Synthesis of malate from phosphoenolpyruvate by rabbit liver mitochondria: implications for lipogenesis

Bd, Carlsen; Do, Lambeth; Pd, Ray

doi:10.1016/0304-4165(88)90143-2

Cited by 12 publications

(2 citation statements)

References 41 publications

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“…PCK2 expression and activity level are critical for many cancer types: in tumor-initiating enriched prostate cancer cell clones, PCK2 was overexpressed, and this correlated with more aggressive tumors and lower survival rates (Zhao et al, 2017); in lung cancer cell lines and in non-small cell lung cancer samples, PCK2 expression and activity were enhanced under low-glucose conditions (Leithner et al, 2015); finally, it was reported that PCK2 is required for glucose-independent cancer cell proliferation and tumor growth in vivo (Vincent et al, 2015). Regarding PCK2 reversibility, the enzyme has been shown to operate in the reaction toward OAA synthesis in mitochondria from rabbit liver (Carlsen et al, 1988), pigeon and rat liver (Wiese et al, 1996), guinea pig liver (Garber and Ballard, 1970;Garber and Salganicoff, 1973), rabbit enterocytes (Wuensch and Ray, 1997), chicken liver (Hebda and Nowak, 1982;Makinen and Nowak, 1983;Wilson et al, 1983;Erecinska and Wilson, 1984), and bullfrog liver (Goto et al, 1980). However, in Vincent et al (2015), it was shown that a fraction of pyruvate originated from glutamine from PEP through PCK2.…”

Section: Pathways Leading To Pyruvate Commencing From Glucose: Intermmentioning

confidence: 99%

From Glucose to Lactate and Transiting Intermediates Through Mitochondria, Bypassing Pyruvate Kinase: Considerations for Cells Exhibiting Dimeric PKM2 or Otherwise Inhibited Kinase Activity

Chinopoulos

2020

Front. Physiol.

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A metabolic hallmark of many cancers is the increase in glucose consumption coupled to excessive lactate production. Mindful that L-lactate originates only from pyruvate, the question arises as to how can this be sustained in those tissues where pyruvate kinase activity is reduced due to dimerization of PKM2 isoform or inhibited by oxidative/nitrosative stress, posttranslational modifications or mutations, all widely reported findings in the very same cells. Hereby 17 pathways connecting glucose to lactate bypassing pyruvate kinase are reviewed, some of which transit through the mitochondrial matrix. An additional 69 converging pathways leading to pyruvate and lactate, but not commencing from glucose, are also examined. The minor production of pyruvate and lactate by glutaminolysis is scrutinized separately. The present review aims to highlight the ways through which L-lactate can still be produced from pyruvate using carbon atoms originating from glucose or other substrates in cells with kinetically impaired pyruvate kinase and underscore the importance of mitochondria in cancer metabolism irrespective of oxidative phosphorylation.

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Section: Pathways Leading To Pyruvate Commencing From Glucose: Intermmentioning

confidence: 99%

From Glucose to Lactate and Transiting Intermediates Through Mitochondria, Bypassing Pyruvate Kinase: Considerations for Cells Exhibiting Dimeric PKM2 or Otherwise Inhibited Kinase Activity

Chinopoulos

2020

Front. Physiol.

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“…Although the bulk of work on this enzyme NOW is in the molecular biology area, a number of excellent recent, largely classical enzymological studies came to our attention (see, e.g. Carlsen et al 1988; Gallwitz et al 1988; Wiese et al 1991; Lambeth et al 1992; Hanson 2009). …”

Section: Phosphoenolpyruvate Carboxykinasementioning

confidence: 99%

A retrospective review of the roles of multifunctional glucose-6-phosphatase in blood glucose homeostasis: Genesis of the tuning/retuning hypothesis

Nordlie

Foster

2010

Life Sciences

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In a scientific career spanning from 1955-2000, my research focused on phosphoenolpyruvate carboxykinase and glucose-6-phosphatase. Grounded in basic enzymology, and initially pursuing the steady-state rate behavior of isolated preparations of these critically important gluconeogenic enzymes, our key findings were confirmed and extended by in situ enzyme rate experiments exploiting isolated liver perfusions. These efforts culminated in the discovery of the liver cytosolic isozyme of carboxykinase, known today as (GTP)PEPCK-C (EC4.1.1.32) and also revealed a biosynthetic function and multicomponent nature of glucose-6-phosphatase (EC3.1.3.9). Discovery that glucose-6-phosphatase possessed an intrinsically biosynthetic activity, now known as carbamyl-P:glucose phosphotransferase-along with a deeper consideration of the enzyme's hydrolytic activity as well as the action of liver glucokinase resulted in the evolution of Tuning/ Retuning Hypothesis for blood glucose homeostasis in health and disease. This THEN & NOW review shares with the reader the joy and exhilaration of major scientific discovery and also contrasts the methodologies and approaches on which I relied with those currently in use.

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Isocitrate dehydrogenases from liver ofSqualus acanthias (spiny dogfish) and citrate formation by isolated mitochondria

1996

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Synthesis of malate from phosphoenolpyruvate by rabbit liver mitochondria: implications for lipogenesis

Cited by 12 publications

References 41 publications

From Glucose to Lactate and Transiting Intermediates Through Mitochondria, Bypassing Pyruvate Kinase: Considerations for Cells Exhibiting Dimeric PKM2 or Otherwise Inhibited Kinase Activity

From Glucose to Lactate and Transiting Intermediates Through Mitochondria, Bypassing Pyruvate Kinase: Considerations for Cells Exhibiting Dimeric PKM2 or Otherwise Inhibited Kinase Activity

A retrospective review of the roles of multifunctional glucose-6-phosphatase in blood glucose homeostasis: Genesis of the tuning/retuning hypothesis

Isocitrate dehydrogenases from liver ofSqualus acanthias (spiny dogfish) and citrate formation by isolated mitochondria

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