Relevant bibliographies by topics / Phosphorylase kinase [PhK]

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Academic literature on the topic 'Phosphorylase kinase [PhK]'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Phosphorylase kinase [PhK]"

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Cawley, K. C., C. G. Akita, and D. A. Walsh. "Expression of a cDNA for the catalytic subunit of skeletal-muscle phosphorylase kinase in transfected 3T3 cells." Biochemical Journal 263, no. 1 (October 1, 1989): 223–29. http://dx.doi.org/10.1042/bj2630223.

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Phosphorylase kinase is a multimeric enzyme of composition (alpha, beta, gamma, delta)4 whose catalytic activity resides in the gamma-subunit. As an approach to understand further its regulation, a cDNA for the gamma-subunit of phosphorylase kinase (gamma PhK) has been cloned into a mammalian expression vector behind the mouse metallothionein-1 promoter. NIH 3T3 cells were co-transfected with this construct (pEV gamma PhK) and pSV2neo, G418-resistant clones were selected, and several were found to have stably incorporated the gamma-subunit cDNA into their genomic DNA. Phosphorylase kinase activity was clearly present in extracts from cultures of pEV gamma PhK-transformed cells and increased several-fold after 24 h of incubation with Zn2+, whereas it was undetectable in the parent 3T3 cells. A significant, but variable, proportion (15-70%) of the activity was Ca2+-dependent. We conclude that the phosphorylase kinase activity expressed by the cells transformed with pEV gamma PhK is due to free gamma-subunit and gamma-subunit associated with cellular calmodulin, which replaces the delta-subunit normally associated with the gamma-subunit in the holoenzyme.
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Lai, Guangrui, Jingjing Wu, Xiaoliang Liu, and Yanyan Zhao. "20-HETE Induces Hyperglycemia through the cAMP/PKA-PhK-GP Pathway." Molecular Endocrinology 26, no. 11 (November 1, 2012): 1907–16. http://dx.doi.org/10.1210/me.2012-1139.

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Abstract We previously generated cytochrome P450 4F2 (CYP4F2) transgenic mice and showed high 20-hydroxyeicosatetraenoic acid (20-HETE) production, which resulted in an elevation of blood pressure. However, it was unclear whether 20-HETE affected glucose metabolism. We measured fasting plasma glucose, insulin, hepatic CYP4F2 expression, and 20-HETE production by hepatic microsomes, and hepatic 20-HETE levels in transgenic mice. We also assessed glycogen phosphorylase (GP) activity and the cAMP/protein kinase A (PKA)-phosphorylase kinase (PhK)-GP pathway, as well as expressions of insulin receptor substrate 1 and glucose transporters in vivo and in vitro. The transgenic mice had overexpressed hepatic CYP4F2, high hepatic 20-HETE and fasting plasma glucose levels but normal insulin level. The GP activity was increased and the cAMP/PKA-PhK-GP pathway was activated in the transgenic mice compared with wild-type mice. Moreover, these alterations were eliminated with the addition of N-hydroxy-N′-(4-butyl-2 methylphenyl) formamidine, which is a selective 20-HETE inhibitor. The results were further validated in Bel7402 cells. In addition, the transgenic mice had functional insulin signaling, and 20-HETE had no effect on insulin signaling in Bel7402 cells, excluding that the observed hyperglycemia in CYP4F2 transgenic mice resulted from insulin dysfunction, because the target tissues were sensitive to insulin. Our study suggested that 20-HETE can induce hyperglycemia, at least in part, through the cAMP/PKA-PhK-GP pathway but not through the insulin-signaling pathway.
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AYERS, Nancy A., Owen W. NADEAU, Mark W. READ, Partha RAY, and Gerald M. CARLSON. "Effector-sensitive cross-linking of phosphorylase b kinase by the novel cross-linker 4-phenyl-1,2,4-triazoline-3,5-dione." Biochemical Journal 331, no. 1 (April 1, 1998): 137–41. http://dx.doi.org/10.1042/bj3310137.

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The dienophile 4-phenyl-1,2,4-triazoline-3,5-dione (PTD) was identified as a novel protein cross-linker, and utilized as a conformational probe of phosphorylase b kinase (PhK), a hexadecameric enzyme with the subunit composition (αβγδ)4. In its reaction with this enzyme, PTD produced five major cross-linked conjugates as resolved by denaturing gel electrophoresis: αβ, βγγ, αγ and a doublet of differently migrating homodimers, ββ1 and ββ2. Cross-linking in the presence of six different activators of the kinase targeted to its various subunits caused substantial changes in the amounts of three of the conjugates. The formation of αγ was increased by all of the activators but the largest enhancement was caused by exogenous Ca2+/calmodulin. All except one of the activators decreased the amount of βγγ formed, with Mg2+ having the greatest effect, and all except two increased the amount of ββ1, with Mg2+ again having the largest influence. From the overall similarity of the changes in cross-linking by PTD induced by the various activators, we conclude that, even though they are targeted to different sites and subunits, they induce activated conformations of PhK that have certain structural features in common. Regarding the mechanism of cross-linking by PTD, its reaction with a model nucleophile suggests that its initial reaction with a side chain nucleophile of PhK involves a 1,4-conjugate addition to form a urazole adduct, with the secondary cross-linking reaction occurring through an as yet unknown pathway.
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Schepetkin, Igor A., Mark B. Plotnikov, Andrei I. Khlebnikov, Tatiana M. Plotnikova, and Mark T. Quinn. "Oximes: Novel Therapeutics with Anticancer and Anti-Inflammatory Potential." Biomolecules 11, no. 6 (May 22, 2021): 777. http://dx.doi.org/10.3390/biom11060777.

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Oximes have been studied for decades because of their significant roles as acetylcholinesterase reactivators. Over the last twenty years, a large number of oximes have been reported with useful pharmaceutical properties, including compounds with antibacterial, anticancer, anti-arthritis, and anti-stroke activities. Many oximes are kinase inhibitors and have been shown to inhibit over 40 different kinases, including AMP-activated protein kinase (AMPK), phosphatidylinositol 3-kinase (PI3K), cyclin-dependent kinase (CDK), serine/threonine kinases glycogen synthase kinase 3 α/β (GSK-3α/β), Aurora A, B-Raf, Chk1, death-associated protein-kinase-related 2 (DRAK2), phosphorylase kinase (PhK), serum and glucocorticoid-regulated kinase (SGK), Janus tyrosine kinase (JAK), and multiple receptor and non-receptor tyrosine kinases. Some oximes are inhibitors of lipoxygenase 5, human neutrophil elastase, and proteinase 3. The oxime group contains two H-bond acceptors (nitrogen and oxygen atoms) and one H-bond donor (OH group), versus only one H-bond acceptor present in carbonyl groups. This feature, together with the high polarity of oxime groups, may lead to a significantly different mode of interaction with receptor binding sites compared to corresponding carbonyl compounds, despite small changes in the total size and shape of the compound. In addition, oximes can generate nitric oxide. This review is focused on oximes as kinase inhibitors with anticancer and anti-inflammatory activities. Oximes with non-kinase targets or mechanisms of anti-inflammatory activity are also discussed.
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Bisciglia, Michela, Roseline Froissart, Anne Laure Bedat-Millet, Norma Beatriz Romero, Magali Pettazzoni, Jean-Yves Hogrel, François M. Petit, and Tanya Stojkovic. "A novel PHKA1 mutation associating myopathy and cognitive impairment: Expanding the spectrum of phosphorylase kinase b (PhK) deficiency." Journal of the Neurological Sciences 424 (May 2021): 117391. http://dx.doi.org/10.1016/j.jns.2021.117391.

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Li, Chunyun, Lihua Huang, Lang Tian, Jia Chen, Shentang Li, and Zuocheng Yang. "PHKG2 mutation spectrum in glycogen storage disease type IXc: a case report and review of the literature." Journal of Pediatric Endocrinology and Metabolism 31, no. 3 (March 28, 2018): 331–38. http://dx.doi.org/10.1515/jpem-2017-0170.

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AbstractBackground:PHKG2gene mutation can lead to liver phosphorylase kinase (PhK) deficiency, which is related to glycogen storage disease type IX (GSD IX). GSD IXc due toPHKG2mutation is the second most common GSD IX.Methods:We identified a novel mutation (c.553C>T, p.Arg185X) inPHKG2in a Chinese family and verified it by next-generation and Sanger sequencing. The mutation spectrum of thePHKG2gene was summarized based on 25 GSD IXc patients withPHKG2mutations.Results:We found that missense mutation (39%) was the most common type of mutation, followed by nonsense mutation (23%). Mutations were more prevalent in Asian (12/25) and European (9/25) populations than in populations from elsewhere. The exons had more sites of mutation than the introns, and exons 3 and 6 were the most frequent sites of mutations.Conclusions:This study expands our knowledge of thePHKG2gene mutation spectrum, providing a molecular basis for GSD IXc.
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Calalb, M. B., D. T. Fox, and S. K. Hanks. "Molecular cloning and enzymatic analysis of the rat homolog of “PhK-gamma T,” an isoform of phosphorylase kinase catalytic subunit." Journal of Biological Chemistry 267, no. 3 (January 1992): 1455–63. http://dx.doi.org/10.1016/s0021-9258(18)45967-4.

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Liu, Li, Stephen R. Rannels, Mary Falconieri, Karen S. Phillips, Ellen B. Wolpert, and Timothy E. Weaver. "The Testis Isoform of the Phosphorylase Kinase Catalytic Subunit (PhK-T) Plays a Critical Role in Regulation of Glycogen Mobilization in Developing Lung." Journal of Biological Chemistry 271, no. 20 (May 17, 1996): 11761–66. http://dx.doi.org/10.1074/jbc.271.20.11761.

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9

Chamberlain, J. S., P. VanTuinen, A. A. Reeves, B. A. Philip, and C. T. Caskey. "Isolation of cDNA clones for the catalytic gamma subunit of mouse muscle phosphorylase kinase: expression of mRNA in normal and mutant Phk mice." Proceedings of the National Academy of Sciences 84, no. 9 (May 1, 1987): 2886–90. http://dx.doi.org/10.1073/pnas.84.9.2886.

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10

Anderton, Brian H., Joanna Betts, Walter P. Blackstock, Jean-Pierre Brion, Sara Chapman, James Connell, Rejith Dayanandan, et al. "Sites of phosphorylation in tau and factors affecting their regulation." Biochemical Society Symposia 67 (February 1, 2001): 73–80. http://dx.doi.org/10.1042/bss0670073.

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The microtubule-associated protein, tau, is the principal component of paired helical filaments (PHFs) in Alzheimer's disease. PHF-tau is highly phosphorylated and a total of 25 sites of phosphorylation have so far been identified. Many of these sites are serine or threonine residues that are immediately followed in the sequence by proline residues, and hence are candidate phosphorylation sites for proline-directed kinases. In vitro, glycogen synthase kinase-3 (GSK-3), extracellular signal-related kinase-1 and -2, and mitogen-activated protein kinases, p38 kinase and c-jun N-terminal kinase, all phosphorylate many of these sites, although with different efficiencies for particular sites. Phosphorylation studies in transfected cells and neurons show that GSK-3 phosphorylates tau more extensively than do these other proline-directed kinases. Mutations in tau have been shown to affect in vitro phosphorylation of tau by GSK-3. The Arg406-->Trp (R406W) tau mutation also affects tau phosphorylation in cells.
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Dissertations / Theses on the topic "Phosphorylase kinase [PhK]"

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Carrière, Cathelène. "Caractérisation des structures et fonctions de la phosphorylase kinase." Paris 6, 2008. http://www.theses.fr/2008PA066419.

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La phosphorylase kinase (PhK), enzyme clé de la glycogénolyse, est un complexe hexadécamérique formé de quatre sous-unités différentes (alpha, beta, gamma, delta)4. L’activité catalytique portée par la PhK gamma est modifiée par l’action des sous-unités apparentées alpha et beta (4/5 de la masse de l’enzyme). Des mutations dans la PhK conduisent à une maladie de stockage du glycogène (GSD) de type IX, le désordre le plus répandu dans le métabolisme du glycogène. Peu de choses sont connues sur la structure de l’holoenzyme et sur celle des sous-unités de la PhK (exception faite du domaine catalytique de la PhK gamma et de la PhK delta (calmoduline)). Dans cette thèse, nous avons utilisé des méthodes d’analyse de séquences pour révéler des caractéristiques structurales et fonctionnelles des sous-unités alpha et beta. Nous avons ainsi confirmé l’appartenance du premier domaine (A) à la famille des glucoamylases (Glycosyl Hydrolase 15) et montré que les domaines C et D sont reliés aux protéines « calcineurin B-like », membres de la famille EF-hand impliqués dans la régulation calcium-dépendante de kinases. La plupart des mutations faux-sens affectant la PhK alpha et conduisant à une déficience en PhK sont situées dans les sites actifs de ces domaines, suggérant qu’elles pourraient avoir un impact direct sur leurs fonctions. Par ailleurs, nous avons recalé dans le volume obtenu par cryo-microscopie électronique (résolution 9. 9 Angstrom) les structures 3D des différents domaines de la PhK en nous aidant des contraintes décrites dans la littérature. L’ensemble de ces résultats ouvre de nouvelles perspectives pour comprendre comment les sous-unités de la PhK régulent son activité
Phosphorylase kinase (PhK) is a key enzyme in glycogenolysis. PhK is a hexadecameric complex, made of four different subunits (alpha, beta, gamma, delta)4. Catalytic activity is conferred by the gamma subunit and is modified by the two related regulatory subunits alpha and beta which together account for ~ 4/5 of the PhK mass. Mutations in PhK lead to Glycogen Storage Disease (GSD) type IX, which is the most frequently encountered disorder of glycogen metabolism. The structural features of the quaternary structure of the holoenzyme and the PhK subunits, except for the catalytic domain of the PhK gamma and the PhK delta subunit are poorly understood. Here we have used sensitive methods of sequence analysis to unravel hidden structural and functional features of the PhK alpha and beta subunits. We confirm that the first domain (A) belongs to the glucoamylase family (Glycosyl Hydrolase 15) and show domains C and D are related to calcineurin B-like proteins, which are EF-hand family members involved in the Ca2+-dependent regulation of kinases. Mutations leading PhK deficiency, mostly missense mutations in PhK alpha, are located within the predicted active sites of these domains, suggesting that they may have a direct impact on their predicted functions. Furthermore, we docked the 3D structures of the different PhK domains into the volume obtained by cryo-electron microscopy at 9. 9 Angstrom resolution constraining with various interaction data reported in the literature. Altogether, our findings open new perspectives to understand how the different PhK subunits may regulate the holoenzyme activity
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Book chapters on the topic "Phosphorylase kinase [PhK]"

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Kushwaha, Bhawna, Rohit Beniwal, Aradhana Mohanty, Ajay Kumar Singh, Raj Kumar Yadav, and Satish Kumar Garg. "Effect of Heavy Metals on Tyrosine Kinases Signaling during Sperm Capacitation." In Infertility and Assisted Reproduction [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.99261.

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Sperm capacitation is the key event prior to fertilization. Success rate of currently used assisted reproductive technology like in-vitro fertilization is 50% dependent on sperm maturation or capacitation. In-vivo capacitation occur almost in female reproductive tract in response to various signaling or enzymatic molecules. Interestingly, both early and late events of capacitation are centrally regulated by protein kinase A (PKA). Influx of Ca2+ and HCO3-transmembrane drive leads to change in pH and intracellular cAMP which ultimately activate PKA regulated capacitation. PKA phosphorylates several target proteins that are presumed to initiate different signaling pathways. Some divalent heavy metals like lead, mercury, arsenic and cadmium mimic Ca++ entry and its functions and ultimately affect capacitation by inhibiting or inducing tyrosine phosphorylation. In this chapter we review the mechanism of heavy metals by which they affect the tyrosine phosphorylation during sperm capacitation.
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