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01:33Hormonal Regulation
The renin-aldosterone system is an endocrine system which guides the renal absorption of water and electrolytes, thus managing blood pressure and osmoregulation. Activation of the system begins in the kidneys with a small cluster of cells adjacent to the afferent and efferent blood vessels of the renal corpuscle. As the nephrons are filtering blood, juxtaglomerular cells monitor blood pressure. If they detect a decrease in pressure, they release the hormone renin into the bloodstream.
01:26Adrenergic Receptors: β Subtype
β-adrenoceptors have varied sensitivities towards adrenaline, noradrenaline, and isoprenaline. The order of agonist potency is as follows:
Isoprenaline > Adrenaline > Noradrenaline
Neurotransmitter binding to these receptors causes activation of adenylyl cyclase resulting in increased concentrations of cAMP and modulation of calcium ion channels within the cell. They are further classified into β1, β2, and β3 subtypes.
β1-adrenoceptors: β1-adrenoceptors have equal affinities for...
Isoprenaline > Adrenaline > Noradrenaline
Neurotransmitter binding to these receptors causes activation of adenylyl cyclase resulting in increased concentrations of cAMP and modulation of calcium ion channels within the cell. They are further classified into β1, β2, and β3 subtypes.
β1-adrenoceptors: β1-adrenoceptors have equal affinities for...
01:27Transducer Mechanism: Enzyme-Linked Receptors
Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Major types that are helpful drug targets include:
01:31Adrenergic Receptors: ɑ Subtype
Adrenoceptors are classified into α and ꞵ classes based on their potencies to catecholamine agonists. α-adrenoceptors show the following order of catecholamine potency:
Adrenaline ≥ Noradrenaline >> Isoprenaline
α-adrenoceptors are further divided into α1 and α2-adrenoceptors.
α1-Adrenoceptors: These receptors are located postsynaptically on the effector organs and cause constriction of smooth muscle mediated by activation of phospholipase C—inositol-1,4,5-trisphosphate...
Adrenaline ≥ Noradrenaline >> Isoprenaline
α-adrenoceptors are further divided into α1 and α2-adrenoceptors.
α1-Adrenoceptors: These receptors are located postsynaptically on the effector organs and cause constriction of smooth muscle mediated by activation of phospholipase C—inositol-1,4,5-trisphosphate...
01:28Renal Drug Excretion: Tubular Secretion
Active tubular secretion is a robust, energy-demanding process that utilizes carrier systems to transport drugs into renal tubules. The active renal secretion systems include the organic anion transporter (OAT) for weak acids and the organic cation transporter (OCT) for weak bases. Structurally similar drugs can compete for the same transporter, potentially leading to drug accumulation and toxicity. However, this principle can be exploited therapeutically. One example is probenecid (Probalan),...
01:25Antihypertensive Drugs: Direct Renin Inhibitors
The renin-angiotensin-aldosterone system (RAAS) is an intricate physiological pathway involving numerous enzymes and hormones, including renin, angiotensin-converting enzyme (ACE), angiotensin I and II, and aldosterone. Imbalances within this system increase the production of angiotensin II and aldosterone. Increased angiotensin II levels promote vasoconstriction and blood pressure elevation. Concurrently, higher aldosterone levels stimulate sodium and water reabsorption in the kidneys,...
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12:03
Receptor Autoradiography Protocol for the Localized Visualization of Angiotensin II Receptors
Published on: June 7, 2016
(Pro)renin receptor: subcellular localizations and functions.
Gabin Sihn1, Celine Burckle, Anthony Rousselle
1Max-Delbrueck-Center for Molecular Medicine, Robert-Roessle-Strasse 10, D-13125 Berlin-Buch, Germany. g.sihn@mdc-berlin.de
Frontiers in Bioscience (Elite Edition)
|January 2, 2013
Summary
The (Pro)renin receptor ((P)RR) has evolved from a cell surface receptor to a protein with essential intracellular functions. Its precise cellular mechanisms remain elusive despite extensive research.
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Published on: March 27, 2017
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Published on: October 26, 2020
Area of Science:
- Cell Biology
- Molecular Biology
- Physiology
Background:
- The (Pro)renin receptor ((P)RR/ATP6ap2) was initially identified as a cell surface receptor.
- Emerging evidence suggests (P)RR has fundamental intracellular roles.
- Its predominantly intracellular localization challenges the initial understanding of its function.
Purpose of the Study:
- To review the known functions of (P)RR.
- To correlate these functions with the protein's subcellular localization.
- To discuss the evolving understanding of (P)RR's cellular roles.
Main Methods:
- Literature review of studies on (P)RR.
- Analysis of research findings, including those from genetically modified animal models.
- Discussion of subcellular localization data.
Main Results:
- (P)RR exhibits diverse functions beyond mediating (pro)renin effects.
- The protein is primarily localized intracellularly, suggesting non-canonical roles.
- Despite research, the exact cellular mechanisms of (P)RR are not fully elucidated.
Conclusions:
- The role of (P)RR has significantly shifted towards intracellular functions.
- Understanding (P)RR's subcellular localization is key to deciphering its mechanisms.
- Further research is needed to fully understand the basic cellular functions of (P)RR.