Assignment of human 3-phosphoglycerate dehydrogenase (PHGDH) to human chromosome band 1p12 by fluorescence in situ hybridization.

Abstract

3-Phosphoglycerate dehydrogenase (PHGDH) catalyzes the transition of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the initiating and rate-limiting step in the phosphorylated pathway of serine biosynthesis. It has been suggested that an enhanced capacity of serine synthesis resulting from upregulation of the activity of PHGDH may confer a growthadvantage to tumor cells through its coupling to nucleotide biosynthesis (Snell et al., 1988). It has also been reported that the deficiency of human PHGDH activity can be a main cause for the inborn errors of serine biosynthesis, which result in a severe neurological syndrome and growth retardation (Jaeken et al., 1996). To elucidate the molecular basis for the changes of PHGDH activity directly associated with these human diseases, we have recently cloned and sequenced the human PHGDH gene (Cho et al., 1999). Here we report assignment of human PHGDH to human chromosome 1p12 by fluorescence in situ hybridization. Materials and methods