Calcitonin receptor

Last updated
CALCR
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases CALCR , CRT, CT-R, CTR, CTR1, calcitonin receptor
External IDs OMIM: 114131; MGI: 101950; HomoloGene: 1320; GeneCards: CALCR; OMA:CALCR - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001742
NM_001164737
NM_001164738

NM_001042725
NM_007588
NM_001355192
NM_001377018

RefSeq (protein)

NP_001158209
NP_001158210
NP_001733

NP_001036190
NP_031614
NP_001342121
NP_001363947

Location (UCSC) Chr 7: 93.42 – 93.57 Mb Chr 6: 3.69 – 3.76 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

The calcitonin receptor (CT) is a G protein-coupled receptor that binds the peptide hormone calcitonin and is involved in maintenance of calcium homeostasis, [5] particularly with respect to bone formation and metabolism. [6] [7] [8]

Contents

CT works by activating the G-proteins Gs and Gq often found on osteoclasts, on cells in the kidney, and on cells in a number of regions of the brain. [9] It may also affect the ovaries in women and the testes in men.

The function of the CT receptor protein is modified through its interaction with Receptor activity-modifying proteins (RAMPs), forming the multimeric amylin receptors AMY1 (CT + RAMP1), AMY2 (CT + RAMP2), and AMY3 (CT+ RAMP3). [10]

Preclinical studies have suggested that dual amylin and calcitonin receptor agonists may be more effective than amylin receptor agonists for obesity and type II diabetes. [11]

Interactions

Structure of human calcitonin recptor-Gs complex. The transmembrane calcitonin receptor (blue) is bound to human calcitonin (red) and the Gs complex (yellow). PDB: 7TYO Human calcitonin recptor-Gs complex PDB 7TYO.png
Structure of human calcitonin recptor-Gs complex. The transmembrane calcitonin receptor (blue) is bound to human calcitonin (red) and the Gs complex (yellow). PDB: 7TYO

Calcitonin receptor has been shown to interact with Apolipoprotein B [12] [13] and LRP1. [14]

Related Research Articles

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<span class="mw-page-title-main">Calcitonin</span> Amino acid peptide hormone secreted by the thyroid gland

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Calcitonin gene-related peptide (CGRP) is a member of the calcitonin family of peptides consisting of calcitonin, amylin, adrenomedullin, adrenomedullin 2 (intermedin) and calcitonin‑receptor‑stimulating peptide. Calcitonin is mainly produced by thyroid C cells whilst CGRP is secreted and stored in the nervous system. This peptide, in humans, exists in two forms: CGRP alpha, and CGRP beta. α-CGRP is a 37-amino acid neuropeptide and is formed by alternative splicing of the calcitonin/CGRP gene located on chromosome 11. β-CGRP is less studied. In humans, β-CGRP differs from α-CGRP by three amino acids and is encoded in a separate, nearby gene. The CGRP family includes calcitonin (CT), adrenomedullin (AM), and amylin (AMY).

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<span class="mw-page-title-main">RAMP1</span> Protein-coding gene in the species Homo sapiens

Receptor activity modifying protein 1 is a protein that in humans is encoded by the RAMP1 gene.

<span class="mw-page-title-main">RAMP2</span> Protein-coding gene in the species Homo sapiens

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References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000004948 Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000023964 Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Purdue BW, Tilakaratne N, Sexton PM (2002). "Molecular pharmacology of the calcitonin receptor". Receptors & Channels. 8 (3–4): 243–55. doi:10.1080/10606820213681. PMID   12529940.
  6. Chambers TJ, Magnus CJ (January 1982). "Calcitonin alters behaviour of isolated osteoclasts". The Journal of Pathology. 136 (1): 27–39. doi:10.1002/path.1711360104. PMID   7057295. S2CID   8395420.
  7. Dacquin R, Davey RA, Laplace C, Levasseur R, Morris HA, Goldring SR, Gebre-Medhin S, Galson DL, Zajac JD, Karsenty G (February 2004). "Amylin inhibits bone resorption while the calcitonin receptor controls bone formation in vivo". The Journal of Cell Biology. 164 (4): 509–14. doi:10.1083/jcb.200312135. PMC   2171986 . PMID   14970190.
  8. Davey RA, Turner AG, McManus JF, Chiu WS, Tjahyono F, Moore AJ, Atkins GJ, Anderson PH, Ma C, Glatt V, MacLean HE, Vincent C, Bouxsein M, Morris HA, Findlay DM, Zajac JD (August 2008). "Calcitonin receptor plays a physiological role to protect against hypercalcemia in mice". Journal of Bone and Mineral Research. 23 (8): 1182–93. doi:10.1359/jbmr.080310. PMC   2680171 . PMID   18627265.
  9. senselab Archived February 28, 2009, at the Wayback Machine
  10. "Calcitonin Receptors: Introduction". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. Archived from the original on 2016-03-03. Retrieved 2008-12-12.
  11. Sonne N, Karsdal MA, Henriksen K (1 April 2021). "Mono and dual agonists of the amylin, calcitonin, and CGRP receptors and their potential in metabolic diseases". Molecular Metabolism. 46: 101109. doi: 10.1016/j.molmet.2020.101109 . ISSN   2212-8778. PMC   8085567 . PMID   33166741.
  12. Zhang J, Herscovitz H (February 2003). "Nascent lipidated apolipoprotein B is transported to the Golgi as an incompletely folded intermediate as probed by its association with network of endoplasmic reticulum molecular chaperones, GRP94, ERp72, BiP, calreticulin, and cyclophilin B". The Journal of Biological Chemistry. 278 (9): 7459–68. doi: 10.1074/jbc.M207976200 . PMID   12397072.
  13. Linnik KM, Herscovitz H (August 1998). "Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state". The Journal of Biological Chemistry. 273 (33): 21368–73. doi: 10.1074/jbc.273.33.21368 . PMID   9694898.
  14. Orr AW, Pedraza CE, Pallero MA, Elzie CA, Goicoechea S, Strickland DK, Murphy-Ullrich JE (June 2003). "Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly". The Journal of Cell Biology. 161 (6): 1179–89. doi:10.1083/jcb.200302069. PMC   2172996 . PMID   12821648.

Further reading