Cargando…

Serine one-carbon catabolism with formate overflow

Serine catabolism to glycine and a one-carbon unit has been linked to the anabolic requirements of proliferating mammalian cells. However, genome-scale modeling predicts a catabolic role with one-carbon release as formate. We experimentally prove that in cultured cancer cells and nontransformed fibr...

Descripción completa

Detalles Bibliográficos
Autores principales: Meiser, Johannes, Tumanov, Sergey, Maddocks, Oliver, Labuschagne, Christiaan Fred, Athineos, Dimitris, Van Den Broek, Niels, Mackay, Gillian M., Gottlieb, Eyal, Blyth, Karen, Vousden, Karen, Kamphorst, Jurre J., Vazquez, Alexei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5091358/
https://www.ncbi.nlm.nih.gov/pubmed/27819051
http://dx.doi.org/10.1126/sciadv.1601273
Descripción
Sumario:Serine catabolism to glycine and a one-carbon unit has been linked to the anabolic requirements of proliferating mammalian cells. However, genome-scale modeling predicts a catabolic role with one-carbon release as formate. We experimentally prove that in cultured cancer cells and nontransformed fibroblasts, most of the serine-derived one-carbon units are released from cells as formate, and that formate release is dependent on mitochondrial reverse 10-CHO-THF synthetase activity. We also show that in cancer cells, formate release is coupled to mitochondrial complex I activity, whereas in nontransformed fibroblasts, it is partially insensitive to inhibition of complex I activity. We demonstrate that in mice, about 50% of plasma formate is derived from serine and that serine starvation or complex I inhibition reduces formate synthesis in vivo. These observations transform our understanding of one-carbon metabolism and have implications for the treatment of diabetes and cancer with complex I inhibitors.