Таблица. Внешние проявления действия инсулина. Перевести на русский язык = Translate into Russian Модификация: Gardner D.G., Shoback D.M., Eds. Greenspan's Basic & Clinical Endocrinology. 9th ed., Lange, 2011, 960 p., см.: Физиология человека: Литература. Иллюстрации.
№	Tissue	Effect of Insulin
1	Liver	•  Catabolic Pathways      —  Inhibits glycogenolysis      —  Inhibits conversion of fatty acids and amino acids to keto acids      —  Inhibits conversion of amino acids to glucose •  Anabolic Pathways      —  Promotes glucose storage as glycogen (induces glucokinase and glycogen synthase, inhibits phosphorylase)      —  Increases triglyceride synthesis and VLDL formation
2	Muscle	•  Protein Synthesis      —  Increases amino acid transport      —  Increases ribosomal protein synthesis •  Glycogen Synthesis      —  Increases glucose transport      —  Induces glycogen synthethase      —  Inhibits phosphorylase
1	Adipose tissue	•  Triglyceride Storage      —  Lipoprotein lipase is induced by insulin to hydro lyze triglycerides in circulating lipoproteins for delivery of fatty acids to the adipocytes      —  Glucose transport into cell provides glycerol phosphate to permit esterification of fatty acids supplied by lipoprotein transport      —  Intracellular lipase is inhibited by insulin
2	Brain	•  Decreased appetite •  Increased energy expenditure
Примечание:
Liver The first major organ reached by insulin via the bloodstream is the liver. Insulin exerts its action on the liver in two major ways: Insulin promotes anabolism Insulin promotes glycogen synthesis and storage while inhibiting glycogen breakdown. These effects are mediated by changes in the activity of enzymes in the glycogen synthesis pathway (see below). The liver has a maximum storage capacity of 100 to 110 g of glycogen, or approximately 440 kcal of energy. Insulin increases both protein and triglyceride synthesis and very low density lipoprotein (VLDL) formation by the liver. It also inhibits gluconeogenesis and promotes glycolysis through its effects on the function and expression of key enzymes of both pathways. Insulin inhibits catabolism Insulin acts to reverse the catabolic events of the postabsorptive state by inhibiting hepatic glycogenolysis, ketogenesis, and gluconeogenesis. Muscle Insulin promotes protein synthesis in muscle by increasing amino acid transport, as well as by stimulating ribosomal protein synthesis. In addition, insulin promotes glycogen synthesis to replace glycogen stores expended by muscle activity. This is accomplished by increasing glucose transport into the muscle cell, enhancing the activity of glycogen synthase, and inhibiting the activity of glycogen phosphorylase. Approximately 500 to 600 g of glycogen are stored in the muscle tissue of a 70-kg man, but because of the lack of glucose 6-phosphatase in this tissue, it cannot be used as a source of blood glucose, except for a small amount produced when the debranching enzyme releases unphosphorylated glucose from branch points in the glycogen polymer, and the glucose indirectly produced via the liver from lactate generated by muscle. Adipose tissue Fat, in the form of triglyceride, is the most efficient means of storing energy. It provides 9 kcal/g of stored substrate, as opposed to the 4 kcal/g generally provided by protein or carbohydrate. In the typical 70-kg man, the energy content of adipose tissue is about 100,000 kcal. Insulin acts to promote triglyceride storage in adipocytes by a number of mechanisms. (1) It induces the production of lipoprotein lipase in adipose tissue (this is the lipoprotein lipase that is bound to endothelial cells in adipose tissue and other vascular beds), which leads to hydrolysis of triglycerides from circulating lipoproteins, thereby yielding fatty acids for uptake by adipocytes. (2) By increasing glucose transport into fat cells, insulin increases the availability of -glycerol phosphate, a substance used in the esterification of free fatty acids into triglycerides. (3) Insulin inhibits intracellular lipolysis of stored triglyceride by inhibiting intracellular lipase (also called hormone-sensitive lipase). This reduction of fatty acid flux to the liver is a key regulatory factor in the action of insulin to lower hepatic gluconeogenesis and ketogenesis. Central nervous system Although the brain is traditionally not considered an insulin-sensitive tissue, and overall glucose utilization by the brain is not acutely regulated by insulin, key regions of the brain can respond to insulin. Insulin signaling via PI3 kinase in key cells in the hypothalamus functions with leptin signaling to decrease appetite and increase energy expenditure (see Chapter 20).

Схема. Инсулин как средство управления метаболизмом. Перевести на русский язык = Translate into Russian Модификация: Gray H., (1821–1865), Standring S., Ed. Gray's Anatomy: The Anatomical Basis of Clinical Practice. 39th ed., Churchill Livingstone, 2008, 1600 p., см.: Анатомия человека: Литература. Иллюстрации.

Примечание:

Insulin signaling. The insulin receptor is autophosphorylated on multiple tyrosine residues, allowing the docking and activation of multiple signaling molecules that mediate the increases in glucose uptake and metabolism as well as changes in protein and lipid metabolism. aPKC, atypical protein kinase C; C3G, guanine nucleotide exchange factor C3G; CAP, Cbl-associated protein; Cbl, Cas-Br-M (murine) ecotropic retroviral transforming sequence; Crk, CT10 related kinase; GAB, Grb2-associated binding protein; Grb2, growth factor receptor-bound protein 2; GSK3, glycogen synthase kinase-3; IGF, insulin-like growth factor; IRS, insulin receptor substrate; MAP, mitogen-activated protein; mek, MAPK/ERK kinases; P, phosphate; PI(3)K, phosphatidylinositol-3-kinase; PP1, protein phosphatase I; PTEN, phosphatase and tensin homolog deleted on chromosome 10; PTP, protein tyrosine phosphatase; RAS, Rat sarcoma oncogene; Shc, SH3-containing protein; SHIP2, SH2 domain–containing inositol 5-phosphatase; SHP2, SH2 domain–containing protein-tyrosine phosphatase (now called PTPN11); SOS, son of seven less, TC10, small GTP binding protein TC10. (From Saltiel AR, Kahn CR. Insulin signalling and the regulation of glucose and lipid metabolism. Nature. 2001;414:799-806.). 1378=1376, 47%