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Calcitonin

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CALCA
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCALCA, CT, CGRP-I, CGRP-alpha, KC, PCT, calcitonin related polypeptide alpha, CGRP, CGRP1, CALC1
External IDsOMIM: 114130; MGI: 2151253; HomoloGene: 88401; GeneCards: CALCA; OMA:CALCA - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001033952
NM_001033953
NM_001741
NM_001378949
NM_001378950

NM_001033954
NM_007587
NM_001289444
NM_001305616

RefSeq (protein)

NP_001029125.1

Location (UCSC)Chr 11: 14.97 – 14.97 MbChr 7: 114.23 – 114.24 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Calcitonin is a 32-amino acid polypeptide hormone that is produced in humans primarily by the parafollicular (also known as C-cells) of the thyroid, and in many other animals in the ultimobranchial body.[5] It acts to reduce blood calcium (Ca2+), opposing the effects of parathyroid hormone (PTH) [6]

It has been found in fish, reptiles, birds, and mammals. Its importance in humans has not been as well established as its importance in other animals.[7]

Biosynthesis

Calcitonin is formed by the proteolytic cleavage of a larger prepropeptide, which is the product of the CALC1 gene (CALCA). The CALC1 gene belongs to a superfamily of related protein hormone precursors including islet amyloid precursor protein, calcitonin gene-related peptide, and the precursor of adrenomedullin.

Physiology

The hormone participates in calcium (Ca2+) and phosphorus metabolism. In many ways, calcitonin has the counter effects of parathyroid hormone (PTH).

To be specific, calcitonin reduces blood Ca2+ levels in three ways:

Actions

Its actions, in a broad sense, are:

  • Bone mineral metabolism:
- Prevent postprandial hypercalcemia resulting from absorption of Ca2+ from foods during a meal
- Promote mineralization of skeletal bone
- Protect against Ca2+ loss from skeleton during periods of Ca2+ stress such as pregnancy and lactation
- Inhibit food intake in rats and monkeys
- May have CNS action involving the regulation of feeding and appetite

Receptor

The calcitonin receptor, found primarily on osteoclasts, is a G protein-coupled receptor, which is coupled by Gs to adenylyl cyclase and thereby to the generation of cAMP in target cells.

History

Calcitonin was purified in 1962 by Copp and Cheney.[11] While it was initially considered a secretion of the parathyroid glands, it was later identified as the secretion of the C-cells of the thyroid gland.

Pharmacology

Salmon calcitonin is used for the treatment of:

The following information is from the UK Electronic Medicines Compendium[13]

General characteristics of the active substance

Salmon calcitonin is rapidly absorbed and eliminated. Peak plasma concentrations are attained within the first hour of administration.

Animal studies have shown that calcitonin is primarily metabolised via proteolysis in the kidney following parenteral administration. The metabolites lack the specific biological activity of calcitonin. Bioavailability following subcutaneous and intramuscular injection in humans is high and similar for the two routes of administration (71% and 66%, respectively).

Calcitonin has short absorption and elimination half-lives of 10-15 minutes and 50-80 minutes, respectively. Salmon calcitonin is primarily and almost exclusively degraded in the kidneys, forming pharmacologically-inactive fragments of the molecule. Therefore, the metabolic clearance is much lower in patients with end-stage renal failure than in healthy subjects. However, the clinical relevance of this finding is not known. Plasma protein binding is 30% to 40%.

Characteristics in patients

There is a relationship between the subcutaneous dose of calcitonin and peak plasma concentrations. Following parenteral administration of 100 IU calcitonin, peak plasma concentration lies between about 200 and 400 pg/ml. Higher blood levels may be associated with increased incidence of nausea and vomiting.

Preclinical safety data

Conventional long-term toxicity, reproduction, mutagenicity, and carcinogenicity studies have been performed in laboratory animals. Salmon calcitonin is devoid of embryotoxic, teratogenic, and mutagenic potential.

An increased incidence of pituitary adenomas has been reported in rats given synthetic salmon calcitonin for 1 year. This is considered a species-specific effect and of no clinical relevance. Salmon calcitonin does not cross the placental barrier.

In lactating animals given calcitonin, suppression of milk production has been observed. Calcitonin is secreted into the milk.

Pharmaceutical manufacture

Calcitonin was extracted from the Ultimobranchial glands (thyroid-like glands) of fish, particularly salmon. Salmon calcitonin resembles human calcitonin, but is more active. At present, it is produced either by recombinant DNA technology or by chemical peptide synthesis. The pharmacological properties of the synthetic and recombinant peptides have been demonstrated to be qualitatively and quantitatively equivalent.[13]


Use of calcitonin in osteoarthritis

Oral calcitonin may have a chondroprotective role in osteoarthritis (OA), according to data in rats presented in December, 2005, at the 10th World Congress of the Osteoarthritis Research Society International (OARSI) in Boston, Massachusetts. Although calcitonin is an established antiresorptive agent, its disease-modifying effects on chondrocytes and cartilage metabolisms have not been well established until now.

This new study, however, may help to explain how calcitonin affects osteoarthritis. “Calcitonin acts both directly on osteoclasts, resulting in inhibition of bone resorption and following attenuation of subchondral bone turnover, and directly on chondrocytes, attenuating cartilage degradation and stimulating cartilage formation,” says researcher Morten Karsdal, MSC, PhD, of the department of pharmacology at Nordic Bioscience in Herlev, Denmark. “Therefore, calcitonin may be a future efficacious drug for OA.”[14]


See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000110680Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030669Ensembl, 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. ^ Sect. 5, Ch. 6: Anatomy, Structure, and Synthesis of Calcitonin (CT)
  6. ^ Medical Physiology, Boron & Boulpaep, ISBN 1-4160-2328-3, Elsevier Saunders 2005. Updated edition. Endocrine system chapter.
  7. ^ Sect. 5, Ch. 6: Biological Actions of CT
  8. ^ Sect. 5, Ch. 6: Effects of CT on the Small Intestine
  9. ^ Sect. 5, Ch. 6: Effects of CT on Bone
  10. ^ Sect. 5, Ch. 6: Effects of CT on Kidneys
  11. ^ Copp DH, Cheney B. Calcitonin-a hormone from the parathyroid, which lowers the calcium-level of the blood. Nature 1962;193:381-2. PMID 13881213
  12. ^ "Calcitonin in phantom limb pain": Ann Pharmacother. 1999 Apr;33(4):499-501 PMID: 10332543
  13. ^ a b http://emc.medicines.org.uk/ UK Electronic Medicines Compendium
  14. ^ Kleinman, Denise Mann (2006-01-04). "Oral Calcitonin May Delay Onset of Joint Disease and Relieve Pain of OA". Musculoskelital Report. Retrieved 2008-05-20.

Further reading