PMID: 8611185Feb 1, 1996Paper

Evidence for intracellular partitioning of serine and glycine metabolism in Chinese hamster ovary cells

The Biochemical Journal
M R NarkewiczP V Fennessey

Abstract

Serine hydroxymethyltransferase (SHMT) is the primary enzyme in the interconversion of serine and glycine. The roles of mitochondrial and cytosolic SHMT in the interconversion of serine and glycine were determined in two Chinese hamster ovary (CHO) cell lines that both contain cytosolic SHMT but either have (CHOm+) or lacK (CHOm-) mitochondrial SHMT. Mitochondrial SHMT activity was significantly reduced in CHOm- (0.24 +/- 0.11 nmol/min per mg of mitochondrial protein) compared with CHOm+ (3.21 +/- 0.66 nmol/min per mg of mitochondrial protein; P = 0.02) cells, whereas cytosolic SHMT activity was similar in CHOm- and CHOm+ cells (1.09 +/- 0.31 and 1.53 +/- 0.12 nmol/min per mg of cytosolic protein respectively; P = 0.57). In CHOm+ and CHOm- cells, the relative flux of glycine to serine measured with either [1-13C]- or [2-13C]-glycine was similar (CHOm-: 538 +/- 82 nmol/24 per mg of DNA; CHOm+: 616 +/- 88 nmol/24 h per mg of DNA; P = 0.42). In contrast, the relative flux of serine to glycine measured with [1-13C]serine was low in CHOm- cells (80 +/- 28 nmol/24 h per mg of DNA) compared with CHOm+ cells (3080 +/- 320 nmol/24 h per mg of DNA; P = 0.0001). The rate of glycine production determined by [1-(13)C]glycine dilution was lo...Continue Reading

Citations

Jun 25, 2013·Biotechnology and Bioengineering·Nuno CarinhasAna P Teixeira
Oct 23, 1998·The Journal of Urology·R P Holmes, D G Assimos
Dec 23, 1999·Molecular Genetics and Metabolism·M R NarkewiczF F Frerman
Apr 26, 2016·Nature Chemical Biology·Michael E PacoldDavid M Sabatini
Sep 24, 2010·Journal of Nucleic Acids·Claus DeslerLene Juel Rasmussen
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Sep 26, 2009·Reproduction : the Official Journal of the Society for the Study of Fertility·Hongling DuHugh S Taylor
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