The relation between glucose utilization, lactic acid production and utilization and the growth cycle of L strain fibroblasts

Munyon, William; Merchant, Donald J.

doi:10.1016/0014-4827(59)90069-2

Cited by 76 publications

(38 citation statements)

References 12 publications

(1 reference statement)

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“…LM was derived from L929 by maintaining a serial subculture of L929 for 4 years in gradually decreasing amounts of serum and eventually replacing all serum with 0.5% Bacto-Peptone. LM has three chromosomes fewer than L929 (40). LM-TK-is a 5'-bromo-2-deoxyuridine-resistant subline of LM.…”

Section: Discussionmentioning

confidence: 99%

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Anchoring and degradation of glycolipid-anchored membrane proteins by L929 versus by LM-TK- mouse fibroblasts: implications for anchor biosynthesis.

Singh¹,

Singleton²,

Tartakoff³

1991

Mol. Cell. Biol.

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Although many cells anchor surface proteins via moieties that are sensitive to phosphatidylinositol-specific phospholipase C (PI-PLC), the anchor moieties of surface proteins of mouse L929 cells resist PI-PLC. By constructing stable hybrids between L929 and lymphoma cells that express glycolipid-anchored proteins in a PI-PLC-sensitive form, we show that PI-PLC resistance behaves as a recessive trait. Since putative mannolipid precursors of the lipid anchors bear alkali-labile substituents which make them resist PI-PLC, these observations are most simply interpreted by postulating that L929 lacks a critical anchor deacylase. Unlike the L929 cell line, two of its descendants, the LM cell line and its thymidine kinase-negative variant (LM-TK-), do not express glycolipid-anchored proteins on their surface. Moreover, unlike L929 cells, LM-TK-cells rapidly inactivate at least one lipid-anchored enzyme in a compartment sensitive to acidotropic amines and leupeptin. By fusion of LM-TK-cells to mouse Thy-l-lymphoma mutants and monitoring of surface expression of lipid-anchored proteins, we assign LM-TK-to lymphoma mutant complementation group H. This genetic assignment is matched by analysis of mannolipids of L929, LM-TK-, wild-type, and class H lymphoma mutant cells: striking similarities are seen between the two wild-type cells by contrast to the mutants. Since the differences pertain to lipids which have properties consistent with their being anchor precursors, we suggest that LM-TK-has a lesion in the synthesis of anchor precursor mannolipids.

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Section: Discussionmentioning

confidence: 99%

“…LM cells, on the other hand, were derived by a seemingly irrelevant selection for growth in serumless medium (40). One intriguing coincidence is that cell growth in serumless medium may require production of intracellular growth factors, some of which may resemble glycolipid anchor fragments (21,37,(48)(49)(50)62).…”

Section: Discussionmentioning

confidence: 99%

Anchoring and degradation of glycolipid-anchored membrane proteins by L929 versus by LM-TK- mouse fibroblasts: implications for anchor biosynthesis.

Singh¹,

Singleton²,

Tartakoff³

1991

Mol. Cell. Biol.

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“…Many non-transformed cells also exhibit high aerobic glycolysis during rapid proliferation. In proliferating mouse fibroblasts, the rate of glucose uptake and lactate production is highest during logarithmic growth (Munyon & Merchant 1959). Increased glucose uptake and lactate excretion has been observed in mitogen-stimulated normal human lymphocytes (Hedeskov 1968), mouse lymphocytes (Wang et al 1976), and rat thymocytes (Brand 1985, Hume et al 1978.…”

Section: Introductionmentioning

confidence: 99%

Aerobic Glycolysis: Meeting the Metabolic Requirements of Cell Proliferation

Lunt

Heiden

2011

Annu. Rev. Cell Dev. Biol.

2,476

2,296

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Warburg's observation that cancer cells exhibit a high rate of glycolysis even in the presence of oxygen (aerobic glycolysis) sparked debate over the role of glycolysis in normal and cancer cells. Although it has been established that defects in mitochondrial respiration are not the cause of cancer or aerobic glycolysis, the advantages of enhanced glycolysis in cancer remain controversial. Many cells ranging from microbes to lymphocytes use aerobic glycolysis during rapid proliferation, which suggests it may play a fundamental role in supporting cell growth. Here, we review how glycolysis contributes to the metabolic processes of dividing cells. We provide a detailed accounting of the biosynthetic requirements to construct a new cell and illustrate the importance of glycolysis in providing carbons to generate biomass. We argue that the major function of aerobic glycolysis is to maintain high levels of glycolytic intermediates to support anabolic reactions in cells, thus providing an explanation for why increased glucose metabolism is selected for in proliferating cells throughout nature.

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“…This is consistent with the demonstration by Clausen & 0vlisen (1965) of a difference in the extent of product inhibition by L-lactate on pyruvate reduction by the two tetramers H4 and M4. The rate of glycolysis in cultured cells is directly related to the composition of the medium (Munyon & Merchant, 1959). A high rate of glycolysis can be maintained by renewing the medium daily to maintain a high glucose concentration (Munyon & Merchant, 1959;Wilson, Jackson & Brues, 1942).…”

Section: Resultsmentioning

confidence: 99%

“…The rate of glycolysis in cultured cells is directly related to the composition of the medium (Munyon & Merchant, 1959). A high rate of glycolysis can be maintained by renewing the medium daily to maintain a high glucose concentration (Munyon & Merchant, 1959;Wilson, Jackson & Brues, 1942). This procedure results in a decrease in H subunit/M subunit ratio, whereas a tenfold decrease in the glucose concentration in the medium limited this decrease.…”

Section: Resultsmentioning

confidence: 99%

Factors affecting the lactate dehydrogenase isoenzyme pattern of cultured kidney-cortex cells

Güttler¹,

Clausen²

1969

Biochemical Journal

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1. The lactate dehydrogenase isoenzyme pattern of cultured calf kidney-cortex cells was correlated to growth phase, changes in oxygen supply, mean generation time and changes in nutritional supply. 2. During culture of free cells and intact explants the lactate dehydrogenase isoenzyme pattern changed towards a dominance of isoenzymes containing the M subunit. 3. Of the shift in monomer proportion, 58% occurred during the lag phase and 42% during the initial part of the exponential growth phase. During the stationary phase the shift in monomer proportion reversed slightly. It was possible to relate the observed shift in monomer proportion to the glycolytic rate. 4. Factors that depressed glycolysis decreased the shift in monomer proportion. Oxygen was found to limit the decrease in the Hsubunit/Msubunit ratio caused by anaerobic culture in vitro. 5. The results obtained support the view that the altered lactate dehydrogenase isoenzyme pattern of urine in renal ischaemia may be explained by anaerobic changes in the lactate dehydrogenase isoenzyme pattern of cortical tubule cells.

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The relation between glucose utilization, lactic acid production and utilization and the growth cycle of L strain fibroblasts

Cited by 76 publications

References 12 publications

Anchoring and degradation of glycolipid-anchored membrane proteins by L929 versus by LM-TK- mouse fibroblasts: implications for anchor biosynthesis.

Anchoring and degradation of glycolipid-anchored membrane proteins by L929 versus by LM-TK- mouse fibroblasts: implications for anchor biosynthesis.

Aerobic Glycolysis: Meeting the Metabolic Requirements of Cell Proliferation

Factors affecting the lactate dehydrogenase isoenzyme pattern of cultured kidney-cortex cells

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