Steroid hormones are a class of hormones derived from cholesterol. Examples include hormones such as cortisol, aldosterone, estrogen, and testosterone. Unlike polypeptide hormones, which are typically hydrophilic and cannot easily pass through the cell membrane, steroid hormones are lipophilic and can readily diffuse across cell membranes.
Once inside the target cell, steroid hormones bind to specific receptors that are located in the cytosol or nucleus of the cell (option B). The receptor-hormone complex then translocates into the nucleus, where it acts as a transcription factor, binding to specific DNA sequences and regulating gene expression. This ultimately leads to changes in protein synthesis and cellular function.
Polypeptide hormones, on the other hand, commonly function via specific second messengers (option C). Upon binding to cell surface receptors, they initiate signaling cascades that involve the activation of second messengers such as cyclic adenosine monophosphate (cAMP), inositol trisphosphate (IP3), and calcium ions. These second messengers propagate the hormone signal within the cell, leading to various cellular responses.
Steroid hormones tend to have longer-lasting effects compared to polypeptide hormones because they alter gene expression, resulting in the synthesis of new proteins (option D). This is in contrast to polypeptide hormones, which often exert more rapid but transient effects by modifying existing proteins or activating existing cellular pathways.
Therefore, the statement that is true about steroid hormones in comparison to polypeptide hormones is that steroid hormones are more likely to have an associated receptor in the cytosol or nucleus (option B).