Novel placental expression of 2,3-bisphosphoglycerate mutase
Pritlove, D. C., Gu, Mei, Boyd, C. A. R., Randeva, Harpal S. and Vatish, Manu. (2006) Novel placental expression of 2,3-bisphosphoglycerate mutase. Placenta, Vol.27 (No.8). pp. 924-927. ISSN 0143-4004Full text not available from this repository.
Official URL: http://dx.doi.org/10.1016/j.placenta.2005.08.010
2,3-Bisphosphoglycerate mutase (2,3-BPGM), an erythroid-expressed enzyme, synthesises 2,3-bisphosphoglycerate (2,3-BPG), the allosteric modulator of haemoglobin. This ligand has a higher affinity for adult haemoglobin than for fetal haemoglobin and differential binding of it facilitates transfer of oxygen between adult and fetal blood by lowering the affinity of adult haemoglobin for oxygen. This paper reports the discovery that 2,3-BPGM is synthesised in non-erythroid cells of the human placenta. Western blot analysis of placental extracts revealed high levels of 2,3-BPGM in the human placenta. Immunohistochemical staining and in situ hybridisation experiments indicated that abundant 2,3-BPGM is present in the syncytiotrophoblast layer of the placental villi at the feto-maternal interface. A cytochemical staining technique showed that the placental 2,3-BPGM is active, indicating that 2,3-BPG is synthesised in the outermost cells of the placenta. These observations demonstrate an unexpected and abundant presence of an enzyme key to oxygen release from adult haemoglobin, at the interface between maternal and fetal circulations.
|Item Type:||Journal Article|
|Subjects:||Q Science > QH Natural history > QH301 Biology
R Medicine > RG Gynecology and obstetrics
|Divisions:||Faculty of Medicine > Warwick Medical School > Translational & Systems Medicine > Reproductive Health
Faculty of Medicine > Warwick Medical School
|Journal or Publication Title:||Placenta|
|Official Date:||August 2006|
|Number of Pages:||4|
|Page Range:||pp. 924-927|
|Access rights to Published version:||Restricted or Subscription Access|
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