wild-type CPAs in Korea. We included 57 subjects with CPAs who underwent adrenalectomy at Seoul National University Hospital. Sanger sequencing for PRKACA was conducted in 57 CPA tumor tissues. RNA sequencing was performed in 13 fresh-frozen tumor tissues. The prevalence of the PRKACA L206R mutation was 51% (29/57). The mean age of the study subjects was 42±12 years, and 87.7% (50/57) of the patients were female. Subjects with PRKACA L206R mutant CPAs showed smaller adenoma size (3.3±0.7 cm vs. 3.8±1.2 cm, P=0.059) and lower dehydroepiandrosterone sulfate levels (218±180 ng/mL vs. 1,511±3,307 ng/mL, P=0.001) than those with PRKACA wild-type CPAs. Transcriptome profiling identified 244 differentially expressed genes (DEGs) between PRKACA L206R mutant (n=8) and wild-type CPAs (n=5), including five upregulated and 239 downregulated genes in PRKACA L206R mutant CPAs (|fold change| ≥2, P<0.05). Among the upstream regulators of DEGs, CTNNB1 was the most significant transcription regulator. In several pathway analyses, the Wnt signaling pathway was downregulated and the steroid biosynthesis pathway was upregulated in PRKACA mutants. Protein-protein interaction analysis also showed that PRKACA downregulates Wnt signaling and upregulates steroid biosynthesis. The PRKACA L206R mutation in CPAs causes high hormonal activity with a limited proliferative capacity, as supported by transcriptome profiling.

Sections du résumé

BACKGROUND
An activating mutation (c.617A>C/p.Lys206Arg, L206R) in protein kinase cAMP-activated catalytic subunit alpha (PRKACA) has been reported in 35% to 65% of cases of cortisol-producing adenomas (CPAs). We aimed to compare the clinical characteristics and transcriptome analysis between PRKACA L206R mutants and wild-type CPAs in Korea.
METHODS
We included 57 subjects with CPAs who underwent adrenalectomy at Seoul National University Hospital. Sanger sequencing for PRKACA was conducted in 57 CPA tumor tissues. RNA sequencing was performed in 13 fresh-frozen tumor tissues.
RESULTS
The prevalence of the PRKACA L206R mutation was 51% (29/57). The mean age of the study subjects was 42±12 years, and 87.7% (50/57) of the patients were female. Subjects with PRKACA L206R mutant CPAs showed smaller adenoma size (3.3±0.7 cm vs. 3.8±1.2 cm, P=0.059) and lower dehydroepiandrosterone sulfate levels (218±180 ng/mL vs. 1,511±3,307 ng/mL, P=0.001) than those with PRKACA wild-type CPAs. Transcriptome profiling identified 244 differentially expressed genes (DEGs) between PRKACA L206R mutant (n=8) and wild-type CPAs (n=5), including five upregulated and 239 downregulated genes in PRKACA L206R mutant CPAs (|fold change| ≥2, P<0.05). Among the upstream regulators of DEGs, CTNNB1 was the most significant transcription regulator. In several pathway analyses, the Wnt signaling pathway was downregulated and the steroid biosynthesis pathway was upregulated in PRKACA mutants. Protein-protein interaction analysis also showed that PRKACA downregulates Wnt signaling and upregulates steroid biosynthesis.
CONCLUSION
The PRKACA L206R mutation in CPAs causes high hormonal activity with a limited proliferative capacity, as supported by transcriptome profiling.

Identifiants

pubmed: 34852451
pii: EnM.2021.1217
doi: 10.3803/EnM.2021.1217
pmc: PMC8743585
doi:

Substances chimiques

Protein Kinases EC 2.7.-
Cyclic AMP-Dependent Protein Kinase Catalytic Subunits EC 2.7.11.11
PRKACA protein, human EC 2.7.11.11
Hydrocortisone WI4X0X7BPJ

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1287-1297

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Auteurs

Insoon Jang (I)

Translational Research Institute, Biomedical Research Institute, Seoul National University Hospital, Seoul, Korea.

Su-Jin Kim (SJ)

Department of Surgery, Seoul National University Hospital, Seoul National University College of Medicine, Seoul, Korea.
Cancer Research Institute, Seoul National University College of Medicine, Seoul, Korea.
Division of Surgery, Thyroid Center, Seoul National University Cancer Hospital, Seoul, Korea.

Ra-Young Song (RY)

Department of Surgery, Chung-Ang University Hospital, Seoul, Korea.

Kwangsoo Kim (K)

Translational Research Institute, Biomedical Research Institute, Seoul National University Hospital, Seoul, Korea.

Seongmin Choi (S)

Translational Research Institute, Biomedical Research Institute, Seoul National University Hospital, Seoul, Korea.

Jang-Seok Lee (JS)

Translational Research Institute, Biomedical Research Institute, Seoul National University Hospital, Seoul, Korea.

Min-Kyeong Gwon (MK)

Translational Research Institute, Biomedical Research Institute, Seoul National University Hospital, Seoul, Korea.

Moon Woo Seong (MW)

Department of Laboratory Medicine, Seoul National University Hospital, Seoul National University College of Medicine, Seoul, Korea.

Kyu Eun Lee (KE)

Department of Surgery, Seoul National University Hospital, Seoul National University College of Medicine, Seoul, Korea.
Cancer Research Institute, Seoul National University College of Medicine, Seoul, Korea.
Division of Surgery, Thyroid Center, Seoul National University Cancer Hospital, Seoul, Korea.

Jung Hee Kim (JH)

Department of Internal Medicine, Seoul National University Hospital, Seoul National University College of Medicine, Seoul, Korea.

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Classifications MeSH