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

Low serine hydroxymethyltransferase activity in the human placenta has important implications for fetal glycine supply
Low serine hydroxymethyltransferase activity in the human placenta has important implications for fetal glycine supply
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.
0021-972X
1594-1598
Lewis, Rohan M.
caaeb97d-ea69-4f7b-8adb-5fa25e2d3502
Godfrey, Keith M.
0931701e-fe2c-44b5-8f0d-ec5c7477a6fd
Jackson, Alan A.
c9a12d7c-b4d6-4c92-820e-890a688379ef
Cameron, Iain T.
f7595539-efa6-4687-b161-e1e93ff710f2
Hanson, Mark A.
1952fad1-abc7-4284-a0bc-a7eb31f70a3f
Lewis, Rohan M.
caaeb97d-ea69-4f7b-8adb-5fa25e2d3502
Godfrey, Keith M.
0931701e-fe2c-44b5-8f0d-ec5c7477a6fd
Jackson, Alan A.
c9a12d7c-b4d6-4c92-820e-890a688379ef
Cameron, Iain T.
f7595539-efa6-4687-b161-e1e93ff710f2
Hanson, Mark A.
1952fad1-abc7-4284-a0bc-a7eb31f70a3f

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 & Metabolism, 90 (3), 1594-1598. (doi:10.1210/jc.2004-0317).

Record type: Article

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.

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More information

Published date: March 2005

Identifiers

Local EPrints ID: 25759
URI: http://eprints.soton.ac.uk/id/eprint/25759
ISSN: 0021-972X
PURE UUID: ed101419-23f0-4c00-840e-b1b8f417c569
ORCID for Rohan M. Lewis: ORCID iD orcid.org/0000-0003-4044-9104
ORCID for Keith M. Godfrey: ORCID iD orcid.org/0000-0002-4643-0618
ORCID for Iain T. Cameron: ORCID iD orcid.org/0000-0002-4875-267X
ORCID for Mark A. Hanson: ORCID iD orcid.org/0000-0002-6907-613X

Catalogue record

Date deposited: 11 Apr 2006
Last modified: 16 Mar 2024 03:21

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