Hormones can be classified into three main types based on their chemical structures: steroids, peptides, and amines. Their actions are mediated by the specific receptors they bind to on target cells.
Steroid hormones are derived from cholesterol and are lipophilic in nature. This allows them to readily traverse the lipid-rich cell membrane to bind to their intracellular receptors in the cytoplasm or nucleus. Once bound, the cytoplasmic hormone-receptor complex translocates to the nucleus. Here, it binds to regulatory sequences on the DNA to alter gene expression.
Peptide hormones are made up of chains of amino acids and are hydrophilic. Hence, they are unable to diffuse across the cell membrane. Instead, they bind to extracellular receptors present on the surface of target cells. Such binding triggers a series of signaling reactions within the cell to ultimately carry out the specific functions of the hormone.
Amine hormones are derived from a single amino acid, either tyrosine or tryptophan. This class of hormones is unique because they share their mechanism of action with both steroid as well as peptide hormones. For example, although epinephrine and thyroxine are both derived from the amino acid tyrosine, they mediate their effects through diverse mechanisms. Epinephrine binds to G-protein coupled receptors present on the surface of the plasma membrane, which initiates a signaling cascade that activates second messengers in the cytoplasm to produce a cell-specific response.
In contrast, the thyroid hormone thyroxine (T4) is converted to its active form triiodothyronine (T3) and transported across the plasma membrane. Within the cell, thyroid hormone receptors are present in a complex with nuclear DNA. The thyroid hormone binds to this hormone-DNA complex to alter gene expression.
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