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An elevated insulin level in blood:Group of answer choicesInhibits glucose uptake by the liverStimulates synthesis of fatty acids and triacylglycerols in the liverStimulates glycogen breakdown in liverInhibits glycogen synthesis in the liver and muscle

Question

An elevated insulin level in blood:Group of answer choicesInhibits glucose uptake by the liverStimulates synthesis of fatty acids and triacylglycerols in the liverStimulates glycogen breakdown in liverInhibits glycogen synthesis in the liver and muscle

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Solution

An elevated insulin level in blood stimulates synthesis of fatty acids and triacylglycerols in the liver.

Here's a step-by-step explanation:

  1. Insulin is a hormone that is produced by the pancreas. It is released into the bloodstream when the levels of glucose (sugar) in the blood are high, such as after a meal.

  2. The main role of insulin is to regulate the amount of glucose in the body. It does this by promoting the uptake and storage of glucose in cells.

  3. In addition to promoting glucose uptake, insulin also stimulates the synthesis of fatty acids and triacylglycerols (a form of fat storage) in the liver.

  4. When insulin levels are high, the liver takes up more glucose from the blood. Some of this glucose is converted into glycogen for storage, but some is also converted into fatty acids.

  5. These fatty acids can then be combined with glycerol to form triacylglycerols, which are stored in the liver and adipose tissue.

  6. Therefore, an elevated insulin level in blood stimulates the synthesis of fatty acids and triacylglycerols in the liver.

So, the correct answer is "Stimulates synthesis of fatty acids and triacylglycerols in the liver".

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Similar Questions

When insulin is released it causesGroup of answer choicesThe liver to decrease fatty acid synthesisMuscle and adipose tissue to increase glucose uptakeThe liver to decrease glucose uptakeLiver and muscle to increase glycogen breakdown

The greater liver glucose output during exercise is due primarily to:Group of answer choicesincreased glycogenolysisreduced hepatic glucose extractionenhanced gluconeogenesis from lactate

In the liver, insulin signalling up-regulates glycolysis. Which of the following signalling pathways explains that mechanism?Group of answer choicesIt activates protein phosphatase-1 which dephosphorylates glycogen phosphorylase.It results in the activation of cAMP dependent protein kinase A (PKA) which phosphorylates pyruvate kinase.It activates the expression of hexokinase, PFK-1 and pyruvate kinase.It results in an increased expression of phosphoenolpyruvate carboxykinase and glucose-6-phosphatase.

Elevated adrenaline levels will inactivateGroup of answer choicesGlycogen breakdown in muscleGlycogen synthesis in the liverGluconeogenesis in the liverGlycolysis in muscle

Glycolysis and gluconeogenesis are tightly regulated, opposing metabolic pathways that help control blood glucose levels.  Glycolysis converts glucose to two pyruvate molecules, whereas gluconeogenesis consumes a net total of 6 NTPs (4 ATPs and 2 GTPs) to convert two pyruvate molecules back to glucose.  When glycolysis is upregulated, gluconeogenesis is downregulated, and vice versa.As shown in Figure 1, glycolysis and gluconeogenesis in the liver are largely regulated by the allosteric action of the small molecule fructose-2,6-bisphosphate (F2,6BP) on the enzymes phosphofructokinase-1 (PFK-1) and fructose-1,6-bisphosphatase (F1,6BPase).  PFK-1 is a kinase that uses ATP to phosphorylate fructose-6-phosphate (F6P) in an irreversible step of glycolysis, forming fructose-1,6-bisphosphate (F1,6BP) and ADP.  During gluconeogenesis, F1,6BPase removes the phosphate group by hydrolysis.Figure 1  Activities of (A) PFK-1 and (B) F1,6BPase on their respective substrates in the presence (solid lines) and absence (dashed lines) of F2,6BPA bifunctional enzyme that contains a phosphofructokinase-2 (PFK-2) domain and a fructose-2,6-bisphosphatase (F2,6BPase) domain controls F2,6BP levels in the liver.  The PFK-2 domain converts F6P to F2,6BP, and the F2,6BPase domain converts F2,6BP back to F6P.  When blood glucose levels are low, the enzyme becomes phosphorylated.  This phosphorylation event simultaneously activates the F2,6BPase domain and inactivates the PFK-2 domain.  Under high blood glucose conditions, the enzyme becomes dephosphorylated, activating the PFK-2 domain and inactivating the F2,6BPase domain.Question 13Which metabolic process most likely provides the energy necessary for sustained gluconeogenesis?A.Fatty acid oxidationB.GlycogenolysisC.FermentationD.Pentose phosphate pathway

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