Human placental lactogen
chorionic somatomammotropin hormone 1 (human placental lactogen) | |
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Crystal Structure of Human Placental Lactogen.[1] | |
Identifiers | |
Symbol | CSH1 |
Entrez | 1442 |
HUGO | 2440 |
OMIM | 150200 |
RefSeq | NM_001317 |
UniProt | Q6PF11 |
Other data | |
Locus | Chr. 17 q22-q24 |
chorionic somatomammotropin hormone 2 | |
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Identifiers | |
Symbol | CSH2 |
Entrez | 1443 |
HUGO | 2441 |
OMIM | 118820 |
PDB | 1Z7C |
RefSeq | NM_020991 |
UniProt | P01243 |
Other data | |
Locus | Chr. 17 q22-q24 |
Human placental lactogen (hPL), also called human chorionic somatomammotropin (HCS), is a polypeptide placental hormone, the human form of placental lactogen (chorionic somatomammotropin). Its structure and function are similar to those of human growth hormone. It modifies the metabolic state of the mother during pregnancy to facilitate the energy supply of the fetus. hPL has anti-insulin properties. hPL is a hormone secreted by the syncytiotrophoblast during pregnancy. Like human growth hormone, hPL is encoded by genes on chromosome 17q22-24. It was identified in 1963.[2]
Structure
hPL molecular mass is 22,125 and contains single chain consisting of 191 amino acid residues that are linked by two disulfide bonds and the structure contains 8 helices. A crystal structure of hPL was determined by X-ray diffraction to a resolution of 2.0 Å.[1]
Levels
hPL is present only during pregnancy, with maternal serum levels rising in relation to the growth of the fetus and placenta. Maximum levels are reached near term, typically to 5–7 mg/L. Higher levels are noted in patients with multiple gestation. Little hPL enters the fetal circulation. Its biological half-life is 15 minutes.
Physiologic function
hPL affects the metabolic system of the maternal organism in the following manners:
- In a bioassay hPL mimics the action of prolactin, yet it is unclear whether hPL has any role in human lactation.
- Metabolic
- ↓ maternal insulin sensitivity leading to an increase in maternal blood glucose levels.
- ↓ maternal glucose utilization, which helps ensure adequate fetal nutrition (the mother responds by increasing beta cells). Chronic hypoglycemia leads to a rise in hPL.
- ↑ lipolysis with the release of free fatty acids. With fasting and release of hPL, free fatty acids become available for the maternal organism as fuel, so that relatively more glucose can be utilized by the fetus. Also, ketones formed from free fatty acids can cross the placenta and be used by the fetus.
These functions help support fetal nutrition even in the case of maternal malnutrition.
This hormone has weak actions similar to those of growth hormone, causing the formation of protein tissues in the same way that growth hormone, but 100 times more hPL than growth hormone is required to promote growth.[3] An enhancer for the human placental lactogen gene is found 2 kb downstream of the gene and participates in the cell-specific control gene expression.
Clinical measurement
While hPL has been used as an indicator of fetal well-being and growth, other fetal testing methods have been found to be more reliable. Also, normal pregnancies have been reported with undetectable maternal levels of hPL.
See also
- Placental lactogen in other species
- Somatotropin family
References
- 1 2 PDB: 1Z7C; Walsh ST, Kossiakoff AA (May 2006). "Crystal structure and site 1 binding energetics of human placental lactogen". J. Mol. Biol. 358 (3): 773–84. doi:10.1016/j.jmb.2006.02.038. PMID 16546209.
- ↑ Josimovich JB, Atwood BL, Goss DA (October 1963). "Luteotrophic, Immunologic and Electrophoretic Properties of Human Placental Lactogen". Endocrinology. 73: 410–20. doi:10.1210/endo-73-4-410. PMID 14068826.
- ↑ Guyton and Hall (2005). Textbook of Medical Physiology (11 ed.). Philadelphia: Saunders. p. 1033. ISBN 81-8147-920-3.
This hormone has weak actions similar to those of growth hormone, causing the formation of protein tissues in the same way that growth hormone.
- "RCSB Protein Data Bank - Structure Summary for 1Z7C - Crystal Structure of Human Placental Lactogen".
- "Human Chorionic Somatomammotropin Enhancer Function Is Mediated by Cooperative Binding of TEF-1 and CSEF-1 to Multiple, Low-Affinity Binding Sites".
Further reading
- Speroff L, Glass RH, Kase NG (1999). Clinical gynecologic endocrinology and infertility (Sixth ed.). Hagerstwon, MD: Lippincott Williams & Wilkins. ISBN 0-683-30379-1.
External links
- Human Placental Lactogen at the US National Library of Medicine Medical Subject Headings (MeSH)