Low-dose angiotensin AT1 receptor β-arrestin-biased ligand, TRV027, protects against cisplatin-induced nephrotoxicity

Esmaeeli, Abdolhamid; Ebrahimi, Fatemeh; Tanha, Kaveh; Assadi, Majid; Seyedabadi, Mohammad

doi:10.1007/s43440-020-00172-5

Cited by 5 publications

(2 citation statements)

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“…In this case, another level of complexity will be added to the capacity of GPCR signaling. In particular, a given GPCR may signal through several transducers, including multiple G proteins and two non-visual arrestins, and the capacity of a biased ligand to direct a signal one way over another is a hot topic in the discovery of GPCR-targeting drugs [83,146,147]. If different conformations of arrestin when bound to differentially phosphorylated receptors result in distinct biological outcomes, there is one more way to create signaling selectivity at this junction, suggesting how pharmacological intervention can direct a signal in favor of or away from particular pathways.…”

Section: Receptor-attached Phosphates In Arrestin Bindingmentioning

confidence: 99%

Receptor-Arrestin Interactions: The GPCR Perspective

et al. 2021

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Arrestins are a small family of four proteins in most vertebrates that bind hundreds of different G protein-coupled receptors (GPCRs). Arrestin binding to a GPCR has at least three functions: precluding further receptor coupling to G proteins, facilitating receptor internalization, and initiating distinct arrestin-mediated signaling. The molecular mechanism of arrestin–GPCR interactions has been extensively studied and discussed from the “arrestin perspective”, focusing on the roles of arrestin elements in receptor binding. Here, we discuss this phenomenon from the “receptor perspective”, focusing on the receptor elements involved in arrestin binding and emphasizing existing gaps in our knowledge that need to be filled. It is vitally important to understand the role of receptor elements in arrestin activation and how the interaction of each of these elements with arrestin contributes to the latter’s transition to the high-affinity binding state. A more precise knowledge of the molecular mechanisms of arrestin activation is needed to enable the construction of arrestin mutants with desired functional characteristics.

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Section: Receptor-attached Phosphates In Arrestin Bindingmentioning

confidence: 99%

Receptor-Arrestin Interactions: The GPCR Perspective

et al. 2021

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“…71 Administration of TRV027 in cisplatin-induced acute kidney injury reduced BUN and creatinine levels and alleviated excess sodium excretion. 72 Interestingly, TRV027 had more beneficial effects than 2 different ARBs, suggesting that preservation of β-arrestin axis can be protective in cisplatin nephrotoxicity.…”

Section: At 1 R β-Arrestin and Renal Diseasementioning

confidence: 99%

Insights Into the Role of Angiotensin-II AT ₁ Receptor-Dependent β-Arrestin Signaling in Cardiovascular Disease

2024

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β-arrestins are a family of intracellular signaling proteins that play a key role in regulating the activity of G protein-coupled receptors. The angiotensin-II type 1 receptor is an important G protein-coupled receptor involved in the regulation of cardiovascular function and has been implicated in the progression of cardiovascular diseases. In addition to canonical G protein signaling, G protein-coupled receptors including the angiotensin-II type 1 receptor can signal via β-arrestin. Dysregulation of β-arrestin signaling has been linked to several cardiovascular diseases including hypertension, atherosclerosis, and heart failure. Understanding the role of β-arrestins in these conditions is critical to provide new therapeutic targets for the treatment of cardiovascular disease. In this review, we will discuss the beneficial and maladaptive physiological outcomes of angiotensin-II type 1 receptor-dependent β-arrestin activation in different cardiovascular diseases.

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Structural basis of GPCR coupling to distinct signal transducers: implications for biased signaling

Seyedabadi

Gharghabi

Gurevich

et al. 2022

Trends in Biochemical Sciences

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Low-dose angiotensin AT1 receptor β-arrestin-biased ligand, TRV027, protects against cisplatin-induced nephrotoxicity

Cited by 5 publications

References 45 publications

Receptor-Arrestin Interactions: The GPCR Perspective

Receptor-Arrestin Interactions: The GPCR Perspective

Insights Into the Role of Angiotensin-II AT ₁ Receptor-Dependent β-Arrestin Signaling in Cardiovascular Disease

Structural basis of GPCR coupling to distinct signal transducers: implications for biased signaling

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Low-dose angiotensin AT1 receptor β-arrestin-biased ligand, TRV027, protects against cisplatin-induced nephrotoxicity

Cited by 5 publications

References 45 publications

Receptor-Arrestin Interactions: The GPCR Perspective

Receptor-Arrestin Interactions: The GPCR Perspective

Insights Into the Role of Angiotensin-II AT 1 Receptor-Dependent β-Arrestin Signaling in Cardiovascular Disease

Structural basis of GPCR coupling to distinct signal transducers: implications for biased signaling

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Insights Into the Role of Angiotensin-II AT ₁ Receptor-Dependent β-Arrestin Signaling in Cardiovascular Disease