Low serine hydroxymethyltransferase activity in the human placenta has important implications for fetal glycine supply


Lewis, Rohan M., Godfrey, Keith M., Jackson, Alan A., Cameron, Iain T. and Hanson, Mark A. (2005) Low serine hydroxymethyltransferase activity in the human placenta has important implications for fetal glycine supply. Journal of Clinical Endocrinology and Metabolism, 90, (3), 1594-1598. (doi:10.1210/jc.2004-0317).

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Original Publication URL: http://dx.doi.org/10.1210/jc.2004-0317

Description/Abstract

Glycine is essential for fetal development, but in both sheep and human pregnancy, little is transported directly from the mother to the fetus, indicating that fetal glycine is derived from other sources. In the sheep, placental conversion of maternal serine by serine hydroxymethyltransferase (SHMT) provides almost all the glycine transported to the fetus. Although mRNA for mitochondrial and cytoplasmic SHMT has been detected in human placenta, it is not known whether substantial placental conversion of serine to glycine occurs in species other than sheep. We determined SHMT activity in human, rat, and sheep placenta by measuring conversion of [3-14C]serine to 14C-methylene tetrahydrofolate. Compared with term human placenta, SHMT activity per gram of placenta was 5.1-fold higher in term rat placenta and 24.1-fold higher in term sheep placenta. In sheep placenta, SHMT activity per gram of placenta increased 2.1-fold between mid-gestation and term. In human placenta, placental SHMT activity was similar 8 wk post conception and at term. The low activity of SHMT in the human and rat placenta suggests that, unlike in the sheep, placental conversion of serine to glycine is not a major source of fetal glycine in these species.

Item Type: Article
ISSNs: 0021-972X (print)
Related URLs:
Subjects: R Medicine > RG Gynecology and obstetrics
Q Science > QH Natural history > QH301 Biology
Divisions: University Structure - Pre August 2011 > School of Medicine > Developmental Origins of Health and Disease
ePrint ID: 25759
Date Deposited: 11 Apr 2006
Last Modified: 27 Mar 2014 18:14
Contact Email Address: rml2@soton.ac.uk.
URI: http://eprints.soton.ac.uk/id/eprint/25759

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