ArticleScientific reports2015
Regulation of growth hormone secretion by (pro)renin receptor.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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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
11 citing papers in PubMed, 17 citations in OpenAlex.
- ATP6AP2 is robustly expressed in pancreatic β cells and neuroendocrine tumors, and plays a role in maintaining cellular viability.Scientific reports · 2023Article
- ANGT_HUMAN[448-462], an Anorexigenic Peptide Identified Using Plasma Peptidomics.Journal of the Endocrine Society · 2022Article
- GIP_HUMAN[22-51] is a new proatherogenic peptide identified by native plasma peptidomics.Scientific reports · 2021Article
- Circulating prorenin: its molecular forms and plasma concentrations.Hypertension research : official journal of the Japanese Society of Hypertension · 2021Article
- Suprabasin-derived bioactive peptides identified by plasma peptidomics.Scientific reports · 2021Article
- Immunohistochemistry for (Pro)renin Receptor in Humans.International journal of endocrinology · 2021Article
- Review
- Molecular form and concentration of serum αScientific reports · 2019Article
- Identification of the salusin-β receptor using proteoliposomes embedded with endogenous membrane proteins.Scientific reports · 2018Article
- Elevated (Pro)renin Receptor Expression Contributes to Maintaining Aerobic Metabolism in Growth Hormone Deficiency.Journal of the Endocrine Society · 2018Article
- V-ATPases and osteoclasts: ambiguous future of V-ATPases inhibitors in osteoporosis.Theranostics · 2018Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
(Pro)renin receptor (PRR) has a single transmembrane domain that co-purifies with the vacuolar H(+)-ATPase (V-ATPase). In addition to its role in cellular acidification, V-ATPase has been implicated in membrane fusion and exocytosis via its Vo domain. Results from the present study show that PRR is expressed in pituitary adenoma cells and regulates growth hormone (GH) release via V-ATPase-induced cellular acidification. Positive PRR immunoreactivity was detected more often in surgically resected, growth hormone-producing adenomas (GHomas) than in nonfunctional pituitary adenomas. GHomas strongly expressing PRR showed excess GH secretion, as evidenced by distinctly high plasma GH and insulin-like growth factor-1 levels, as well as an elevated nadir GH in response to the oral glucose tolerance test. Suppression of PRR expression in rat GHoma-derived GH3 cells using PRR siRNA resulted in reduced GH secretion and significantly enhanced intracellular GH accumulation. GH3 treatment with bafilomycin A1, a V-ATPase inhibitor, also blocked GH release, indicating mediation via impaired cellular acidification of V-ATPase. PRR knockdown decreased Atp6l, a subunit of the Vo domain that destabilizes V-ATPase assembly, increased intracellular GH, and decreased GH release. To our knowledge, this is the first report demonstrating a pivotal role for PRR in a pituitary hormone release mechanism.
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