A variety of synthetic steroids and sterols have also been contrived. Most are steroids, but some non-steroidal molecules can interact with the steroid receptors because of a similarity of shape. Some synthetic steroids are weaker, and some much stronger, than the natural steroids whose receptors they activate.
Steroids exert a wide variety of effects mediated by slow genomic as well as by rapid nongenomic mechanisms. They bind to nuclear receptors in the cell nucleus for genomic actions. Membrane-associated steroid receptors activate intracellular signaling cascades involved in nongenomic actions.
Because steroids and sterols are lipid-soluble, they can diffuse fairly freely from the blood through the cell membrane and into the cytoplasm of target cells. In the cytoplasm, the steroid may or may not undergo an enzyme-mediated alteration such as reduction, hydroxylation, or aromatization. In the cytoplasm, the steroid binds to the specific receptor, a large metalloprotein. Upon steroid binding, many kinds of steroid receptor dimerize: Two receptor subunits join together to form one functional DNA-binding unit that can enter the cell nucleus. In some of the hormone systems known, the receptor is associated with a heat shock protein, which is released on the binding of the ligand, the hormone. Once in the nucleus, the steroid-receptor ligand complex binds to specific DNA sequences and induces transcription of its target genes.