Results 11 to 20 of about 94,706 (117)

The MDM2–p53–pyruvate carboxylase signalling axis couples mitochondrial metabolism to glucose-stimulated insulin secretion in pancreatic β-cells

Nature Communications, 2016
Mitochondrial metabolism is pivotal for glucose-stimulated insulin secretion (GSIS) in pancreatic β-cells. However, little is known about the molecular machinery that controls the homeostasis of intermediary metabolites in mitochondria. Here we show that
Xiaomu Li, K. Cheng, Zhuohao Liu, Jinkui Yang, Baile Wang, Xue Jiang, Yawen Zhou, P. Hallenborg, R. L. Hoo, K. Lam, Y. Ikeda, Xin Gao, A. Xu   +12 more
semanticscholar   +1 more source

Malonate as a ROS product is associated with pyruvate carboxylase activity in acute myeloid leukaemia cells

Cancer & Metabolism, 2016
BackgroundThe role of anaplerotic nutrient entry into the Krebs cycle via pyruvate carboxylase has been the subject of increased scrutiny and in particular whether this is dysregulated in cancer.
M. Reed, C. Ludwig, C. Bunce, F. Khanim, U. Günther   +4 more
semanticscholar   +1 more source

The Metabolic Fates of Pyruvate in Normal and Neoplastic Cells

Cells, 2021
Pyruvate occupies a central metabolic node by virtue of its position at the crossroads of glycolysis and the tricarboxylic acid (TCA) cycle and its production and fate being governed by numerous cell-intrinsic and extrinsic factors.
E. Prochownik, Huabo Wang
semanticscholar   +1 more source

Long Noncoding RNA GCASPC, a Target of miR-17-3p, Negatively Regulates Pyruvate Carboxylase-Dependent Cell Proliferation in Gallbladder Cancer.

Cancer Research, 2016
Long noncoding RNAs (lncRNA) are being implicated in the development of many cancers. Here, we report the discovery of a critical role for the lncRNA GCASPC in determining the progression of gallbladder cancer.
M. Ma, Yan Zhang, M. Weng, Shouhua Wang, Ye Hu, Z. Hou, Yiyu Qin, W. Gong, Yong-jie Zhang, X. Kong, Jian-dong Wang, Z. Quan   +11 more
semanticscholar   +1 more source

A distinct holoenzyme organization for two-subunit pyruvate carboxylase

Nature Communications, 2016
Pyruvate carboxylase (PC) has important roles in metabolism and is crucial for virulence for some pathogenic bacteria. PC contains biotin carboxylase (BC), carboxyltransferase (CT) and biotin carboxyl carrier protein (BCCP) components.
P. H. Choi, Jeanyoung K. Jo, Yu-Cheng Lin, Min-Han Lin, C. Chou, L. Dietrich, L. Tong   +6 more
semanticscholar   +1 more source

Pyruvate Carboxylase Is Up-Regulated in Breast Cancer and Essential to Support Growth and Invasion of MDA-MB-231 Cells

PLoS ONE, 2015
Pyruvate carboxylase (PC) is an anaplerotic enzyme that catalyzes the carboxylation of pyruvate to oxaloacetate, which is crucial for replenishing tricarboxylic acid cycle intermediates when they are used for biosynthetic purposes.
Phatchariya Phannasil, C. Thuwajit, M. Warnnissorn, J. Wallace, M. MacDonald, S. Jitrapakdee   +5 more
semanticscholar   +1 more source

Glioma Cells with the IDH1 Mutation Modulate Metabolic Fractional Flux through Pyruvate Carboxylase

PLoS ONE, 2014
Background Over 70% of low-grade gliomas carry a heterozygous R132H mutation in the gene coding for isocitrate dehydrogenase 1 (IDH1). This confers the enzyme with the novel ability to convert α-ketoglutarate to 2-hydroxyglutarate, ultimately leading to ...
J. L. Izquierdo-García, L. Cai, M. Chaumeil, P. Eriksson, Aaron E. Robinson, R. Pieper, J. Phillips, S. Ronen   +7 more
semanticscholar   +1 more source

Pyruvate Carboxylase Deficiency

, 2015
Clinical characteristics Pyruvate carboxylase (PC) deficiency is characterized in most affected individuals by failure to thrive, developmental delay, recurrent seizures, and metabolic acidosis.
Dong Wang, D. Vivo
semanticscholar   +1 more source

Targeting Pyruvate Carboxylase Reduces Gluconeogenesis and Adiposity and Improves Insulin Resistance

Diabetes, 2013
We measured the mRNA and protein expression of the key gluconeogenic enzymes in human liver biopsy specimens and found that only hepatic pyruvate carboxylase protein levels related strongly with glycemia.
N. Kumashiro, S. Beddow, D. Vatner, S. Majumdar, Jennifer L. Cantley, F. Guebre-egziabher, Ioana Fat, B. Guigni, M. Jurczak, A. Birkenfeld, M. Kahn, B. Perler, M. Puchowicz, Vara Prasad Manchem, S. Bhanot, C. Still, G. Gerhard, K. Petersen, G. Cline, G. Shulman, V. Samuel   +20 more
semanticscholar   +1 more source

A Substrate-induced Biotin Binding Pocket in the Carboxyltransferase Domain of Pyruvate Carboxylase*

Journal of Biological Chemistry, 2013
Background: Biotin-dependent enzymes efficiently coordinate multiple reactions in physically separate active sites. Results: Substrate binding remodels the carboxyltransferase active site to form a biotin binding pocket.
A. Lietzan, M. St. Maurice
semanticscholar   +1 more source