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Title: Fish caudal neurosecretory system: a model for the study of neuroendocrine secretion. Author: McCrohan CR, Lu W, Brierley MJ, Dow L, Balment RJ. Journal: Gen Comp Endocrinol; 2007; 153(1-3):243-50. PubMed ID: 17316635. Abstract: The caudal neurosecretory system (CNSS) is unique to fish and has suggested homeostatic roles in osmoregulation and reproduction. Magnocellular neuroendocrine Dahlgren cells, located in the terminal segments of the spinal cord, project to a neurohaemal organ, the urophysis, from which neuropeptides are released. In the euryhaline flounder Platichthys flesus Dahlgren cells synthesise at least four peptides, including urotensins I and II and CRF. These peptides are differentially expressed with co-localisation of up to three in a single cell. Dahlgren cells display a range of electrical firing patterns, including characteristic bursting activity, which is dependent on L-type Ca(2+) and Ca-activated K(+)channels. Activity is modulated by a range of extrinsic and intrinsic neuromodulators. This includes autoregulation by the secreted peptides themselves, leading to enhanced bursting. Electrophysiological and mRNA expression studies have examined changes in response to altered physiological demands. Bursting activity is more robust and more Dahlgren cells are recruited in seawater compared to freshwater adapted fish and this is mirrored by a reduction in mRNA expression for L-type Ca(2+) and Ca-activated K(+) channels. Acute seawater/freshwater transfer experiments support a role for UII in adaptation to hyperosmotic conditions. Responses to stress suggest a shared role for CRF and UI, released from the CNSS. We hypothesise that the Dahlgren cell population is reprogrammed, both in anticipation of and in response to changed physiological demands, and this is seen as changes in gene expression profile and electrical activity. The CNSS shows striking parallels with the hypothalamic-neurohypophysial system, providing a highly accessible system for studies of neuroendocrine mechanisms. Furthermore, the presence of homologues of urotensins throughout the vertebrates has sparked new interest in these peptides and their functional evolution.[Abstract] [Full Text] [Related] [New Search]