β-Adrenergic Receptor and Insulin Resistance in the Heart

Supachoke Mangmool, Tananat Denkaew, Warisara Parichatikanond, Hitoshi Kurose, Supachoke Mangmool, Tananat Denkaew, Warisara Parichatikanond, Hitoshi Kurose

Abstract

Insulin resistance is characterized by the reduced ability of insulin to stimulate tissue uptake and disposal of glucose including cardiac muscle. These conditions accelerate the progression of heart failure and increase cardiovascular morbidity and mortality in patients with cardiovascular diseases. It is noteworthy that some conditions of insulin resistance are characterized by up-regulation of the sympathetic nervous system, resulting in enhanced stimulation of β-adrenergic receptor (βAR). Overstimulation of βARs leads to the development of heart failure and is associated with the pathogenesis of insulin resistance in the heart. However, pathological consequences of the cross-talk between the βAR and the insulin sensitivity and the mechanism by which βAR overstimulation promotes insulin resistance remain unclear. This review article examines the hypothesis that βARs overstimulation leads to induction of insulin resistance in the heart.

Keywords: G protein-coupled receptor kinase; Heart diseases; Insulin resistance; Protein kinase A; β-adrenergic receptor; β-blockers.

Conflict of interest statement

We declare that we have no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Structure of insulin receptor. Insulin receptor is a heterotetrameric receptor that contains two α subunits, which is extracellular and has the ligand-binding domain, and two β subunits, which consist of extracellular, transmembrane and intracellular domains. The tyrosine kinase domain of the receptor is present at the intracellular β subunits.
Fig. 2.
Fig. 2.
Insulin signaling pathway. Upon binding of insulin to its receptor, a cascade of intracellular events in the cells is initiated. The activated insulin receptor phosphorylates and activates substrate proteins such as Shc and IRS. Phosphorylation of Shc promotes the formation of Shc/Grb-2/SOS complex which stimulates MAP kinase pathway, resulting in mitogenesis, cell growth, and differentiation. Phosphorylated IRS proteins interact with many other signaling proteins including Grb-2 and PI3K, and change cellular function. PI3K catalyzes the formation of PIP3 which, in turn, activates Akt and aPKC, and controls many aspects of insulin action, including protein synthesis, glycogen synthesis, and glucose transport via the translocation of GLUT4 to the plasma membrane. Glucose that enters the cells is rapidly phosphorylated by hexokinase enzymes to generate glucose-6-phosphate (G-6-P), and is subsequently utilized for metabolism and/or stored in the cells as glycogen or TG.
Fig. 3.
Fig. 3.
Insulin actions on many tissues. Insulin is secreted from the pancreas from the β-cells of the islets of Langerhans and circulated throughout the body via the bloodstream. The released insulin acts on insulin receptors located on the plasma membrane of target tissues (i.e., skeletal muscle, liver, adipose tissue and heart). In skeletal muscle, cardiac muscle, and liver, insulin promotes glucose uptake and storage as glycogen or TG. In adipose tissue, insulin promotes conversion of glucose to TG by increasing lipid synthesis.
Fig. 4.
Fig. 4.
Schematic diagram representing the signaling pathway for βAR-mediated cardiac insulin resistance. Agonist binding to β2ARs leads to the G protein-mediated activation of AC and cAMP generation. cAMP directly binds to and activates PKA. In β2AR signaling, PKA phosphorylates GRK2, which subsequently increases GRK2 activity. This leads to the inhibition of insulin-induced GLUT4 expression and the translocation of GLUT4 to the plasma membrane, thereby interfering with glucose uptake into cells and insulin-induced IRS1 phosphorylation. In β1AR signaling, PKA and PI3K activate Akt by phosphorylation at Ser 473, which in turn, phosphorylates the β subunit of insulin receptor (IRβ) at Thr residues. Tyrosine phosphorylation of IRβ inhibits insulin-induced tyrosine autophosphorylation of IRβ, leading to impairment of insulin signaling. These conditions lead to insulin resistance in the heart. Treatment with β-blockers antagonizes ISO-mediated insulin resistance in the heart.

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