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Corrigendum Free access | 10.1172/JCI79293

Osteocalcin regulates murine and human fertility through a pancreas-bone-testis axis

Franck Oury, Mathieu Ferron, Wang Huizhen, Cyrille Confavreux, Lin Xu, Julie Lacombe, Prashanth Srinivas, Alexandre Chamouni, Francesca Lugani, Herve Lejeune, T. Rajendra Kumar, Ingrid Plotton, and Gerard Karsenty

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First published December 1, 2014 - More info

Published in Volume 124, Issue 12 on December 1, 2014
J Clin Invest. 2014;124(12):5522–5522. https://doi.org/10.1172/JCI79293.
Copyright © 2014, American Society for Clinical Investigation
First published December 1, 2014 - Version history

Related article:

Osteocalcin regulates murine and human fertility through a pancreas-bone-testis axis
Franck Oury, … , Ingrid Plotton, Gerard Karsenty
Franck Oury, … , Ingrid Plotton, Gerard Karsenty
Category: Research Article

Osteocalcin regulates murine and human fertility through a pancreas-bone-testis axis

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Abstract

The osteoblast-derived hormone osteocalcin promotes testosterone biosynthesis in the mouse testis by binding to GPRC6A in Leydig cells. Interestingly, Osteocalcin-deficient mice exhibit increased levels of luteinizing hormone (LH), a pituitary hormone that regulates sex steroid synthesis in the testes. These observations raise the question of whether LH regulates osteocalcin’s reproductive effects. Additionally, there is growing evidence that osteocalcin levels are a reliable marker of insulin secretion and sensitivity and circulating levels of testosterone in humans, but the endocrine function of osteocalcin is unclear. Using mouse models, we found that osteocalcin and LH act in 2 parallel pathways and that osteocalcin-stimulated testosterone synthesis is positively regulated by bone resorption and insulin signaling in osteoblasts. To determine the importance of osteocalcin in humans, we analyzed a cohort of patients with primary testicular failure and identified 2 individuals harboring the same heterozygous missense variant in one of the transmembrane domains of GPRC6A, which prevented the receptor from localizing to the cell membrane. This study uncovers the existence of a second endocrine axis that is necessary for optimal male fertility in the mouse and suggests that osteocalcin modulates reproductive function in humans.

Authors

Franck Oury, Mathieu Ferron, Wang Huizhen, Cyrille Confavreux, Lin Xu, Julie Lacombe, Prashanth Srinivas, Alexandre Chamouni, Francesca Lugani, Herve Lejeune, T. Rajendra Kumar, Ingrid Plotton, Gerard Karsenty

×

Original citation: J Clin Invest. 2013;123(6):2421–2433. doi:10.1172/JCI65952.

Citation for this corrigendum: J Clin Invest. 2014;124(12):5522. doi:10.1172/JCI79293.

In the original article, the substitution mutation in GPRC6A at F464Y was erroneously described as located in one of the transmembrane domains of GPRC6A; however, the F464Y mutation is located in the long N-terminal region of GPRC6A (1-594AA). This error affected portions of the text in the Abstract, Introduction, Results, and Discussion. The corrected sentences appear below.

Abstract (page 2421):

To determine the importance of osteocalcin in humans, we analyzed a cohort of patients with primary testicular failure and identified 2 individuals harboring the same heterozygous missense variant of GPRC6A, which prevented the receptor from localizing to the cell membrane.

Introduction (page 2421):

In trying to expand the biological relevance of osteocalcin from mouse to human, we identified in 2 patients with peripheral testicular failure the same amino acid substitution affecting a highly conserved residue in the long N-terminal domain (1-594AA) of GPRC6A.

Results (page 2429):

We sequenced all exons of Osteocalcin and GPRC6A, the receptor mediating osteocalcin reproductive function in Leydig cells (2), in these patients. Two patients in this cohort harbored a T→A transversion in exon 4 (g.117121904A/T), resulting in an amino acid substitution in the long N-terminal domain of GPRC6A (F464Y) (Figure 7, A and B, and Supplemental Figure 6A).

Discussion (page 2431):

This missense mutation affected a highly conserved residue, occurred in the N-terminal domain region of the molecule, and prevented its localization to the cell membrane, therefore resulting in a loss of function of GPRC6A.

The authors regret the error.

Footnotes

See the related article beginning on page 2421.

Version history
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