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Chapter 9: Q. 27 (page 252)

Insulin is a hormone that regulates blood sugar by binding to its receptor, insulin receptor tyrosine kinase. How does insulin’s behavior differ from steroid hormone signaling, and what can you infer about its structure?

Short Answer

Expert verified

Insulin is polar as a result it does not enter the cell while the steroid is smaller in size and non-polar it easily crosses the membrane and form a hormone-receptor complex and directly communicate with cellular DNA to regulate transcription.

Step by step solution

01

Step 1. Introduction

Insulin is a blood sugar-regulating hormone that binds to its receptor tyrosine kinase which is an enzyme-linked transmembrane receptor.

02

Step 2. Explanation

Tyrosine kinase receptors are embedded in the plasma membrane and insulin attach to the outer surface of the receptor to initiate intercellular signaling cascades. Usually, Steroid hormone enters the cell to bind with intercellular receptors as it is small and non-polar. These intercellular hormone-receptor complexes directly communicate with cellular DNA and regulate transcription. However, insulin does not cross the plasma membrane it could be because of its large size or polar.

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Most popular questions from this chapter

What property prevents the ligands of cell-surface receptors from entering the cell?

a. The molecules bind to the extracellular domain.

b. The molecules are hydrophilic and cannot penetrate the hydrophobic interior of the plasma membrane.

c. The molecules are attached to transport proteins that deliver them through the bloodstream to target cells.

d. The ligands are able to penetrate the membrane and directly influence gene expression upon receptor binding.

A scientist notices that a cancer cell line shows high levels of phosphorylated ERK in the absence of EGF. What are two possible explanations for the increase in phosphorylated ERK? Be specific in which proteins are involved.

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a. Intracellular

b. Hormone

c. Enzyme-linked

d. Gated ion channel-linked
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