Recent studies have indicated that arachidonic acid is primarily metabolized by cytochromeP-450 (CYP) enzymes in the brain, lung, kidney, and peripheral vasculature to 20-hydroxyeicosatetraenoic ac...

P-450 Metabolites of Arachidonic Acid in the Control of Cardiovascular Function

This review is aimed at providing readers with a comprehensive reference article about the distribution and function of P2 receptors in all the organs, tissues, and cells in the body. Each section provides an account of the early history of purinergic signaling in the organ/cell up to 1994, then summarizes subsequent evidence for the presence of P2X and P2Y receptor subtype mRNA and proteins as well as functional data, all fully referenced. A section is included describing the plasticity of expression of P2 receptors during development and aging as well as in various pathophysiological conditions. Finally, there is some discussion of possible future developments in the purinergic signaling field.

/pdf/cellular-distribution-and-functions-of-p2-receptor-subtypes-32555c8g2p.pdf

Cellular distribution and functions of P2 receptor subtypes in different systems.

The Na(+)-K(+)-ATPase, or sodium pump, is the membrane-bound enzyme that maintains the Na(+) and K(+) gradients across the plasma membrane of animal cells. Because of its importance in many basic and specialized cellular functions, this enzyme must be able to adapt to changing cellular and physiological stimuli. This review presents an overview of the many mechanisms in place to regulate sodium pump activity in a tissue-specific manner. These mechanisms include regulation by substrates, membrane-associated components such as cytoskeletal elements and the gamma-subunit, and circulating endogenous inhibitors as well as a variety of hormones, including corticosteroids, peptide hormones, and catecholamines. In addition, the review considers the effects of a range of specific intracellular signaling pathways involved in the regulation of pump activity and subcellular distribution, with particular consideration given to the effects of protein kinases and phosphatases.

Mechanisms of sodium pump regulation

Tubular reabsorption of filtered sodium is quantitatively the main contribution of kidneys to salt and water homeostasis The transcellular reabsorption of sodium proceeds by a two-step mechanism: 

https://www.physiology.org/doi/pdf/10.1152/physrev.2001.81.1.345

Sodium-Potassium-Adenosinetriphosphatase-Dependent Sodium Transport in the Kidney: Hormonal Control

—In the brain, pressure-induced myogenic constriction of cerebral arteriolar muscle contributes to autoregulation of cerebral blood flow (CBF). This study examined the role of 20-HETE in au...

Production of 20-HETE and Its Role in Autoregulation of Cerebral Blood Flow

It is well documented that the activity of Na+,K+-ATPase can be inhibited by the arachidonic acid metabolite, 20-hydroxyeicosa-tetraenoic acid (20 HETE). Evidence is presented here that this effect is mediated by protein kinase C (PKC). PKC inhibitors abolished 20 HETE inhibition of rat Na+,K+-ATPase in renal tubular cells. 20 HETE caused translocation of PKC alpha from cytoplasm to membrane in COS cells. It also inhibited Na+,K+-ATPase activity in COS cells transfected with rat wild-type renal Na+,K+-ATPase alpha1 subunit, but not in cells transfected with Na+,K+-ATPase alpha1, where the PKC phosphorylation site, serine 23, had been mutated to alanine. PKC-induced phosphorylation of rat renal Na+,K+-ATPase, as well as of histone was strongly enhanced by 20 HETE at the physiologic calcium concentration of 1.3 microM, but not at the calcium concentration of 200 microM. The results indicate that phospholipase A2-arachidonic acid-20 HETE pathway can exert important biological effects via activation of PKC and that this effect may occur in the absence of a rise in intracellular calcium.

/pdf/20-hydroxyeicosa-tetraenoic-acid-20-hete-activates-protein-1jermxruln.pdf

20-Hydroxyeicosa-tetraenoic acid (20 HETE) activates protein kinase C. Role in regulation of rat renal Na+,K+-ATPase.

1. It is well established that the activity of Na+,K+-ATPase (NKA) is regulated by protein kinases A (PKA) and C (PKC), but results on their effects have been conflicting. The aim of this study was to examine if this is ascribed to the intracellular concentration of Ca2+ ([Ca2+]i). 2. Rat renal NKA was stably expressed in COS cells (green monkey kidney cells). Increases in [Ca2+]i were achieved with the Ca2+ ionophore A23187 and verified by direct measurements of [Ca2+]i using fura-2 AM as an indicator. The activity of NKA was measured as ouabain-sensitive 86Rb+ uptake and the state of phosphorylation of NKA was monitored with two site-directed phosphorylation state-specific antibodies. 3. Activation of PKA with forskolin decreased NKA activity by 45.5 +/- 8.9 % at low [Ca2+]i (120 nM) and increased it by 40.5 +/- 6.4 % at high [Ca2+]i (420 nM). The change in NKA activity by forskolin correlated with the level of increase in [Ca2+]i. 4. The effect of 1-oleoyl-2-acetoyl-sn-glycerol (OAG), a specific PKC activator, on the activity of NKA was also Ca2+ dependent, being inhibitory when [Ca2+]i was low (29.3 +/- 3.6 % decrease at 120 nM Ca2+) and stimulatory when [Ca2+]i was high (36.6 +/- 10.1 % increase at 420 nM Ca2+). 5. The alpha subunit of NKA was phosphorylated under both low and high [Ca2+]i conditions upon PKA or PKC activation. PKA phosphorylates Ser943. PKC phosphorylates Ser23. 6. To see if the observed effects on NKA activity are secondary to changes in Na+ entry, we measured NKA hydrolytic activity using permeabilized membranes isolated from cells under controlled Na+ conditions. A decreased activity at low [Ca2+]i and no change in activity at high [Ca2+]i were observed following forskolin or OAG treatment. 7. Purified NKA from rat renal cortex was phosphorylated and inhibited by PKC. This phosphorylation-associated inhibition of NKA was neither affected by Ca2+ nor by calmodulin, tested alone or together. 8. We conclude that effect of PKA/PKC on NKA activity is dependent on [Ca2+]i. This Ca2+ dependence may provide an explanation for the diversity of responses of NKA to activation of either PKA or PKC.

https://physoc.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1469-7793.1999.0037r.x

[Ca2+]i determines the effects of protein kinases A and C on activity of rat renal Na+,K+‐ATPase

The kidney maintains electrolyte and fluid balance with great precision. Under basal conditions, almost all filtered Na+ is reabsorbed in the renal tubules. The Na+,K+-ATPase pump, localized to the basolateral membranes, is the active step of this process, providing the energy for the vectorial transport of electrolytes and solutes across the epithelial cells at the cost of ATP hydrolysis. Na+ reabsorption is a dynamic process under the influence of local and humoral factors which can cause several-fold variations in Na+ excretion. Imperfect regulation of Na+ homeostasis results in disturbances in electrolyte balance of significant clinical importance. Revealing the molecular mechanisms underlying the regulation of natriuresis is of prime importance in understanding the pathogenesis o,f and directing specific therapy for, diseases such as hypertension. Here we present a model in which a cascade of intracellular events results in a bidirectional modulation of Na+,K+-ATPase activity through regulation of its phosphorylation and dephosphorylation.

Hormonal regulation of Na+,K+-ATPase activity

S.04.03 Allosteric changes of the NMDA receptor trap diffusible dopamine 1 receptors in spines

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20-Hydroxyeicosa-tetraenoic acid (20 HETE) activates protein kinase C. Role in regulation of rat renal Na+,K+-ATPase.

[Ca2+]i determines the effects of protein kinases A and C on activity of rat renal Na+,K+‐ATPase

Hormonal regulation of Na+,K+-ATPase activity

S.04.03 Allosteric changes of the NMDA receptor trap diffusible dopamine 1 receptors in spines