Angiotensin II (Ang II) is a peptide associated with the regulation of blood pressure, though the elevated presence of Ang II in the inflamed bowel – and other inflamed tissues – and the presence of receptors for Ang II on sensory neurons may point to additional roles in nociception in inflammatory disease. Work in this Thesis sought to examine the identity of sensory neurons with which Ang II interacts, the mechanisms underpinning these interactions, and the consequences on neuronal properties and function. Ca2+ imaging revealed that Ang II stimulated a rise in cytosolic Ca2+ in small-diameter sensory neurons which expressed the nociceptive markers TRPV1 and Nav1.8. This population of Ang II-sensitive neurons could be divided in two, with one subpopulation expressing Tmem45b and binding the non-peptidergic marker isolectin-B4 (IB4), while the other subpopulation lacked both Tmem45b and IB4 binding. The response of IB4-binding sensory neurons to Ang II was mediated by the Type I Ang II receptor (AT1R). Conversely, the response of IB4-negative neurons to Ang II did not require AT1R but did require the presence of non-neuronal satellite cells. Ang II-evoked Ca2+ signals downstream of AT1R were mediated by Ca2+ release from intracellular stores via the activation of IP3 receptors, followed by store-operated Ca2+ entry (SOCE). SOCE downstream of Ang II application was found to be mediated by the non-selective cation channel, TRPC3, activated by the endoplasmic reticulum Ca2+ sensor, STIM. Incubation of sensory neurons with Ang II induced to nuclear translocation of the transcription factor, nuclear factor of activated T-cells 5 (NFAT5). This translocation was dependent on Ca2+ influx through TRPC3 and the Ca2+-sensitive phosphatase, calcineurin. Translocation of NFAT5 may indicate prolonged changes in nociceptor properties induced by Ang II, as evidenced by an increase in electrical excitability of IB4-binding neurons following overnight Ang II incubation. In summary, experiments detailed in this Thesis have revealed that Ang II stimulated nociceptive sensory neurons in vitro. Ang II-evoked Ca2+ signals were mediated by store depletion and subsequent SOCE through TRPC3. These Ca2+ signals drove translocation of NFAT5 to the nucleus in a manner dependent on calcineurin. Finally, non-peptidergic neurons exposed to Ang II displayed elevated excitability. These data highlight a mechanism through which Ang II may drive prolonged changes in nociceptor function.