| Calcitonin-related polypeptide alpha |
NMR solution structure of salmon calcitonin in SDS micelles.[1] |
| Available structures |
| PDB |
Ortholog search: PDBe, RCSB |
| List of PDB id codes |
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1LS7, 2JXZ
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| Identifiers |
| Symbols |
CALCA ; CALC1; CGRP; CGRP-I; CGRP1; CT; KC |
| External IDs |
OMIM: 114130 MGI: 2151253 HomoloGene: 88401 ChEMBL: 5293 GeneCards: CALCA Gene |
| Gene ontology |
| Molecular function |
• receptor binding
• hormone activity
• protein binding
• calcitonin receptor binding
• protein complex binding
• identical protein binding
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| Cellular component |
• extracellular region
• extracellular space
• nucleus
• cytoplasm
• neuronal cell body
• terminal bouton
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| Biological process |
• endothelial cell proliferation
• vasculature development
• neurological system process involved in regulation of systemic arterial blood pressure
• vasodilation of artery involved in baroreceptor response to increased systemic arterial blood pressure
• regulation of heart rate
• G-protein coupled receptor internalization
• monocyte chemotaxis
• protein phosphorylation
• inflammatory response
• leukocyte cell-cell adhesion
• adenylate cyclase-activating G-protein coupled receptor signaling pathway
• activation of adenylate cyclase activity
• positive regulation of cytosolic calcium ion concentration
• neuropeptide signaling pathway
• cell-cell signaling
• embryo implantation
• aging
• feeding behavior
• regulation of blood pressure
• response to heat
• negative regulation of calcium ion transport into cytosol
• negative regulation of ossification
• positive regulation of cAMP biosynthetic process
• receptor internalization
• negative regulation of neurological system process
• activation of protein kinase activity
• positive regulation of interleukin-1 alpha production
• positive regulation of interleukin-8 production
• endothelial cell migration
• positive regulation of macrophage differentiation
• negative regulation of osteoclast differentiation
• positive regulation of adenylate cyclase activity
• negative regulation of blood pressure
• positive regulation of ossification
• negative regulation of bone resorption
• negative regulation of transcription, DNA-templated
• positive regulation of vasodilation
• negative regulation of smooth muscle contraction
• response to pain
• regulation of inflammatory response
• detection of temperature stimulus involved in sensory perception of pain
• cytosolic calcium ion homeostasis
• positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway
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| Sources: Amigo / QuickGO |
|
| RNA expression pattern |
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
|
| Entrez |
796 |
12310 |
|
| Ensembl |
ENSG00000110680 |
ENSMUSG00000030669 |
|
| UniProt |
P01258 |
P70160 |
|
| RefSeq (mRNA) |
NM_001033952 |
NM_001033954 |
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| RefSeq (protein) |
NP_001029124 |
NP_001029126 |
|
| Location (UCSC) |
Chr 11:
14.99 – 14.99 Mb |
Chr 7:
114.63 – 114.64 Mb |
|
| PubMed search |
[1] |
[2] |
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Calcitonin (also known as thyrocalcitonin) is a 32-amino acid linear polypeptide hormone that is produced in humans primarily by the parafollicular cells (also known as C-cells) of the thyroid, and in many other animals in the ultimobranchial body.[2] It acts to reduce blood calcium (Ca2+), opposing the effects of parathyroid hormone (PTH).[3]
Calcitonin 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, as its function is usually not significant in the regulation of normal calcium homeostasis.[4] It belongs to the calcitonin-like protein family.
Contents
- 1 Biosynthesis and regulation
- 2 Effects
- 3 Receptor
- 4 Discovery
- 5 Pharmacology
- 5.1 General characteristics of the active substance
- 5.2 Characteristics in patients
- 5.3 Preclinical safety data
- 6 Pharmaceutical manufacture
- 7 Uses of calcitonin
- 7.1 Treatments
- 7.2 Diagnostics
- 7.3 Structure
- 8 See also
- 9 References
- 10 Further reading
- 11 External links
Biosynthesis and regulation
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.
Secretion of calcitonin is stimulated by:
-
- an increase in serum [Ca2+][5]
- gastrin and pentagastrin.[6]
Effects
The hormone participates in calcium (Ca2+) and phosphorus metabolism. In many ways, calcitonin counteracts parathyroid hormone (PTH).
More specifically, calcitonin lowers blood Ca2+ levels in four ways:
-
- Inhibits Ca2+ absorption by the intestines[7]
- Inhibits osteoclast activity in bones[8]
- Stimulates osteoblastic activity in bones. [8]
- Inhibits renal tubular cell reabsorption of Ca2+ allowing it to be excreted in the urine[9][10]
However, effects of calcitonin that mirror those of PTH include the following:
-
- Inhibits phosphate reabsorption by the kidney tubules[11]
In its skeleton-preserving actions, calcitonin protects against calcium loss from skeleton during periods of calcium mobilization, such as pregnancy and, especially, lactation.
Other effects are in preventing postprandial hypercalcemia resulting from absorption of Ca2+. Also, calcitonin inhibits food intake in rats and monkeys, and may have CNS action involving the regulation of feeding and appetite.
Receptor
The calcitonin receptor, found on osteoclasts,[12] and in kidney and regions of the brain, is a G protein-coupled receptor, which is coupled by Gs to adenylate cyclase and thereby to the generation of cAMP in target cells. It may also affect the ovaries in women and the testes in men.
Discovery
Calcitonin was purified in 1962 by Copp and Cheney.[13] 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.[14]
Pharmacology
Salmon calcitonin is used for the treatment of:
- Postmenopausal osteoporosis
- Hypercalcaemia
- Paget's disease
- Bone metastases
- Phantom limb pain[15]
It has been investigated as a possible non-operative treatment for spinal stenosis.[16]
The following information is from the UK Electronic Medicines Compendium[17]
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, vomiting, and secretory diarrhea.
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.[citation needed] 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.[17]
Uses of calcitonin
Treatments
Calcitonin can be used therapeutically for the treatment of hypercalcemia or osteoporosis.
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 a known 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.”[18]
Subcutaneous injections of calcitonin in patients suffering from mania resulted in significant decreases in irritability, euphoria and hyperactivity and hence calcitonin holds promise for treating bipolar disorder.[19] However no further work on this potential application of calcitonin has been reported.
Diagnostics
It may be used diagnostically as a tumor marker for medullary thyroid cancer, in which high calcitonin levels may be present and elevated levels after surgery may indicate recurrence. It may even be used on biopsy samples from suspicious lesions (e.g., lymph nodes that are swollen) to establish whether they are metastasis of the original cancer.
Cutoffs for calcitonin to distinguish cases with medullary thyroid cancer have been suggested to be as follows, with a higher value increasing the suspicion of medullary thyroid cancer:[20]
- females: 5 ng/L or pg/mL
- males: 12 ng/L or pg/mL
- children under 6 months of age: 40 ng/L or pg/mL
- children between 6 months and 3 years of age: 15 ng/L or pg/mL
When over 3 years of age, adult cutoffs may be used
Increased levels of calcitonin have also been reported for various other conditions. They include: C-cell hyperplasia, Nonthyroidal oat cell carcinoma, Nonthyroidal small cell carcinoma and other nonthyroidal malignancies, acute and chronic renal failure, hypercalcemia, hypergastrinemia and other gastrointestinal disorders, and pulmonary disease.[21]
Structure
Calcitonin is a polypeptide hormone of 32 amino acids, with a molecular weight of 3454.93 daltons. Its structure comprises a single alpha helix.[1] Alternative splicing of the gene coding for calcitonin produces a distantly related peptide of 37 amino acids, called calcitonin gene-related peptide (CGRP), beta type.[22]
The following are the amino acid sequences of salmon and human calcitonin:[23]
Cys-Ser-Asn-Leu-Ser-Thr-Cys-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Thr-Gly-Ser-Gly-Thr-Pro
Cys-Gly-Asn-Leu-Ser-Thr-Cys-Met-Leu-Gly-Thr-Tyr-Thr-Gln-Asp-Phe-Asn-Lys-Phe-His-Thr-Phe-Pro-Gln-Thr-Ala-Ile-Gly-Val-Gly-Ala-Pro
Compared to salmon calcitonin, human calcitonin differs at 16 residues.
See also
References
- ^ a b PDB 2glhAndreotti G, Méndez BL, Amodeo P, Morelli MA, Nakamuta H, Motta A (August 2006). "Structural determinants of salmon calcitonin bioactivity: the role of the Leu-based amphipathic alpha-helix". J. Biol. Chem. 281 (34): 24193–203. doi:10.1074/jbc.M603528200. PMID 16766525.
- ^ Costoff A. "Sect. 5, Ch. 6: Anatomy, Structure, and Synthesis of Calcitonin (CT)". Endocrinology: hormonal control of calcium and phosphate. Medical College of Georgia. Retrieved 2008-08-07.
- ^ Boron WF, Boulpaep EL (2004). "Endocrine system chapter". Medical Physiology: A Cellular And Molecular Approach. Elsevier/Saunders. ISBN 1-4160-2328-3.
- ^ Costoff A. "Sect. 5, Ch. 6: Biological Actions of CT". Medical College of Georgia. Retrieved 2008-08-07.
- ^ Costanzo, Linda S. (2007). BRS Physiology. Lippincott, Williams, & Wilkins. p. 263. ISBN 978-0-7817-7311-9.
- ^ Erdogan MF, Gursoy A, Kulaksizoglu M (October 2006). "Long-term effects of elevated gastrin levels on calcitonin secretion". J Endocrinol Invest. 29 (9): 771–775. PMID 17114906.
- ^ Costoff A. "Sect. 5, Ch. 6: Effects of CT on the Small Intestine". Medical College of Georgia. Retrieved 2008-08-07. [dead link]
- ^ a b Costoff A. "Sect. 5, Ch. 6: Effects of CT on Bone". Medical College of Georgia. Retrieved 2008-08-07.
- ^ Potts, John; Jüppner, Harald (2008). "Chapter 353. Disorders of the Parathyroid Gland and Calcium Homeostasis". In Dan L. Longo, Dennis L. Kasper, J. Larry Jameson, Anthony S. Fauci, Stephen L. Hauser, and Joseph Loscalzo. Harrison's Principles of Internal Medicine (18 ed.). McGraw-Hill.
- ^ Rhoades, Rodney (2009). Medical Physiology: Principles for Clinical Medicine. Philadelphia: Lippincott Williams & Wilkins. ISBN 978-0-7817-6852-8.
- ^ Carney SL (1997). "Calcitonin and human renal calcium and electrolyte transport". Miner Electrolyte Metab 23 (1): 43–7. PMID 9058369.
- ^ Nicholson GC, Moseley JM, Sexton PM, et al (1986). "Abundant calcitonin receptors in isolated rat osteoclasts. Biochemical and autoradiographic characterization". J Clin Invest 78 (2): 355–60. doi:10.1172/JCI112584. PMC 423551. PMID 3016026.
- ^ Copp DH, Cheney B (January 1962). "Calcitonin-a hormone from the parathyroid which lowers the calcium-level of the blood". Nature 193 (4813): 381–2. doi:10.1038/193381a0. PMID 13881213.
- ^ Hirsch PF, Gauthier GF, Munson PL (August 1963). "Thyroid hypocalcemic principle and recurrent laryngeal nerve injury as factors affecting the response to parathyroidectomy in rats". Endocrinology 73 (2): 244–252. doi:10.1210/endo-73-2-244. PMID 14076205.
- ^ Wall GC, Heyneman CA (April 1999). "Calcitonin in phantom limb pain". Ann Pharmacother 33 (4): 499–501. doi:10.1345/aph.18204. PMID 10332543.
- ^ Tran de QH, Duong S, Finlayson RJ (July 2010). "Lumbar spinal stenosis: a brief review of the nonsurgical management". Can J Anaesth 57 (7): 694–703. doi:10.1007/s12630-010-9315-3. PMID 20428988.
- ^ a b "Electronic Medicines Compendium". Retrieved 2008-08-07.
- ^ Kleinman DM (2006-01-04). "Oral Calcitonin May Delay Onset of Joint Disease and Relieve Pain of OA". Musculoskeletal Report. Musculoskeletal Report, LLC. Retrieved 2008-08-07.
- ^ Vik A, Yatham LN (March 1998). "Calcitonin and bipolar disorder: a hypothesis revisited". J Psychiatry Neurosci 23 (2): 109–17. PMC 1188909. PMID 9549251.
- ^ Basuyau, J. -P.; Mallet, E.; Leroy, M.; Brunelle, P. (2004). "Reference Intervals for Serum Calcitonin in Men, Women, and Children". Clinical Chemistry 50 (10): 1828–1830. doi:10.1373/clinchem.2003.026963. PMID 15388660. edit
- ^ Burtis CA, Ashwood ER, Bruns DE. Tietz Textbook of Clinical Chemistry and Molecular Diagnostics, 5th edition. Elsevier Saunders. p. 1774. ISBN 978-1-4160-6164-9.
- ^ "calcitonin domain annotation". SMART (a Simple Modular Architecture Research Tool). embl-heidelberg.de. Retrieved 2009-02-22.
- ^ http://www.newworldencyclopedia.org/entry/Calcitonin
Further reading
- MacIntyre I, Alevizaki M, Bevis PJ, Zaidi M (1987). "Calcitonin and the peptides from the calcitonin gene". Clin. Orthop. Relat. Res. &na; (217): 45–55. doi:10.1097/00003086-198704000-00007. PMID 3549095.
- Di Angelantonio S, Giniatullin R, Costa V, et al. (2004). "Modulation of neuronal nicotinic receptor function by the neuropeptides CGRP and substance P on autonomic nerve cells". Br. J. Pharmacol. 139 (6): 1061–73. doi:10.1038/sj.bjp.0705337. PMC 1573932. PMID 12871824.
- Findlay DM, Sexton PM (2005). "Calcitonin". Growth Factors 22 (4): 217–24. doi:10.1080/08977190410001728033. PMID 15621724.
- Sponholz C, Sakr Y, Reinhart K, Brunkhorst F (2007). "Diagnostic value and prognostic implications of serum procalcitonin after cardiac surgery: a systematic review of the literature". Critical care (London, England) 10 (5): R145. doi:10.1186/cc5067. PMC 1751067. PMID 17038199.
- Schneider HG, Lam QT (2007). "Procalcitonin for the clinical laboratory: a review". Pathology 39 (4): 383–90. doi:10.1080/00313020701444564. PMID 17676478.
- Grani, G; Nesca, A; Del Sordo, M; Calvanese, A; Carbotta, G; Bianchini, M; Fumarola, A (Jun 2012). "Interpretation of serum calcitonin in patients with chronic autoimmune thyroiditis.". Endocrine-related cancer 19 (3): 345–9. doi:10.1530/ERC-12-0013. PMID 22399011.
External links
- The Calcitonin Protein
- Calcitonin at the US National Library of Medicine Medical Subject Headings (MeSH)
- Endocrine system:
- hormones
- Peptide hormones
- Steroid hormones
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Endocrine
glands |
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Hypothalamic-
pituitary
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Hypothalamus
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- GnRH
- TRH
- Dopamine
- CRH
- GHRH/Somatostatin
- Melanin concentrating hormone
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Posterior pituitary
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Anterior pituitary
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- α
- FSH
- FSHB
- LH
- LHB
- TSH
- TSHB
- CGA
- Prolactin
- POMC
- CLIP
- ACTH
- MSH
- Endorphins
- Lipotropin
- GH
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Adrenal axis
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Adrenal cortex:
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- aldosterone
- cortisol
- DHEA
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Adrenal medulla:
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- epinephrine
- norepinephrine
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Thyroid axis
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Thyroid:
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- thyroid hormone
- calcitonin
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Parathyroid:
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Gonadal axis
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Testis::
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Ovary:
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- estradiol
- progesterone
- activin and inhibin
- relaxin (pregnancy)
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Placenta:
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- hCG
- HPL
- estrogen
- progesterone
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Islet–acinar
axis
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Pancreas:
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- glucagon
- insulin
- amylin
- somatostatin
- pancreatic polypeptide
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Pineal gland
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Other
glands |
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Thymus:
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- Thymosins
- Thymosin α1
- Beta thymosins
- Thymopoietin
- Thymulin
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Digestive system:
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Stomach:
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Duodenum:
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- CCK
- Incretins
- secretin
- motilin
- VIP
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Ileum:
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- enteroglucagon
- peptide YY
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Liver/other
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- Insulin-like growth factor
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Adipose tissue:
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- leptin
- adiponectin
- resistin
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Skeleton::
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Kidney:
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- JGA (renin)
- peritubular cells
- calcitriol
- prostaglandin
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Heart:
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| Description |
- Glands
- Hormones
- Physiology
- Development
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| Disease |
- Diabetes
- Congenital
- Neoplasms and cancer
- Other
- Symptoms and signs
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| Treatment |
- Procedures
- Drugs
- calcium balance
- corticosteroids
- oral hypoglycemics
- pituitary and hypothalamic
- thyroid
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Peptides: neuropeptides
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| Hormones |
see hormones
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| Opioid peptides |
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Dynorphins
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- Big dynorphin
- Dynorphin A
- Dynorphin B
- Leumorphin
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Endomorphins
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- Endomorphin-1
- Endomorphin-2
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Endorphins
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- α-Endorphin
- β-Endorphin
- γ-Endorphin
- α-Neoendorphin
- β-Neoendorphin
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Enkephalins
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- Met-enkephalin
- Leu-enkephalin
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Others
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- Adrenorphin
- Amidorphin
- Hemorphin
- Nociceptin
- Opiorphin
- Spinorphin
- Valorphin
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Other
neuropeptides |
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Kinins
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- Tachykinins: mammal
- Substance P
- Neurokinin A
- Neurokinin B
- amphibian
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Neuromedins
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Other
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- Angiotensin
- Bombesin
- Calcitonin gene-related peptide
- Carnosine
- Cocaine and amphetamine regulated transcript
- Delta sleep-inducing peptide
- FMRFamide
- Galanin
- Galanin-like peptide
- Gastrin releasing peptide
- Ghrelin
- Neuropeptide S
- Neuropeptide Y
- Neurophysins
- Neurotensin
- Pancreatic polypeptide
- Pituitary adenylate cyclase activating peptide
- RVD-Hpα
- VGF
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B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
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Neurotransmitters
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| Amino acid-derived |
- Major excitatory/inhibitory systems: Glutamate system: Agmatine
- Aspartic acid (aspartate)
- Cycloserine
- Glutamic acid (glutamate)
- Glycine
- Kynurenic acid
- NAA
- NAAG
- Serine; GABA system: GABA
- GABOB
- Proline; Glycine system: β-Alanine
- Alanine
- Glycine
- Hypotaurine
- Proline
- Sarcosine
- Serine
- Taurine; GHB system: GHB
- T-HCA
- Biogenic amines: Monoamines: Dopamine
- Epinephrine (adrenaline)
- Histamine
- Melatonin
- NAS (normelatonin)
- Norepinephrine (noradrenaline)
- Serotonin (5-HT); Trace amines:
- 3-Iodothyronamine
- N-Methylphenethylamine
- N-Methyltryptamine
- m-Octopamine
- p-Octopamine
- Phenylethanolamine
- Phenethylamine
- Synephrine
- Tryptamine
- m-Tyramine
- p-Tyramine
- Neuropeptides: See here instead.
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| Lipid-derived |
- Endocannabinoids: 2-AG
- 2-AGE (noladin ether)
- 2-OG
- AA-5-HT
- Anandamide (AEA)
- DEA
- LPI
- NADA
- NAGly
- OEA
- Oleamide
- PEA
- SEA
- Virodhamine (OAE)
- Neurosteroids: See here instead.
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| Nucleobase-derived |
- Nucleosides: Adenosine system: Adenosine
- ADP
- AMP
- ATP
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| Vitamin-derived |
- Cholinergic system: Acetylcholine
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| Miscellaneous |
- Gasotransmitters: Carbon monoxide (CO)
- Hydrogen sulfide (H2S)
- Nitrous oxide (NO); Candidates: Acetaldehyde
- Ammonia (NH3)
- Carbonyl sulfide (COS)
- Nitrous oxide (N2O)
- Sulfur dioxide (SO2)
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Index of the peripheral nervous system
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| Description |
- Anatomy
- Nerves
- cranial
- trigeminal
- cervical
- brachial
- lumbosacral plexus
- somatosensory
- spinal
- autonomic
- Physiology
- reflexes
- proteins
- neurotransmitters
- transporters
- Development
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| Disease |
- Autonomic
- Congenital
- Injury
- Neoplasms and cancer
- Other
- Symptoms and signs
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| Treatment |
- Procedures
- Local anesthetics
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Tumor markers
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| Blood |
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| Endocrine |
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Thyroid cancer
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- Thyroglobulin
- Medullary thyroid cancer (Calcitonin
- Carcinoembryonic antigen)
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Pheochromocytoma
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- Normetanephrine
- Enolase 2
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Neuroendocrine tumors
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- Synaptophysin
- Chromogranin A
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Neuroblastoma
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| Nervous system |
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Brain tumor
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Astrocytoma
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- Glial fibrillary acidic protein
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NC/Melanoma
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- S-100 protein
- Melanoma inhibitory activity
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Cardiovascular/
respiratory |
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Lung cancer
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- Carcinoembryonic antigen
- Enolase 2
- Autocrine motility factor
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Hemangiosarcoma (endothelium)
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| Digestive |
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Colorectal cancer
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- CA19-9
- Carcinoembryonic antigen
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Pancreatic cancer
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- CA19-9
- Carcinoembryonic antigen
- CA 242
- Tumor-associated glycoprotein 72
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Hepatocellular carcinoma
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Reproductive/
urinary/
breast |
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Ovarian tumor
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- Surface epithelial-stromal tumor
- EC
- EST
- Choriocarcinoma
- Dysgerminoma
- Sertoli-Leydig cell tumour
- GCT
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Testicular cancer
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- βhCG
- Alpha-fetoprotein/AFP-L3
- CD30
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Prostate cancer
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- Prostate specific antigen
- Prostatic acid phosphatase
- Glutamate carboxypeptidase II
- erbB-3 receptor
- Early prostate cancer antigen-2
- SPINK1
- GOLPH2
- PCA3
- TMPRSS2
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Germ cell tumor
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Bladder cancer
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Breast cancer
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- CA 15-3
- erbB-2 receptor
- erbB-3 receptor
- Cathepsin D
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| General histology |
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Sarcoma
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Carcinoma (epithelium)
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| Musculoskeletal |
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| Description |
- Tumor suppressing and oncogenes
- Tumor markers
|
|
| Disease |
- Neoplasms and cancer
- Symptoms and signs
- Paraneoplastic
|
|
| Treatment |
- Drugs
- intracellular chemotherapeutics
- extracellular chemotherapeutics
- adjuvant detoxification
|
|
|
|
Metabolic disease: amyloidosis (E85, 277.3)
|
|
| Common amyloid forming proteins |
- AA
- ATTR
- Aβ2M
- AL
- Aβ/APP
- AIAPP
- ACal
- APro
- AANF
- ACys
- ABri
|
|
| Systemic amyloidosis |
- AL amyloidosis
- AA amyloidosis
- Aβ2M/Haemodialysis-associated
- AGel/Finnish type
- AA/Familial Mediterranean fever
- ATTR/Transthyretin-related hereditary
|
|
| Organ-limited amyloidosis |
|
Heart
|
AANF/Isolated atrial
|
|
|
Brain
|
- Familial amyloid neuropathy
- ACys+ABri/Cerebral amyloid angiopathy
- Aβ/Alzheimer's disease
|
|
|
Kidney
|
- AApoA1+AFib+ALys/Familial renal
|
|
|
Cutaneous
|
- Primary cutaneous amyloidosis
- Amyloid purpura
|
|
|
Endocrine
|
- Thyroid
- ACal/Medullary thyroid cancer
- Pituitary
- APro/Prolactinoma
- Pancreas
- AIAPP/Insulinoma
- AIAPP/Diabetes mellitus type 2
|
|
|
