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Last update 08 May 2025

renin receptor

Last update 08 May 2025

Basic Info

Synonyms

APT6M8-9, ATP6AP2, ATP6IP2

+ [18]

Introduction

Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (PubMed:12045255, PubMed:29127204, PubMed:30374053, PubMed:32276428). May mediate renin-dependent cellular responses by activating ERK1 and ERK2 (PubMed:12045255). By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS) (PubMed:12045255). Through its function in V-type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission (By similarity).

Drugs associated with renin receptor

BNC-1601

Target

renin receptor

Mechanism

renin receptor inhibitors

Active Org.

BONAC Corp.

Originator Org.

BONAC Corp.

Active Indication

Dystrophy, Macular [+2]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with renin receptor

100 Translational Medicine associated with renin receptor

0 Patents (Medical) associated with renin receptor

272

Literatures (Medical) associated with renin receptor

01 May 2025·Animal Reproduction Science

The surface proteome of rabbit spermatozoa

Article

Author: Impens, Francis ; Pinto-Pinho, Patrícia ; Fardilha, Margarida ; Colaço, Bruno ; Dufour, Sara ; Pinto-Leite, Rosário ; Howl, John ; Van Haver, Delphi

Cell surface proteins, targeted by approximately 70 % of current pharmaceuticals, offer promising prospects for therapeutic and biotechnological advancements. The recent identification of cell surface proteins, differentially expressed by rabbit spermatozoa, could support technologies to enable sperm sex selection. However, a more detailed knowledge of the rabbit sperm plasma membrane proteome is crucial to such developments. Hence, the primary objective of this study was to conduct a shotgun proteomic (LC-MS/MS) analysis of New Zealand White rabbit spermatozoa protein lysates enriched in cell surface proteins isolated through biotinylation. This approach was designed to provide an overall characterization of this proteome and so determine an expanded list of protein candidates with potential for rabbit sperm sexing. The most promising targets were identified through functional annotation (UniProt and eggNOG-mapper v.2.1.9) and topology prediction (DeepTMHMM v.1.0.13). Additionally, a statistical overrepresentation test (PANTHER 18.0) and analysis of protein-protein interactions (STRING v.12.0) were conducted. Among the 859 detected proteins, 803 had Gene Ontology information, with 574 predicted as globular proteins, 152 as transmembrane proteins, and 133 possessing only a signal peptide. The combined data identified 107 proteins as potential cell surface targets, including three transmembrane proteins encoded by the X chromosome (ADGRG2, ATP6AP2, and VSIG1). Furthermore, two proteins (BCAP31 and PGRMC1), previously identified as putative rabbit X-targets, were recognized. This study enhances our comprehension of rabbit spermatozoa proteomics. Further validation of the utility of these five proteins to differentiate between X- and Y-sperm will determine their suitability for integration into sperm sexing technologies.

01 Feb 2025·American Journal of Physiology-Renal Physiology

Soluble (pro)renin receptor as a novel regulator of renal medullary Na⁺ reabsorption

Review

Author: Mao, Zi-Hui ; Wu, Peng ; Yang, Tianxin ; Gao, Zhong-Xiuzi

Epithelial sodium channel (ENaC) represents a major route of Na+ reabsorption in the aldosterone-sensitive distal nephron where the bulk of ENaC activity is considered to occur in the cortical collecting duct (CCD). Relatively, ENaC activity in the medulla, especially the inner medulla, is often neglected. (Pro)renin receptor (PRR), also termed ATP6ap2, a newly characterized member of the renin-angiotensin system, has emerged as an important regulator of ENaC in the distal nephron. The ENaC regulatory action of PRR is largely mediated by the 28 kDa soluble PRR (sPRR). Although all three subunits of ENaC are under the control of aldosterone, sPRR only mediates the upregulation of α-ENaC but not the other two subunits. Furthermore, sPRR-dependent regulation of α-ENaC only occurs in the renal inner medulla but not in the cortex. sPRR also rapidly upregulates ENaC activity via Nox4-derived H2O2. Overall, sPRR has emerged as an important regulator of renal medullary Na+ reabsorption in the context of overactivation of the renin-angiotensin-aldosterone system.

01 Dec 2024·Clinical Proteomics

Biomarker discovery in progressive supranuclear palsy from human cerebrospinal fluid

Article

Author: Tropea, Thomas F. ; Hall, Anna J. ; Jang, Yura ; Dawson, Ted M ; Na, Chan Hyun ; Pantelyat, Alexander Y ; Rosenthal, Liana S ; Pantelyat, Alexander Y. ; Hall, Anna J ; Zhang, Zhen ; Oh, Sungtaek ; Tropea, Thomas F ; Dawson, Ted M. ; Chen-Plotkin, Alice ; Rosenthal, Liana S.

AbstractBackgroundProgressive supranuclear palsy (PSP) is a neurodegenerative disorder often misdiagnosed as Parkinson’s Disease (PD) due to shared symptoms. PSP is characterized by the accumulation of tau protein in specific brain regions, leading to loss of balance, gaze impairment, and dementia. Diagnosing PSP is challenging, and there is a significant demand for reliable biomarkers. Existing biomarkers, including tau protein and neurofilament light chain (NfL) levels in cerebrospinal fluid (CSF), show inconsistencies in distinguishing PSP from other neurodegenerative disorders. Therefore, the development of new biomarkers for PSP is imperative.MethodsWe conducted an extensive proteome analysis of CSF samples from 40 PSP patients, 40 PD patients, and 40 healthy controls (HC) using tandem mass tag-based quantification. Mass spectrometry analysis of 120 CSF samples was performed across 13 batches of 11-plex TMT experiments, with data normalization to reduce batch effects. Pathway, interactome, cell-type-specific enrichment, and bootstrap receiver operating characteristic analyses were performed to identify key candidate biomarkers.ResultsWe identified a total of 3,653 unique proteins. Our analysis revealed 190, 152, and 247 differentially expressed proteins in comparisons of PSP vs. HC, PSP vs. PD, and PSP vs. both PD and HC, respectively. Gene set enrichment and interactome analysis of the differentially expressed proteins in PSP CSF showed their involvement in cell adhesion, cholesterol metabolism, and glycan biosynthesis. Cell-type enrichment analysis indicated a predominance of neuronally-derived proteins among the differentially expressed proteins. The potential biomarker classification performance demonstrated that ATP6AP2 (reduced in PSP) had the highest AUC (0.922), followed by NEFM, EFEMP2, LAMP2, CHST12, FAT2, B4GALT1, LCAT, CBLN3, FSTL5, ATP6AP1, and GGH.ConclusionBiomarker candidate proteins ATP6AP2, NEFM, and CHI3L1 were identified as key differentiators of PSP from the other groups. This study represents the first large-scale use of mass spectrometry-based proteome analysis to identify cerebrospinal fluid (CSF) biomarkers specific to progressive supranuclear palsy (PSP) that can differentiate it from Parkinson’s disease (PD) and healthy controls. Our findings lay a crucial foundation for the development and validation of reliable biomarkers, which will enhance diagnostic accuracy and facilitate early detection of PSP.

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renin receptor

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