Parathyroid hormone

Parathyroid hormone
PDB rendering based on 1bwx.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1BWX​, 1ET1​, 1ET2​, 1FVY​, 1HPH​, 1HPY​, 1HTH​, 1ZWA​, 1ZWB​, 1ZWD​, 1ZWE​, 1ZWF​, 1ZWG​, 2L1X​, 3C4M​
Identifiers
Symbols	PTH ; PTH1
External IDs	OMIM: 168450 MGI: 97799 HomoloGene: 266 GeneCards: PTH Gene
Gene ontology Molecular function • RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity • hormone activity • parathyroid hormone receptor binding • type 1 parathyroid hormone receptor binding • peptide hormone receptor binding Cellular component • extracellular region • extracellular space • intracellular Biological process • negative regulation of transcription from RNA polymerase II promoter • skeletal system development • cellular calcium ion homeostasis • G-protein coupled receptor signaling pathway • adenylate cyclase-activating G-protein coupled receptor signaling pathway • Rho protein signal transduction • cell-cell signaling • hormone-mediated apoptotic signaling pathway • positive regulation of signal transduction • response to lead ion • regulation of gene expression • positive regulation of bone mineralization • positive regulation of cAMP biosynthetic process • response to vitamin D • cellular macromolecule biosynthetic process • response to drug • bone resorption • response to ethanol • positive regulation of glycogen biosynthetic process • positive regulation of transcription from RNA polymerase II promoter • cAMP metabolic process • positive regulation of glucose import • response to cadmium ion • response to parathyroid hormone • response to fibroblast growth factor Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5741	19226
Ensembl	ENSG00000152266	ENSMUSG00000059077
UniProt	P01270	n/a
RefSeq (mRNA)	NM_000315	NM_020623
RefSeq (protein)	NP_000306	NP_065648
Location (UCSC)	Chr 11: 13.49 – 13.5 Mb	Chr 7: 113.39 – 113.39 Mb
PubMed search

Parathyroid hormone (PTH), parathormone or parathyrin, is secreted by the chief cells of the parathyroid glands as a polypeptide containing 84 amino acids, yet effective hormone-receptor interaction requires solely the 34-N-terminal amino acids. While PTH acts to increase the concentration of ionic calcium (Ca²⁺) in the blood, calcitonin, a hormone produced by the parafollicular cells (C cells) of the thyroid gland, acts to decrease ionic calcium concentration. PTH essentially acts to increase the concentration of calcium in the blood by acting upon the parathyroid hormone 1 receptor, which is present at high levels in bone and kidney, and the parathyroid hormone 2 receptor, which is present at high levels in the central nervous system, pancreas, testis, and placenta.^[1] PTH half-life is approximately 4 minutes.^[2] It has a molecular mass of approximately 9500 Da.^[3]

Structure

hPTH-(1-34) crystallizes as a slightly bent, long helical dimer. Analysis reveals that the extended helical conformation of hPTH-(1-34) is the likely bioactive conformation.^[4] The N-terminal fragment 1-34 of parathyroid hormone (PTH) has been crystallized and the structure has been refined to 0.9 Å resolution.

helical dimer structure of hPTH-(1-34)[5]

Function

Regulation of serum calcium

A diagrammatic representation of the movements of calcium ions into and out of the blood plasma (the central square labeled PLASMA Ca²⁺) in an adult in calcium balance. The widths of the red arrows indicating movement into and out of the plasma are roughly in proportion to the daily amounts of calcium moved in the indicated directions. The size of the central square in not in proportion to the size of the diagrammatic bone, which represents the calcium present in the skeleton, and contains approximately 25,000 mmol (or 1 kg) of calcium compared to the 9 mmol (360 mg) dissolved in the blood plasma. The differently colored narrow arrows indicate where the specified hormones act, and their effects (“+” means stimulates; “-“ means inhibits) when their plasma levels are high. PTH is parathyroid hormone, 1,25 OH VIT D₃ is calcitriol or 1,25 dihydroxyvitamin D₃, and CALCITONIN is a hormone secreted by the thyroid gland when the plasma ionized calcium level is high or rising. The diagram does not show the extremely small amounts of calcium that move into and out of the cells of the body, nor does it indicate the calcium that is bound to the extracellular proteins (in particular the plasma proteins) or to plasma phosphate.^{[6][7][8][9][10]}

Parathyroid hormone regulates serum calcium through its effects on bone, kidney, and the intestine:^[11]

In bone, PTH enhances the release of calcium from the large reservoir contained in the bones.^[12] Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL and inhibits their secretion of Osteoprotegerin (OPG). Free OPG competitively binds to RANKL as a decoy receptor, preventing RANKL from interacting with RANK, a receptor for RANKL. The binding of RANKL to RANK (facilitated by the decreased amount of OPG available for binding the excess RANKL) stimulates these osteoclast precursors to fuse, forming new osteoclasts, which ultimately enhances bone resorption.

In the kidney, approximately 250 mmol of calcium ions are filtered into the glomerular filtrate per day. Most of this (245 mmol/d) is reabsorbed from the tubular fluid, leaving about 5 mmol/d to be excreted in the urine. This reabsorption occurs throughout the tubule (most, 60-70%, of it in the proximal tubule), except in the thin segment of the loop of Henle.^[6] Circulating parathyroid hormone only influences the reabsorption that occurs in the distal tubules and the renal collecting ducts^[6] (but see Foot Note^{[nb 1]}). A more important effect of PTH on the kidney is, however, its inhibition of the reabsorption of phosphate (HPO₄^2-) from the tubular fluid, resulting in a decrease in the plasma phosphate concentration. Phosphate ions form water-insoluble salts with calcium. Thus, a decrease in the phosphate concentration of the blood plasma (for a given total calcium concentration) increases the amount of calcium that is ionized.^[15][16] A third important effect of PTH on the kidney is its stimulation of the conversion of 25-hydroxy vitamin D into 1,25-dihydroxy vitamin D (calcitriol), which is released into the circulation. This latter form of vitamin D is the active hormone which stimulates calcium uptake from the intestine.^[17]

In the intestine, via kidney, PTH enhances the absorption of calcium in the intestine by increasing the production of activated vitamin D. Vitamin D activation occurs in the kidney. PTH up-regulates 25-hydroxyvitamin D₃ 1-alpha-hydroxylase, the enzyme responsible for 1-alpha hydroxylation of 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D). This activated form of vitamin D increases the absorption of calcium (as Ca²⁺ ions) by the intestine via calbindin.

PTH was one of the first hormones to be shown to use the G-protein, adenylyl cyclase second messenger system.

Regulation of serum phosphate

PTH reduces the reabsorption of phosphate from the proximal tubule of the kidney,^[18] which means more phosphate is excreted through the urine.

However, PTH enhances the uptake of phosphate from the intestine and bones into the blood. In the bone, slightly more calcium than phosphate is released from the breakdown of bone. In the intestines, absorption of both calcium and phosphate is mediated by an increase in activated vitamin D. The absorption of phosphate is not as dependent on vitamin D as is that of calcium. The end result of PTH release is a small net drop in the serum concentration of phosphate.

Vitamin D synthesis

PTH increases the activity of 1-α-hydroxylase enzyme, which converts 25-hydroxycholecalciferol, the major circulating form of inactive vitamin D, into 1,25-dihydroxycholecalciferol, the active form of vitamin D, in the kidney.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^{[§ 1]}

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|{{{bSize}}}px|alt=Vitamin D Synthesis Pathway edit]]

Vitamin D Synthesis Pathway edit

1. The interactive pathway map can be edited at WikiPathways: "VitaminDSynthesis_WP1531".

Regulation of PTH secretion

Secretion of parathyroid hormone is determined chiefly by serum ionized calcium concentration through negative feedback. Calcium-sensing receptors located on parathyroid cells are activated when [Ca²⁺] is elevated. The G-protein coupled calcium receptors bind extracellular calcium and may be found on the surface on a wide variety of cells distributed in the brain, heart, skin, stomach, C cells, and other tissues. In the parathyroid gland, high concentrations of extracellular calcium result in activation of the Gq G-protein coupled cascade through the action of phospholipase C. This hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to liberate intracellular messengers IP3 and diacylglycerol (DAG). Ultimately, these two messengers result in a release of calcium from intracellular stores and a subsequent flux of extracellular calcium into the cytoplasmic space. The effect of this signaling of high extracellular calcium results in an intracellular calcium concentration that inhibits the secretion of preformed PTH from storage granules in the parathyroid gland. In contrast to the mechanism that most secretory cells use, calcium inhibits vesicle fusion and release of PTH.

In the parathyroids, magnesium serves this role in stimulus-secretion coupling. A mild decrease in serum magnesium levels stimulates the resorptive activity PTH has on the kidneys. Severe Hypomagnesemia inhibits PTH secretion and also causes resistance to PTH, leading to a form of hypoparathyroidism that is reversible.^[19]

Stimulators

• Decreased serum [Ca²⁺].
• Mild decreases in serum [Mg²⁺].
• An increase in serum phosphate (increased phosphate causes it to complex with serum calcium, forming calcium phosphate, which reduces stimulation of Ca-sensitive receptors (CaSr) that do not sense calcium phosphate, triggering an increase in PTH).

Inhibitors

• Increased serum [Ca²⁺].
• Severe decreases in serum [Mg²⁺], which also produces symptoms of hypoparathyroidism (such as hypocalcemia).^[20]
• Calcitriol

Clinical significance

Hyperparathyroidism, the presence of excessive amounts of parathyroid hormone in the blood, occurs in two very distinct sets of circumstances. Primary hyperparathyroidism is due to autonomous, abnormal hypersecretion of PTH from the parathyroid gland, while secondary hyperparathyroidism is an appropriately high PTH level seen as a physiological response to hypocalcaemia. A low level of PTH in the blood is known as hypoparathyroidism and is most commonly due to damage to or removal of parathyroid glands during thyroid surgery.

There are a number of rare but well-described genetic conditions affecting parathyroid hormone metabolism, including pseudohypoparathyroidism, familial hypocalciuric hypercalcaemia, and autosomal dominant hypercalciuric hypocalcaemia. In osteoporotic women, administration of an exogenous parathyroid hormone analogue (teriparatide, by daily injection) superimposed on estrogen therapy produced increases in bone mass and reduced vertebral and nonvertebral fractures by 45 to 65%.^[21]

Measurement

PTH can be measured in the blood in several different forms: intact PTH; N-terminal PTH; mid-molecule PTH, and C-terminal PTH, and different tests are used in different clinical situations.

The average PTH level is 8–51 pg/mL.^[22] Normal total plasma calcium level ranges from 8.5 to 10.2 mg/dL (2.12 mmol/L to 2.55 mmol/L).^[23]

Model organisms

Model organisms have been used in the study of PTH function. A conditional knockout mouse line called Pth^{tm1a(EUCOMM)Wtsi} was generated at the Wellcome Trust Sanger Institute.^[24] Male and female animals underwent a standardized phenotypic screen^[25] to determine the effects of deletion.^{[26][27][28][29]} Additional screens performed: - In-depth immunological phenotyping^[30]

Pth knockout mouse phenotype

Characteristic	Phenotype
All data available at.[25][30]
Insulin	Normal
Homozygous viability at P14	Normal
Homozygous Fertility	Normal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Abnormal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Salmonella infection	Normal

See also

• Calcium metabolism
• Disorders of calcium metabolism
• Parathyroid hormone family
• Parathyroid hormone-related protein

Foot note

1. This reduction in the rate of calcium excretion via the urine is a minor effect of high parathyroid hormone levels in the blood. The main determinant of the amount of calcium excreted into the urine per day is the plasma ionized calcium concentration itself. The plasma parathyroid hormone (PTH) concentration only increases or decreases the amount of calcium excreted at any specified plasma ionized calcium concentration. Thus, in primary hyperparathyroidism the quantity of calcium excreted in the urine per day is increased despite the high levels of PTH in the blood. This is because hyperparathyroidism results in hypercalcemia, which increases the urinary calcium concentration (hypercalcuria) despite the moderately increased rate of calcium re-absorption from the renal tubular fluid caused by PTH's direct effect on those tubules. Renal stones are therefore often a first indication of hyperparathyroidism, especially since the hypercalcuria is accompanied by an increase in urinary phosphate excretion (a direct result of the high plasma PTH levels). Together the calcium and phosphate tend to precipitate out as water-insoluble salts, which readily form solid “stones”.^[6][13][14]

References

1. Physiology: 5/5ch6/s5ch6_11 - Essentials of Human Physiology
2. Bieglmayer C, Prager G, Niederle B (Oct 2002). "Kinetic analyses of parathyroid hormone clearance as measured by three rapid immunoassays during parathyroidectomy". Clinical Chemistry 48 (10): 1731–8. PMID 12324490.
3. Brewer HB, Fairwell T, Ronan R, Sizemore GW, Arnaud CD (1972). "Human parathyroid hormone: amino-acid sequence of the amino-terminal residues 1-34". Proceedings of the National Academy of Sciences of the United States of America 69 (12): 3585–8. doi:10.1073/pnas.69.12.3585. PMC 389826. PMID 4509319.
4. Jin L, Briggs SL, Chandrasekhar S, Chirgadze NY, Clawson DK, Schevitz RW, Smiley DL, Tashjian AH, Zhang F (Sep 2000). "Crystal structure of human parathyroid hormone 1-34 at 0.9-A resolution". The Journal of Biological Chemistry 275 (35): 27238–44. doi:10.1074/jbc.M001134200. PMID 10837469.
5. PDB: 1ETE​; Savvides SN, Boone T, Andrew Karplus P (Jun 2000). "Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots". Nature Structural Biology 7 (6): 486–91. doi:10.1038/75896. PMID 10881197.
6. Blaine J, Chonchol M, Levi M (2015). "Renal control of calcium, phosphate, and magnesium homeostasis". Clinical Journal of the American Society of Nephrology 10 (7): 1257–72. doi:10.2215/CJN.09750913. PMID 25287933.
7. Brini M, Ottolini D, Calì T, Carafoli E (2013). "Chapter 4. Calcium in Health and Disease". In Sigel A, Helmut RK. Interrelations between Essential Metal Ions and Human Diseases. Metal Ions in Life Sciences 13. Springer. pp. 81–137. doi:10.1007/978-94-007-7500-8_4.
8. Walter F. (2003). "The Parathyroid Glands and Vitamin D in:". Medical Physiology: A Cellular And Molecular Approach. Elsevier/Saunders. p. 1094. ISBN 1-4160-2328-3.
9. Guyton A (1976). ‘’Medical Physiology’’. p.1062; New York,Saunders and Co.
10. Barrett KE, Barman SM, Boitano S, Brooks H, "Chapter 23. Hormonal Control of Calcium & Phosphate Metabolism & the Physiology of Bone" (Chapter). Barrett KE, Barman SM, Boitano S, Brooks H: Ganong's Review of Medical Physiology, 23e: http://www.accessmedicine.com/content.aspx?aID=5244785.
11. Coetzee M, Kruger MC (May 2004). "Osteoprotegerin-receptor activator of nuclear factor-kappaB ligand ratio: a new approach to osteoporosis treatment?". Southern Medical Journal 97 (5): 506–11. doi:10.1097/00007611-200405000-00018. PMID 15180028.
12. Poole KE, Reeve J (Dec 2005). "Parathyroid hormone - a bone anabolic and catabolic agent". Current Opinion in Pharmacology 5 (6): 612–7. doi:10.1016/j.coph.2005.07.004. PMID 16181808.
13. Harrison TR, Adams RD, Bennett IL, Resnick WH, Thorn GW, Wintrobe MM (1958). "Metabolic and Endocrine Disorders". Principles of Internal Medicine (Third ed.). New York: McGraw-Hill Book Company. pp. 575–578.
14. "Symptoms of Hyperparathyroidism and Symptoms of Parathyroid Disease.". Parathyroid.com. Norman Parathyroid Center. Retrieved 2015-12-30.
15. Haldimann B, Vogt K (1983). "[Hyperphosphatemia and tetany following phosphate enema]". Schweizerische Medizinische Wochenschrift (in French) 113 (35): 1231–3. PMID 6623048.
16. Sutters M, Gaboury CL, Bennett WM (1996). "Severe hyperphosphatemia and hypocalcemia: a dilemma in patient management". Journal of the American Society of Nephrology : JASN 7 (10): 2056–61. PMID 8915965.
17. Stryer L (1995). Biochemistry (Fourth ed.). New York: W.H. Freeman and Company. p. 707. ISBN 978-0-7167-2009-6.
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Further reading

• Drüeke TB, Massy ZA (2003). "Advanced oxidation protein products, parathyroid hormone and vascular calcification in uremia". Blood Purification 20 (5): 494–7. doi:10.1159/000065203. PMID 12207101.
• Parfitt AM (Oct 2002). "Parathyroid hormone and periosteal bone expansion". Journal of Bone and Mineral Research 17 (10): 1741–3. doi:10.1359/jbmr.2002.17.10.1741. PMID 12369776.
• Martin TJ (Mar 2004). "Does bone resorption inhibition affect the anabolic response to parathyroid hormone?". Trends in Endocrinology and Metabolism 15 (2): 49–50. doi:10.1016/j.tem.2004.01.002. PMID 15080150.
• Keutmann HT, Sauer MM, Hendy GN, O'Riordan LH, Potts JT (Dec 1978). "Complete amino acid sequence of human parathyroid hormone". Biochemistry 17 (26): 5723–9. doi:10.1021/bi00619a019. PMID 728431.
• Keutmann HT, Niall HD, O'Riordan JL, Potts JT (May 1975). "A reinvestigation of the amino-terminal sequence of human parathyroid hormone". Biochemistry 14 (9): 1842–7. doi:10.1021/bi00680a006. PMID 1125201.
• Parkinson DB, Thakker RV (May 1992). "A donor splice site mutation in the parathyroid hormone gene is associated with autosomal recessive hypoparathyroidism". Nature Genetics 1 (2): 149–52. doi:10.1038/ng0592-149. PMID 1302009.
• Handt O, Reis A, Schmidtke J (Nov 1992). "Ectopic transcription of the parathyroid hormone gene in lymphocytes, lymphoblastoid cells and tumour tissue". The Journal of Endocrinology 135 (2): 249–56. doi:10.1677/joe.0.1350249. PMID 1474331.
• Tonoki H, Narahara K, Matsumoto T, Niikawa N (1991). "Regional mapping of the parathyroid hormone gene (PTH) by cytogenetic and molecular studies". Cytogenetics and Cell Genetics 56 (2): 103–4. doi:10.1159/000133059. PMID 1672845.
• Marx UC, Adermann K, Bayer P, Meyer M, Forssmann WG, Rösch P (Feb 1998). "Structure-activity relation of NH2-terminal human parathyroid hormone fragments". The Journal of Biological Chemistry 273 (8): 4308–16. doi:10.1074/jbc.273.8.4308. PMID 9468478.
• Arnold A, Horst SA, Gardella TJ, Baba H, Levine MA, Kronenberg HM (Oct 1990). "Mutation of the signal peptide-encoding region of the preproparathyroid hormone gene in familial isolated hypoparathyroidism". The Journal of Clinical Investigation 86 (4): 1084–7. doi:10.1172/JCI114811. PMC 296835. PMID 2212001.
• Nussbaum SR, Gaz RD, Arnold A (Nov 1990). "Hypercalcemia and ectopic secretion of parathyroid hormone by an ovarian carcinoma with rearrangement of the gene for parathyroid hormone". The New England Journal of Medicine 323 (19): 1324–8. doi:10.1056/NEJM199011083231907. PMID 2215618.
• Ahn TG, Antonarakis SE, Kronenberg HM, Igarashi T, Levine MA (Mar 1986). "Familial isolated hypoparathyroidism: a molecular genetic analysis of 8 families with 23 affected persons". Medicine 65 (2): 73–81. doi:10.1097/00005792-198603000-00001. PMID 3005800.
• Tregear GW, van Rietschoten J, Greene E, Niall HD, Keutmann HT, Parsons JA, O'Riordan JL, Potts JT (Apr 1974). "Solid-phase synthesis of the biologically active N-terminal 1 - 34 peptide of human parathyroid hormone". Hoppe-Seyler's Zeitschrift für Physiologische Chemie 355 (4): 415–21. doi:10.1515/bchm2.1974.355.1.415. PMID 4474131.
• Niall HD, Sauer RT, Jacobs JW, Keutmann HT, Segre GV, O'Riordan JL, Aurbach GD, Potts JT (Feb 1974). "The amino-acid sequence of the amino-terminal 37 residues of human parathyroid hormone". Proceedings of the National Academy of Sciences of the United States of America 71 (2): 384–8. doi:10.1073/pnas.71.2.384. PMC 388010. PMID 4521809.
• Andreatta RH, Hartmann A, Jöhl A, Kamber B, Maier R, Riniker B, Rittel W, Sieber P (1973). "[Synthesis of sequence 1-34 of human parathyroid hormone]". Helvetica Chimica Acta 56 (1): 470–3. doi:10.1002/hlca.19730560139. PMID 4721748.
• Jacobs JW, Kemper B, Niall HD, Habener JF, Potts JT (May 1974). "Structural analysis of human proparathyroid hormone by a new microsequencing approach". Nature 249 (453): 155–7. doi:10.1038/249155a0. PMID 4833516.
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External links

• PTH at Lab Tests Online
• Parathyroid hormone: analyte monograph - the Association for Clinical Biochemistry and Laboratory Medicine
• Parathyroid Function Test Online