Amylin inhibits bone resorption while the calcitonin receptor controls bone formation in vivo
(2004) In Journal of Cell Biology 164(4). p.509-514- Abstract
- Amylin is a member of the calcitonin family of hormones cosecreted with insulin by pancreatic beta cells. Cell culture assays suggest that amylin could affect bone formation and bone resorption, this latter function after its binding to the calcitonin receptor (CALCR). Here we show that Amylin inactivation leads to a low bone mass due to an increase in bone resorption, whereas bone formation is unaffected. In vitro, amylin inhibits fusion of mononucleated osteoclast precursors into multinucleated osteoclasts in an ERK1/2-dependent manner. Although Amylin +/- mice like Amylin-deficient mice display a low bone mass phenotype and increased bone resorption, Calcr +/- mice display a high bone mass due to an increase in bone formation. Moreover,... (More)
- Amylin is a member of the calcitonin family of hormones cosecreted with insulin by pancreatic beta cells. Cell culture assays suggest that amylin could affect bone formation and bone resorption, this latter function after its binding to the calcitonin receptor (CALCR). Here we show that Amylin inactivation leads to a low bone mass due to an increase in bone resorption, whereas bone formation is unaffected. In vitro, amylin inhibits fusion of mononucleated osteoclast precursors into multinucleated osteoclasts in an ERK1/2-dependent manner. Although Amylin +/- mice like Amylin-deficient mice display a low bone mass phenotype and increased bone resorption, Calcr +/- mice display a high bone mass due to an increase in bone formation. Moreover, compound heterozygote mice for Calcr and Amylin inactivation displayed bone abnormalities observed in both Calcr +/- and Amylin +/- mice, thereby ruling out that amylin uses CALCR to inhibit osteoclastogenesis in vivo. Thus, amylin is a physiological regulator of bone resorption that acts through an unidentified receptor. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/287071
- author
- Dacquin, R ; Davey, RA ; Laplace, C ; Levasseur, G ; Morris, HA ; Goldring, SR ; Gebre-Medhin, Samuel LU ; Galson, DL ; Zajac, JD and Karsenty, G
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- mouse models, CALCR, islet amyloid polypeptide, CTR, osteoclast
- in
- Journal of Cell Biology
- volume
- 164
- issue
- 4
- pages
- 509 - 514
- publisher
- Rockefeller University Press
- external identifiers
-
- wos:000189077200017
- pmid:14970190
- scopus:10744220002
- ISSN
- 0021-9525
- DOI
- 10.1083/jcb.200312135
- language
- English
- LU publication?
- yes
- id
- 1b41b9c5-a4eb-4a98-8ae9-05373cd89337 (old id 287071)
- date added to LUP
- 2016-04-01 11:57:21
- date last changed
- 2022-03-05 08:52:19
@article{1b41b9c5-a4eb-4a98-8ae9-05373cd89337, abstract = {{Amylin is a member of the calcitonin family of hormones cosecreted with insulin by pancreatic beta cells. Cell culture assays suggest that amylin could affect bone formation and bone resorption, this latter function after its binding to the calcitonin receptor (CALCR). Here we show that Amylin inactivation leads to a low bone mass due to an increase in bone resorption, whereas bone formation is unaffected. In vitro, amylin inhibits fusion of mononucleated osteoclast precursors into multinucleated osteoclasts in an ERK1/2-dependent manner. Although Amylin +/- mice like Amylin-deficient mice display a low bone mass phenotype and increased bone resorption, Calcr +/- mice display a high bone mass due to an increase in bone formation. Moreover, compound heterozygote mice for Calcr and Amylin inactivation displayed bone abnormalities observed in both Calcr +/- and Amylin +/- mice, thereby ruling out that amylin uses CALCR to inhibit osteoclastogenesis in vivo. Thus, amylin is a physiological regulator of bone resorption that acts through an unidentified receptor.}}, author = {{Dacquin, R and Davey, RA and Laplace, C and Levasseur, G and Morris, HA and Goldring, SR and Gebre-Medhin, Samuel and Galson, DL and Zajac, JD and Karsenty, G}}, issn = {{0021-9525}}, keywords = {{mouse models; CALCR; islet amyloid polypeptide; CTR; osteoclast}}, language = {{eng}}, number = {{4}}, pages = {{509--514}}, publisher = {{Rockefeller University Press}}, series = {{Journal of Cell Biology}}, title = {{Amylin inhibits bone resorption while the calcitonin receptor controls bone formation in vivo}}, url = {{http://dx.doi.org/10.1083/jcb.200312135}}, doi = {{10.1083/jcb.200312135}}, volume = {{164}}, year = {{2004}}, }