Vasopressin V1a and V1b Receptors: From Molecules to Physiological Systems

Abstract

The neurohypophysial hormone arginine vasopressin (AVP) is essential for a wide range of physiological functions, including water reabsorption, cardiovascular homeostasis, hormone secretion, and social behavior. These and other actions of AVP are mediated by at least three distinct receptor subtypes: V1a, V1b, and V2. Although the antidiuretic action of AVP and V2 receptor in renal distal tubules and collecting ducts is relatively well understood, recent years have seen an increasing understanding of the physiological roles of V1a and V1b receptors. The V1a receptor is originally found in the vascular smooth muscle and the V1b receptor in the anterior pituitary. Deletion of V1a or V1b receptor genes in mice revealed that the contributions of these receptors extend far beyond cardiovascular or hormone-secreting functions. Together with extensively developed pharmacological tools, genetically altered rodent models have advanced the understanding of a variety of AVP systems. Our report reviews the findings in this important field by covering a wide range of research, from the molecular physiology of V1a and V1b receptors to studies on whole animals, including gene knockout/knockdown studies.

Evolutionary pattern in the OXT-OXTR system in primates: Coevolution and positive selection footprints

“…OXT activity depends on adequate interaction with its unique receptor, OXTR, although it can also bind to the vasopressin receptors (AVPR1a, AVPR1b, and AVPR2) with lower affinity (11)(12)(13). Similar to other receptors that use G proteins as transducer signals across the cell membranes, OXTR is composed of seven transmembrane (TM1-TM7), four extracellular (N-terminal tail-ECL3), and four intracellular (ICL1-C-terminal tail) domains.…”

In vivo processing and release into the circulation of GFP fusion protein in arginine vasopressin enhanced GFP transgenic rats: response to osmotic stimulation

“…However, the significance of the sexual difference in the AVP or CP systems remains unknown. Since only a fragment (possibly CP [1][2][3][4][5][6][7][8][9][10][11][12][13][14] of CP is expressed in these Tg rats as part of the fusion protein with GFP, it is not clear if CP would be functional in these Tg rats in vivo. In fact, some of the exaggerated responses of this Tg animal might be related to this mutation [13].…”

“…AVP preproprotein (A) and AVP-GFP fusion preproprotein (B) consist of the signal peptide (SP), AVP hormone, AVP-associated neurophysin (NP) II and the glycoprotein copeptin (CP), where the glycan is represented by a diamond. The translation as a CP [1][2][3][4][5][6][7][8][9][10][11][12][13][14] is expected in this transgene, and the sixth asparagine of CP is expected to be a glycosylation site. The numbers denote the amino acids present in each region.…”

“…After GFP-IP, the CP 7-14 positive band was only detected at the same level of 28 kDa (B). The second incubation with GFP antibodies demonstrated that the CP 7-14 positive proteins appeared to exist as CP [1][2][3][4][5][6][7][8][9][10][11][12][13][14] and GFP fusion proteins (B). Western analyses were repeated independently three times by using different samples and gave similar results.…”

Activation of V2 vasopressin receptors induces recovery of motor function in patients with stroke, Parkinson’s disease and parkinsonism of different nature

“…К таким нейро-пептидам относится аргинин-вазопрессин (АВП), который наряду с гормональными свойствами (ан-тидиуретическим и вазопрессорным) проявляет свойства нейротрансмиттера и нейромодулятора. Показано, что АВП обеспечивает адаптацию гипо-таламо-гипофизарно-надпочечниковой системы к стрессу, участвует в регуляции автономных функ-ций (сердечно-сосудистой системы, терморегу-ляции), циркадной ритмичности, в оценке запахов, в социальном поведении, в процессе обучения, влияет на память и эмоциональную сферу [24,44]. Установлено, что V1-рецепторы вазопрессина (ВП) широко представлены в гипоталамических и экс-трагипоталамических образованиях у крыс, в том числе в структурах мозга, имеющих отношение к регуляции двигательной функции [38,46,47,51].…”