China 
Africa 
Explore chapters and articles related to this topic
Catabolite Regulation of the Main Metabolism
Published in Kazuyuki Shimizu, Metabolic Regulation and Metabolic Engineering for Biofuel and Biochemical Production, 2017
Eukaryotic glycogen synthases cannot initiate glycogen synthesis de novo, where they function to elongate a pre-existing oligosaccharide primer attached to glycogenin. Glycogenin participates in the initiation of glycogen synthesis in yeast and mammals, whereas it may not exist in bacteria. The expression of glycogen synthase, glycogen phosphorylase, branching enzyme, debranching enzyme, and glycogenin is tightly regulated, where the Ras/Protein kinase A (PKA) pathway controls transcription of the related genes (Wilson et al. 2010).
p-synephrine induces transcriptional changes via the cAMP/PKA pathway but not cytotoxicity or mutagenicity in human gastrointestinal cells
Published in Journal of Toxicology and Environmental Health, Part A, 2021
Diego Luis Ribeiro, Ana Rita Thomazela Machado, Carla Machado, Alexandre Ferro Aissa, Patrick Wellington Dos Santos, Gustavo Rafael Mazzaron Barcelos, Lusânia Maria Greggi Antunes
In MNP01 cells, SN upregulated the expression of ADCY3 (adenylate cyclase 3), which transcribes a family member of cyclases that catalyze the synthesis of secondary cAMP from ATP in the cytoplasm (Saeed et al. 2018). Thermogenic supplements based upon citrus fruits stimulate cAMP phosphorylation in skeletal muscle (Gannon, Conn, and Vaughan 2015). cAMP exerts its effects by activating PKA, which transduces the signal via phosphorylation of different target proteins. In this study, the lower SN concentration tested (2 μM) upregulated PRKACA and PRKAR2A gene expression in Caco-2 cells. PRKACA and PRKAR2A encode catalytic subunits of PKA, also known as cAMP-dependent protein kinase that participate in the regulation of metabolism and homeostasis (Sarwar et al. 2014; Stratakis 2019).