Kinase glucocorticoid inducible

Pyruvate dehydrogenase kinases are induced by glucocorticoid hormones and long-chain fatty acids (acting via the peroxisome proliferation-activated... 

Inhibitors of the serum- and glucocorticoid-inducible-kinase 1 (SGK1)... 

Watt GB, Ismail NA, Caballero AG et al (2012) Epithelial Na+ channel activity in human airway epithelial cells the role of serum and glucocorticoid-inducible kinase 1. Br J Pharmacol 166(4) 1272-1289... 

Glucocorticoids—mainly cortisol (see p. 374)—induce all of the key enzymes involved in gluconeogenesis [4, 6, 8, 9]. At the same time, they also induce enzymes involved in amino acid degradation and thereby provide precursors for gluconeogenesis. Regulation of the expression of PEP carbo>Q -kinase, a key enzyme in gluconeogenesis, is discussed in detail on p. 244. 

Phosphoenolpyruvate carboxykinase is induced. Oxaloacetate produces PEP in a reaction catalyzed by PEPCK. Cytosolic PEPCK is an inducible enzyme, which means that the quantity of the enzyme in the cell increases because of increased transcription of its gene and increased translation of its mRNA. The major inducer is cyclic adenosine monophosphate (cAMP), which is increased by hormones that activate adenylate cyclase. Adenylate cyclase produces cAMP from ATP. Glucagon is the hormone that causes cAMP to rise during fasting, whereas epinephrine acts during exercise or stress. cAMP activates protein kinase A, which phosphorylates a set of specific transcription factors (CREB) that stimulate transcription of the PEPCK gene (see Chapter 16 and Pig. 16.18). Increased synthesis of mRNA for PEPCK results in increased synthesis of the enzyme. Cortisol, the major human glucocorticoid, also induces PEPCK. 

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