Human placental lactogen

"HPL" redirects here. For other uses, see HPL (disambiguation).

chorionic somatomammotropin hormone 1 (human placental lactogen)
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
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, is a polypeptide placental hormone. Its structure and function is similar to that 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 weight is 22,125 and contains one unique 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 biologic half-life is 15 minutes.

Function

In a bioassay HPL mimics the action of prolactin, yet it is unclear whether HPL has any role in human lactation.

HPL affects the metabolic system of the maternal organism. HPL decreases maternal insulin sensitivity, and, therefore, raises maternal blood glucose levels, whilst decreasing maternal glucose utilization, which helps ensure adequate fetal nutrition (the mother responds by pancreatic endocrine upregulation; this is thought to represent an evolutionary 'arms-race' resulting from the conflict of interest between mother and fetus). Chronic hypoglycemia leads to a rise in HPL. HPL induces 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 of HPL

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.

References

1. ^ ^{a b} 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. 
2. ^ Josimovich JB, Atwood BL, Goss DA (October 1963). "LLuteotrophic, Immunologic and Electrophoretic Properties of Human Placental Lactogen". Endocrinology 73: 410–20. doi:10.1210/endo-73-4-410. PMID 14068826. 
3. ^ Guyton and hall (2005) (in en). Textbook of Medical Physiology (11 ed.). Philadelphia: Saunders. pp. 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." 

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

• MeSH Human+Placental+Lactogen

• "RCSB Protein Data Bank - Structure Summary for 1Z7C - Crystal Structure of Human Placental Lactogen". http://www.rcsb.org/pdb/explore/explore.do?structureId=1Z7C. 

• "Human Chorionic Somatomammotropin Enhancer Function Is Mediated by Cooperative Binding of TEF-1 and CSEF-1 to Multiple, Low-Affinity Binding Sites". http://mend.endojournals.org/cgi/content/full/11/9/1223.