Induction of 2,3-bisphosphoglycerate synthase in friend leukemia cells

Narita, Hiroshi; Yanagawa, Shin-ichi; Sasaki, Ryuzo; Chiba, Hideo

doi:10.1016/0006-291x(81)91664-8

Cited by 14 publications

(3 citation statements)

References 15 publications

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“…DPGM catalyzes the synthesis of 2,3-diphosphoglycerate (2,3-DPG), which controls the oxygen affinity of hemoglobin. DPGM activity has been shown to be increased by induced erythroid differentiation of Friend erythroleukemia cells 23,24) as well as CFUe isolated from murine spleens. 12) As shown in Table I, all examined Friend cells showed increased DPGM activity (up to 2-fold) when compared to uninduced cells on the 3rd day.…”

Section: Changes Of Pk Activity and Isozymes During Erythrodifferentimentioning

confidence: 99%

Apoptotic Changes Precede Mitochondrial Dysfunction in Red Cell‐type Pyruvate Kinase Mutant Mouse Erythroleukemia Cell Lines

Aisaki¹,

Kanno²,

Oyaizu³

et al. 1999

Japanese Journal of Cancer Research

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Section: Changes Of Pk Activity and Isozymes During Erythrodifferentimentioning

confidence: 99%

Apoptotic Changes Precede Mitochondrial Dysfunction in Red Cell‐type Pyruvate Kinase Mutant Mouse Erythroleukemia Cell Lines

Aisaki¹,

Kanno²,

Oyaizu³

et al. 1999

Japanese Journal of Cancer Research

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“…The most plausible phosphoryl donor is 2,3-BPG, which is made from 1,3-BPG by BPGM. However, BPGM protein expression has only been detected in erythrocytes 12 , 13 and placenta tissue 23 , which led us to investigate its levels in the HEK 293T cell line. We failed to detect BPGM protein in HEK 293T cells and the mRNA levels were found to be extremely low ( Supplementary Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The production of 2,3-BPG can occur through the activity of bisphosphoglycerate mutase (BPGM), which catalyzes the rearrangement of the glycolytic intermediate 1,3-BPG 11 . BPGM has a well-known role in red blood cells where it is highly expressed 12 , 13 and participates in the Luebering-Rapoport pathway that functions to generate high levels of 2,3-BPG for regulation of oxygen transport via direct binding to deoxyhemoglobin 14 , 15 . However, little is known about the importance of BPGM for maintaining PGAM1 activity and glycolytic flux.…”

Section: Introductionmentioning

confidence: 99%

Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate

Oslund

Haugbro

et al. 2017

Nat Chem Biol

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Lower glycolysis involves a series of reversible reactions, which interconvert intermediates that also feed anabolic pathways. 3-phosphoglycerate (3-PG) is an abundant lower glycolytic intermediate that feeds serine biosynthesis via the enzyme phosphoglycerate dehydrogenase, which is genomically amplified in several cancers. Phosphoglycerate mutase (PGAM1) catalyzes the isomerization of 3-PG into the downstream glycolytic intermediate 2-phosphoglycerate (2-PG). Catalytic activity of PGAM1 requires its histidine phosphorylation. We show that the primary PGAM1 histidine phosphate donor is 2,3-bisphosphoglycerate (2,3-BPG), which is made from the glycolytic intermediate 1,3-bisphosphoglycerate (1,3-BPG) by bisphosphoglycerate mutase (BPGM). When BPGM is knocked out, 1,3-BPG can directly phosphorylate PGAM1. In this case, PGAM1 phosphorylation and activity are decreased, but nevertheless sufficient to maintain normal glycolytic flux and cellular growth rate. 3-PG, however, accumulates, leading to increased serine synthesis. Thus, one biological function of BPGM is to control glycolytic intermediate levels and thereby serine biosynthetic flux.

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