The prolactin receptor (PRLR) is a member of the class I cytokine/lactogen receptor family which mediates the diverse cellular actions of prolactin in several tissues. PRLRs are expressed in normal and neoplastic human breast tissue, and in most breast cancer cells. PRLR contains an extracellular region that binds prolactin, a transmembrane region, and a cytoplasmatic region required for the activation of the Jak2–Stat5 signal transduction pathway by Prl which is essential for transcriptional activation of all known prolactin regulated genes. PRLRs have also been observed in ovarian follicular cells of mice, pigs, sheep, deer, and humans, as well as in luteal tissue in cow and horse ovaries. Furthermore, PRLR knockout mice exhibit failure of embryonic implantation, reduced number of mature oocytes, and low fertilization rates. Knockout females also display a reduced number of primary follicles.
Prolactin receptor (PRLR) is a single-pass transmembrane receptor belonging to the type â… cytokine receptor superfamily, and contains two fibronectin type-â…¢ domains. All class 1 ligands activate their respective receptors by clustering mechanisms. Ligand binding results in the transmembrane PRLR dimerization, followed by phosphorylation and activation of the molecules invloved in the signaling pathways, such as Jak-STAT, Ras/Raf/MAPK. The PRLR contains no intrinsic tyrosine kinase cytoplasmic domain but associates with a cytoplasmic tyrosine kinase, JAK2. PRLR mainly serves as the receptor for the pituitary hormone prolactin (PRL), a secreted hormone that affects reproduction and homeostasis in vertebrates. PRLR can be regulated by an interplay of two different mechanisms, PRL or ovarian steroid hormones independently or in combination in a tissue-specific manner. The role of the hormone prolactin (PRL) in the pathogenesis of breast cancer is mediated by its cognate receptor (PRLR). Ubiquitin-dependent degradation of the PRLR that negatively regulates PRL signaling is triggered by PRL-mediated phosphorylation of PRLR on Ser349 followed by the recruitment of the beta-transducin repeats-containing protein (beta-TrCP) ubiquitin-protein isopeptide ligase. which altered PRLR stability may directly influence the pathogenesis of breast cancer.
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