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Last update 08 May 2025

ATP2A1

Last update 08 May 2025

Basic Info

Synonyms

ATP2A, ATP2A1, ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 1

+ [7]

Introduction

Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (By similarity). Contributes to calcium sequestration involved in muscular excitation/contraction (PubMed:10914677).

Drugs associated with ATP2A1

Artesunate/Pyronaridine Phosphate

Target

ATP2A1 x SERCA2

Mechanism

ATP2A1 inhibitors [+1]

Active Org.

Shinpoong Pharmaceutical Co., Ltd. ESOA

Originator Org.

Shinpoong Pharmaceutical Co., Ltd. ESOA

Active Indication

Malaria

Inactive Indication

Malaria, Falciparum [+1]

Drug Highest PhaseApproved

First Approval Ctry. / Loc.

South Korea

First Approval Date17 Aug 2011

Artesunate/Mefloquine Hydrochloride

Target

ATP2A1 x SERCA2

Mechanism

ATP2A1 inhibitors [+1]

Active Org.

Fundação Oswaldo Cruz

Originator Org.

Fundação Oswaldo Cruz

Active Indication

Malaria, Falciparum [+1]

Inactive Indication-

Drug Highest PhaseApproved

First Approval Ctry. / Loc.

Brazil

First Approval Date01 Jan 2008

Artemether/Lumefantrine

Target

ATP2A1 x SERCA2

Mechanism

ATP2A1 inhibitors [+1]

Active Org.

Novartis Pharmaceuticals Australia Pty Ltd. [+4]

Originator Org.

Novartis Pharma AG

Active Indication

Acute Malaria [+1]

Inactive Indication

Malaria, Falciparum

Drug Highest PhaseApproved

First Approval Ctry. / Loc.

China

First Approval Date01 Jan 1992

527

Clinical Trials associated with ATP2A1

NCT06872112

/ Not yet recruitingPhase 1IIT

Phase I Study: a Dose-Escalation Study Evaluating the Safety and Tolerability of Artesunate in Patients with Pulmonary Arterial Hypertension

This is a 20-week, Phase 1, single-center, open-label, dose-escalation study evaluating the safety and tolerability of daily oral artesunate in patients with PAH.

Start Date01 Jan 2026

Sponsor / Collaborator

Stanford University

NCT06869850

/ Not yet recruitingNot ApplicableIIT

MFGM-EnhaNceD RUTF for Children With SAM

The goal of this clinical trial is to test the use of milk fat globule membrane (MFGM) in ready-to-use therapeutic food (RUTF) in children with severe acute malnutrition in Sierra Leone. The main questions it aims to answer are:
* Will the inclusion of MFGM in RUTF for 6-59-month-old Sierra Leonean children with severe acute malnutrition improve their neurodevelopment?
* Will the inclusion of MFGM in RUTF for 6-59-month-old Sierra Leonean children with severe acute malnutrition reduce its worst consequences: death, hospitalization, and remaining severely malnourished despite treatment?
Researchers will compare the MFGM-containing RUTF to standard RUTF, which contains skim milk powder.
Participants will:
* undergo measurement of length, weight, mid-upper arm circumference, and nutritional edema assessment every two weeks during severe malnutrition treatment
* be treated with either MFGM-RUTF or standard RUTF at a dose of 2 sachets per day for up to 12 weeks
* undergo neurodevelopmental testing using the Malawi Developmental Assessment Tool at the end of SAM treatment and 6 months later
* a subset of participants will undergo blood spot collection and stool sample collection

Start Date01 Jul 2025

Sponsor / Collaborator

Washington University School of Medicine

[+1]

NCT05441410

/ Not yet recruitingPhase 1/2IIT

Comparing Safety and Protective Efficacy of the Whole Plasmodium Falciparum Sporozoite Chemoprophylaxis Vaccine Candidate PfSPZ-CVac and Prime- Target Vaccination with Viral Vectored Vaccine Candidate Regime MVA ME-TRAP/ ChAd63 ME-TRAP in Malaria-naïve, Healthy Adult Volunteers in Germany

This is a single centre, randomized, placebo-controlled phase 1/2 study comparing two malaria vaccine candidates. The first vaccine candidate PfSPZ-CVac (Plasmodium falciparum sporozoites (PfSPZ) challenge administered with a chemoprophylactic antimalarial) will be chemoattenuated in vivo with the antimalarial Pyramax. The second vaccine candidate is prime- target vaccination with viral vectored vaccine candidate regime MVA ME-TRAP (Modified Vaccinia Ankara (MVA) multiple epitope thrombosponin-related adhesion protein (ME-TRAP)) and ChAd63 ME-TRAP (Chimpanzee adenovirus 63 (ChAd63). The safety and protective efficacy of both vaccine candidates will be to assessed by controlled human malaria infection with PfSPZ Challenge strain NF54 administered intravenously by syringe.

Start Date01 Jun 2025

Sponsor / Collaborator

University Hospital Tübingen

[+2]

100 Clinical Results associated with ATP2A1

100 Translational Medicine associated with ATP2A1

0 Patents (Medical) associated with ATP2A1

467

Literatures (Medical) associated with ATP2A1

02 Apr 2025·Journal of Agricultural and Food Chemistry

Protein Aggregation during Storage of Roe Deer Meat: a Proteomic Study

Article

Author: Fornal, Emilia ; Stachniuk, Anna ; Montowska, Magdalena ; Kasałka-Czarna, Natalia

Understanding the biochemical changes associated with protein aggregation in meat during storage is critical to improving food safety, quality assurance, and consumer satisfaction in the global meat market. The study evaluated oxygen-induced protein aggregation in the meat of European roe deer (Capreolus capreolus) stored for up to 21 days under refrigeration. Three packaging methods were compared: modified atmosphere packaging with two different gas compositions (MAP(1): 80% O₂/20% CO₂ and MAP(2): 40% CO₂/60% N₂) and vacuum packaging (VAC). Additionally, meat dry aging (DA) was included in the study for comparison. Structural proteins most susceptible to aggregation included titin isoform X1 and myosin 1 isoform X1, and among sarcoplasmic proteins, sarcoplasmic/endoplasmic reticulum calcium ATPase 1 isoform X1. In addition, specific proteins involved in aggregate formation under high oxygen conditions were identified, mainly nebulin, isocitrate dehydrogenase, glyceraldehyde phosphate dehydrogenase, and creatine kinase. The extent of their aggregation varied with the type of muscle analyzed, with the most pronounced changes observed in MAP(1) after 21 days. Oxidation plays a crucial role in determining meat quality and shelf life; based on our findings, VAC is recommended for roe deer meat storage.

01 Apr 2025·Journal of Cachexia, Sarcopenia and Muscle

Calcium Handling Machinery and Sarcomere Assembly are Impaired Through Multipronged Mechanisms in Cancer Cytokine‐Induced Cachexia

Article

Author: Pich, Andreas ; Nayak, Arnab ; Li, Mugeng ; Bär, Christian ; Gand, Luis Vincens ; Kraft, Theresia ; Weber, Natalie ; Amrute‐Nayak, Mamta ; Lu, Dongchao ; Thum, Thomas ; Lanzuolo, Chiara ; Rosti, Valentina

AbstractBackgroundCachexia is a severe form of muscle wasting disorder particularly observed in patients with advanced cancer. The absence of effective strategies to ameliorate cachexia indicates our poor understanding of the mechanisms of cachexia. By employing system‐wide approaches, we investigated molecular mechanisms underlying cancer secreted pro‐inflammatory cytokine‐induced cachexia (CIC).MethodsAs cellular model systems, we employed mouse satellite stem cell‐derived primary muscle cells, mouse C2C12 myoblast progenitor cell‐derived myotubes, and neonatal rat cardiomyocytes. We induced CIC by incubating striated muscle cells with pro‐inflammatory cytokines TNF‐α and IFN‐γ. To understand the physiological effects of CIC, we probed the contractile properties of muscle cells following electrical stimulation and measured intracellular calcium transients. Effects of CIC on sarcomere organization were monitored by confocal microscopy. Large‐scale quantitative proteomics and RNA sequencing assays enabled us to examine molecular mechanisms underlying CIC. Using chromatin immunoprecipitation experiments, chromatin signalling and modulation of epigenetic marks on muscle‐specific genes were investigated.ResultsHere, we observed a drastic loss of striated muscle cell contraction in CIC, primarily, due to acutely disorganized sarcomere structures and impeded calcium handling process. In calcium transients, the extent of calcium (Ca2+) release, as indicated by the calcium amplitude during the excitation–contraction coupling (ECC) process, was reduced (19.6 ± 2.35% in control to 8.6 ± 1.52% in CIC, p = 4.8 * 10−11). Kinetics of calcium transients, i.e., the Ca2+ release rate (26 ± 0.5 ms in control to 29 ± 5.1 ms in CIC, median p = 0.014), and calcium re‐uptake rate (137 ± 13 ms in control to 185 ± 24 ms in CIC, p = 0.032) were both prolonged. Proteomic analysis showed altered proteostasis in CIC, particularly related to sarcomere and sarcoplasmic reticulum (SR). Transcriptomic analysis unravelled upstream deregulation of global transcriptional events for sarcomeric and SR genes. Mechanistically, chromatin loading of transcriptionally active RNA Polymerase II on muscle‐specific genes, including Myh1 and Atp2a1, was impeded. This was due to diminished transcriptionally active epigenetic marks H3K4 trimethylation on Myh1 and Atp2a1, resulted in lower transcriptional activity of these muscle‐specific genes in CIC and ultimately reduced MyHC‐IId molecular motor protein and SERCA1 protein levels.ConclusionsOur top‐down approach elucidated that the altered transcriptional mechanism and proteomic state perturbed functionally related machinery responsible for calcium handling and sarcomere organization in CIC. Knowledge of the underlying cause of muscle mass loss and compromised muscle function is key for developing therapeutic solutions to ameliorate cachectic conditions.

01 Mar 2025·Journal of Biological Chemistry

The juxtamembrane sequence of small ankyrin 1 mediates the binding of its cytoplasmic domain to SERCA1 and is required for inhibitory activity

Article

Author: Bloch, Robert J ; Li, Yi ; Wright, Nathan T

Sarcoplasmic/endoplasmic reticulum Ca²⁺-ATPase1 (SERCA1) is responsible for the clearance of cytosolic Ca²⁺ in skeletal muscle. Due to its vital importance in regulating Ca²⁺ homeostasis, the regulation of SERCA1 has been intensively studied. Small ankyrin 1 (sAnk1, Ank1.5), a 17 kDa muscle-specific isoform of ANK1, binds to SERCA1 directly via both its transmembrane and cytoplasmic domains and inhibits SERCA1's ATPase activity. Here, we characterize the interaction between the cytoplasmic domain of sAnk1 (sAnk1(29-155)) and SERCA1. The binding affinity for sAnk1 (29-155) to SERCA1 was 444 nM by blot overlay, about 7-fold weaker than the binding of sAnk1(29-155) to obscurin, a giant protein of the muscle cytoskeleton. Site-directed mutagenesis identified K38, H39, and H41, in the juxtamembrane region, as residues likely to mediate binding to SERCA1. These residues are not required for obscurin binding. Residues R64-K73, which do contribute to obscurin binding, are also required for binding to SERCA1, but only the hydrophobic residues in this sequence are required, not the positively charged residues necessary for obscurin binding. Circular dichroism analysis of sAnk1(29-155) indicates that most mutants show significant structural changes, with the exception of those containing alanines in place of K38, H39 and H41. Although the cytoplasmic domain of sAnk1 does not inhibit SERCA1's Ca²⁺-ATPase activity, with or without mutations in the juxtamembrane sequence, the inhibitory activity of full-length sAnk1 requires the WT juxtamembrane sequence. We used these data to model sAnk1 and the sAnk1-SERCA1 complex. Our results suggest that, in addition to its transmembrane domain, sAnk1 uses its juxtamembrane sequence and perhaps part of its obscurin binding site to bind to SERCA1, and that this binding contributes to their robust association in situ, as well as regulation of SERCA1's activity.

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ATP2A1

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