Dependence of Collagen Synthesis by Embryonic Chick Tendon Cells on the Extracellular Concentrations of Glutamine

Lehtinen, Pirjo; Takala, I; Kulonen, E.

doi:10.3109/03008207809152625

Cited by 6 publications

(4 citation statements)

References 20 publications

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“…It is noteworthy that in an animal model of type 2 diabetes mellitus, troglitazone inhibits this thickening (26). We know that production of extracellular matrix proteins is glutamine dependent (2,10,24,34,37), and, therefore, troglitazone might act to halt matrix expansion at least in part through glutamine metabolism.…”

Section: Discussionmentioning

confidence: 99%

“…1. If glutamate undergoes transamination or conversion to proline, largely cytosolic reactions (2,25), then the amino nitrogen as well as carbon skeleton may be distributed into amino acids, which serve as building blocks for protein synthesis and particularly collagens, as in the case of glutamate conversion to proline (2,24). On the other hand, if glutamate is deaminated by GDH, a mitochondrial matrix space activity (35), then the amino nitrogen is released as ammonium, and the carbon skeleton, ␣-ketoglutarate, is oxidized and therefore would not contribute to biosynthetic processes.…”

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confidence: 99%

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Glitazones regulate glutamine metabolism by inducing a cellular acidosis in MDCK cells

Coates

Nissim

Battarbee

et al. 2002

American Journal of Physiology-Endocrinology and Metabolism

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-We studied the effect of the antihyperglycemic glitazones, ciglitazone, troglitazone, and rosiglitazone, on glutamine metabolism in renal tubule-derived Madin-Darby canine kidney (MDCK) cells. Troglitazone (25 M) enhanced glucose uptake and lactate production by 108 and 92% (both P Ͻ 0.001). Glutamine utilization was not inhibited, but alanine formation decreased and ammonium formation increased (both P Ͻ 0.005). The decrease in net alanine formation occurred with a change in alanine aminotransferase (ALT) reactants, from close to equilibrium to away from equilibrium, consistent with inhibition of ALT activity. A shift of glutamine's amino nitrogen from alanine into ammonium was confirmed by using L-[2-15 N]glutamine and measuring the [ 15 N]alanine and [15 N]ammonium production. The glitazone-induced shift from alanine to ammonium in glutamate metabolism was dose dependent, with troglitazone being twofold more potent than rosiglitazone and ciglitazone. All three glitazones induced a spontaneous cellular acidosis, reflecting impaired acid extrusion in responding to both an exogenous (NH 4 ϩ ) and an endogenous (lactic acid) load. Our findings are consistent with glitazones inducing a spontaneous cellular acidosis associated with a shift in glutamine amino nitrogen metabolism from predominantly anabolic into a catabolic pathway.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Glitazones regulate glutamine metabolism by inducing a cellular acidosis in MDCK cells

Coates

Nissim

Battarbee

et al. 2002

American Journal of Physiology-Endocrinology and Metabolism

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“…In addition, although the mechanism remains unclear, the importance of L-glutamine in protein synthesis and secretion has been demonstrated in several cell types. Collagen synthesis by chick tendon cells requires Lglutamine (Lehtinen et al, 1978). In rat pancreatic islet cells, L-glutamine markedly enhances insulin release (Malaisse et al, 1980).…”

Section: Discussionmentioning

confidence: 99%

The essential role of L‐glutamine in lymphocyte differentiation in vitro

Crawford

Cohen

1985

Journal Cellular Physiology

101

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The biochemistry of human B lymphocyte differentiation to plasma cells is incompletely understood. L-glutamine appears to be required for both lymphoblastic transformation and plasma cell formation in pokeweed-mitogen-stimulated human peripheral blood mononuclear cell cultures. Cells cultured with pokeweed mitogen in glutamine-deficient RPMI-1640 with 10% heat-inactivated and dialyzed fetal bovine serum were unable to incorporate 3H-thymidine or undergo morphologic lymphoblastic transformation assessed at 72 hours. However, 3H-thymidine incorporation could be maximally restored with as little as 0.08 mM L-glutamine or by using nondialyzed heat-inactivated fetal bovine serum, containing approximately. 1 mM L-glutamine. In subsequent cultures, using glutamine-deficient RPMI-1640 with 10% nondialyzed heat-inactivated fetal bovine serum, lymphoblastic transformation was equivalent with or without additional L-glutamine supplementation. However, only cultures with 2 mM L-glutamine supplementation underwent plasma cell differentiation as assessed by cytoplasmic staining with fluorescein-conjugated anti-immunoglobulin. When the kinetics of cellular immunoglobulin synthesis and secretion were analyzed by 3H- leucine incorporation into immunoglobulin, synthesis was 2-5 fold greater, and secretion 3-10-fold greater in cell cultures with 2 mM L-glutamine supplementation. By electron microscopy, only the glutamine-supplemented cells showed development of rough endoplasmic reticulum consistent with active immunoglobulin production. L-glutamine supplementation had no apparent effect on cell recovery, viability, % B cells, % T cells, % monocytes, or % helper and suppressor T cells. Thus, L-glutamine is essential for both lymphoblastic transformation and plasma cell differentiation. Future investigation of the selective nutritional requirements of cultured cells should yield further insights into the biochemical control of immune cell differentiation and function.

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“…A primary source of proline for collagen synthesis by fibroblasts in culture is glutamine, suggesting that glutamine metabolism could be an important pathway in fibroblasts (Bellon et al 1987, Lehtinen et al 1978. A recent study demonstrated that glutaminase expression was higher in CAFs than in cancer cells in pancreatic tumors and that the CAFs were more sensitive to glutamine withdrawal than cancer cells (Knudsen et al 2016).…”

Section: Fibroblast Metabolismmentioning

confidence: 99%

Metabolism in the Tumor Microenvironment

Lau

Heiden

2020

Annu. Rev. Cancer Biol.

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Experiments in culture systems where one cell type is provided with abundant nutrients and oxygen have been used to inform much of our understanding of cancer metabolism. However, many differences have been observed between the metabolism of tumors and the metabolism of cancer cells grown in monoculture. These differences reflect, at least in part, the presence of nonmalignant cells in the tumor microenvironment and the interactions between those cells and cancer cells. However, less is known about how the metabolism of various tumor stromal cell types differs from that of cancer cells, and how this difference might inform therapeutic targeting of metabolic pathways. Emerging data have identified both cooperative and competitive relationships between different cell types in a tumor, and this review examines how four abundant stromal cell types in the tumor microenvironment, fibroblasts, T cells, macrophages, and endothelial cells, contribute to the metabolism of tumors.

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Dependence of Collagen Synthesis by Embryonic Chick Tendon Cells on the Extracellular Concentrations of Glutamine

Cited by 6 publications

References 20 publications

Glitazones regulate glutamine metabolism by inducing a cellular acidosis in MDCK cells

Glitazones regulate glutamine metabolism by inducing a cellular acidosis in MDCK cells

The essential role of L‐glutamine in lymphocyte differentiation in vitro

Metabolism in the Tumor Microenvironment

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