نتایج جستجو برای: pyruvate kinase

تعداد نتایج: 238659  

Journal: :Circulation 2011
Helen J Atherton Michael S Dodd Lisa C Heather Marie A Schroeder Julian L Griffin George K Radda Kieran Clarke Damian J Tyler

BACKGROUND Hyperthyroidism increases heart rate, contractility, cardiac output, and metabolic rate. It is also accompanied by alterations in the regulation of cardiac substrate use. Specifically, hyperthyroidism increases the ex vivo activity of pyruvate dehydrogenase kinase, thereby inhibiting glucose oxidation via pyruvate dehydrogenase. Cardiac hypertrophy is another effect of hyperthyroidis...

Journal: :The Journal of biological chemistry 1960
I A ROSE

Unlike the usual “kinase” reaction between ATP and an alcohol, pyruvate kinase catalyzes phosphate transfer to an oxygen which in the substrate, pyruvate, is in carbonyl linkage. It is of particular interest to ask whether enolization of pyruvate occurs sufficiently rapidly under physiological conditions so that the true substrate for the enzyme may be the enol form of pyruvate. In the work rep...

Journal: :The Journal of biological chemistry 1985
J M Van Divender C M Grisham

The interactions between ATP, monovalent cations, and divalent cations on rabbit muscle pyruvate kinase have been examined using 7Li, 31P, and 1H nuclear magnetic resonance. Water proton nuclear relaxation studies are consistent with the binding of Li+ to the K+ site on pyruvate kinase with an affinity of 120 mM in the absence of substrates and 16 mM in the presence of P-enolpyruvate. Titration...

Journal: :Bioscience reports 1986
M Devchand M Kapoor

In Neurospora crassa, there is a single pyruvate kinase (PK) consisting of four identical subunits of approximately 60k daltons. Northern and dot blot hybridization studies, using most of the yeast pyruvate kinase gene as a probe, suggest the presence of two distinct mRNA species for pyruvate kinase, separable on the basis of the length of their polyadenylated tails, by oligo(dT)cellulose chrom...

Journal: :Cell 2013
William J. Israelsen Talya L. Dayton Shawn M. Davidson Brian P. Fiske Aaron M. Hosios Gary Bellinger Jie Li Yimin Yu Mika Sasaki James W. Horner Laura N. Burga Jianxin Xie Michael J. Jurczak Ronald A. DePinho Clary B. Clish Tyler Jacks Richard G. Kibbey Gerburg M. Wulf Dolores Di Vizio Gordon B. Mills Lewis C. Cantley Matthew G. Vander Heiden

The pyruvate kinase M2 isoform (PKM2) is expressed in cancer and plays a role in regulating anabolic metabolism. To determine whether PKM2 is required for tumor formation or growth, we generated mice with a conditional allele that abolishes PKM2 expression without disrupting PKM1 expression. PKM2 deletion accelerated mammary tumor formation in a Brca1-loss-driven model of breast cancer. PKM2 nu...

2012
Dimitrios Anastasiou Yimin Yu William J. Israelsen Jian-kang Jiang Matthew B. Boxer Bum Soo Hong Wolfram Tempel Svetoslav Dimov Min Shen Abhishek Jha Hua Yang Katherine R. Mattaini Christian M. Metallo Brian P. Fiske Kevin D. Courtney Scott Malstrom Tahsin M. Khan Charles Kung Amanda P. Skoumbourdis Henrike Veith Noel Southall Martin J. Walsh Kyle R. Brimacombe William Leister Sophia Y. Lunt Zachary R. Johnson Katharine E. Yen Kaiko Kunii Shawn M. Davidson Heather R. Christofk Christopher P. Austin James Inglese Marian H. Harris John M. Asara Gregory Stephanopoulos Francesco G. Salituro Shengfang Jin Lenny Dang Douglas S. Auld Hee-Won Park Lewis C. Cantley Craig J. Thomas Matthew G. Vander Heiden

Cancer cells engage in a metabolic program to enhance biosynthesis and support cell proliferation. The regulatory properties of pyruvate kinase M2 (PKM2) influence altered glucose metabolism in cancer. The interaction of PKM2 with phosphotyrosine-containing proteins inhibits enzyme activity and increases the availability of glycolytic metabolites to support cell proliferation. This suggests tha...

2015
Zita Garate Oscar Quintana-Bustamante Ana M. Crane Emmanuel Olivier Laurent Poirot Roman Galetto Penelope Kosinski Collin Hill Charles Kung Xabi Agirre Israel Orman Laura Cerrato Omaira Alberquilla Fatima Rodriguez-Fornes Noemi Fusaki Felix Garcia-Sanchez Tabita M. Maia Maria L. Ribeiro Julian Sevilla Felipe Prosper Shengfang Jin Joanne Mountford Guillermo Guenechea Agnes Gouble Juan A. Bueren Brian R. Davis Jose C. Segovia

Pyruvate kinase deficiency (PKD) is a rare erythroid metabolic disease caused by mutations in the PKLR gene. Erythrocytes from PKD patients show an energetic imbalance causing chronic non-spherocytic hemolytic anemia, as pyruvate kinase defects impair ATP production in erythrocytes. We generated PKD induced pluripotent stem cells (PKDiPSCs) from peripheral blood mononuclear cells (PB-MNCs) of P...

Journal: :Haematologica 2009
Sandrine Hayette Kaddour Chabane Andrei Tchirkov Marc G Berger Franck E Nicolini Olivier Tournilhac

in normal lymphocytes (Figure 2E). In samples from ALL patients, however, equivalent expression levels of PKM1/2 and PKM2 were present (Figure 2F). Analogous to the Q-PCR results, no significant difference in protein levels were observed between prednisolone-resistant and prednisolone–sensitive cases, suggesting that pyruvate kinase isoform M2 is not responsible for glucocorticoid resistance in...

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