Quantitative light microscopic autoradiographic localization of binding sites labelled with [3H]vasopressin antagonist d(CH2)5Tyr(Me)VP in the rat brain, pituitary and kidney
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Cited by (94)
Vasopressin-dependent short-term regulation of aquaporin 4 expressed in Xenopus oocytes
2009, NeuroscienceCitation Excerpt :These studies emphasize that AQP4 regulation is clearly a complicated matter which may take place on the protein and/or mRNA level and may depend on several different signaling pathways and on differences in the underlying mechanism of edema formation which may affect the expression level of AQP4 differentially. The V1aR is expressed in rat brain (van Leeuwen et al., 1987; Chen et al., 1993) in neurons, glial cells, and in the endothelial cells of the blood–brain-barrier (Szmydynger-Chodobska et al., 2004). Notably, the expression of V1aR increased in astrocytes as well as in endothelial cells following traumatic brain injury in rats and was associated with a noticeable redistribution of V1aR towards the astrocytic processes (Szmydynger-Chodobska et al., 2004).
AVP effects and water channels in non-neuronal CNS cells
2003, Advances in Molecular and Cell BiologyCitation Excerpt :Intracerebroventricular injection of AVP reduces blood flow in the choroid plexus and decreases CSF secretion (Faraci et al., 1988, 1990; Maktabi et al., 1993; Chodobski et al., 1998a) as well as transfer of 22Na from blood to CSF (Davson and Segal, 1970). AVP binding sites are abundant in choroid plexus epithelial cells (van Leeuwen et al., 1987; Tribollet et al., 1999), and they are both of the V1a and V1b subtype (Ostrowski et al., 1994; Burbach et al., 1995). In addition, V2 receptor mRNA was detected in the choroid plexus of newborn rats, but it was not detectable in the adult (Kato et al., 1995).
Intracellular pathways of V<inf>1</inf> and V<inf>2</inf> receptors activated by arginine vasopressin in rat hippocampal neurons
1999, Journal of Biological Chemistry