SERCA1
- Known as:
- SERCA1
- Catalog number:
- 000388A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- SERCA1
Related genes to: SERCA1
- Gene:
- ATP2A1 NIH gene
- Name:
- ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 1
- Previous symbol:
- ATP2A
- Synonyms:
- SERCA1
- Chromosome:
- 16p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1990-09-10
- Date modifiied:
- 2016-10-05
Related products to: SERCA1
Related articles to: SERCA1
- The calcium ion (Ca) is a fundamental intracellular messenger involved in the transduction of diverse receptor signaling pathways. Transient increases in cytoplasmic Ca concentration ([Ca]) regulate many cellular functions, including the contraction of vascular smooth muscle cells (VSMCs), which are active components of the blood vessels. A key protein in intracellular Ca handling is the sarco/endoplasmic reticulum (SR/ER) Ca ATPase, or SERCA pump. This transmembrane protein belongs to the P-type ATPase family and uses energy from ATP hydrolysis to transport Ca from the cytoplasm into intracellular reservoirs within the SR of VSMCs. By lowering [Ca], SERCA activity promotes vasorelaxation. In mammals, three genes, ATP2A1, ATP2A2, and ATP2A3, encode at least twelve SERCA pump isoforms. Alternative mRNA splicing is the primary mechanism for generating most isoforms, leading to tissue-specific expression patterns. In VSMCs from the aorta and mesenteric arteries, the expression of SERCA2a, SERCA2b, and, more recently, SERCA3 has been reported. This chapter will review the structure, mechanism of action, and physiological role of the SERCA pump in the intracellular Ca handling of VSMCs, as well as its alterations in metabolic syndrome. - Source: PubMed
Publication date: 2026/05/12
Arriero-Carrillo Cristian JRueda Angélica - Skeletal muscle is a fundamental tissue as it is found throughout the body, sustains posture, and produces movement. Yet, skeletal muscle disorders, such as myopathies, affect a large percentage of the population, degrading an individual's quality of life. A recent study links myopathy progression to the decline in chaperone-mediated autophagy that occurs during aging. Underscoring the importance of a balanced CMA pathway in maintaining skeletal muscle function and integrity, the study also provides mechanistic insights into the pathways that are dysregulated due to defective CMA and presents an approach to reverse the age-dependent decline in this process.: ATP2A1, ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 1; CMA, chaperone-mediated autophagy; HSPA8, heat shock protein family A (Hsp70) member 8; LAMP2A, lysosomal associated membrane protein 2A. - Source: PubMed
Publication date: 2026/04/19
Dialynaki DimitraKlionsky Daniel J - The sarco-/endoplasmatic reticulum calcium ATPase (SERCA) is a calcium transporter that plays a key role in the excitation-contraction-relaxation cycle by enabling muscle relaxation. Pathogenic variants in the SERCA-encoding gene cause Brody disease, a rare recessive myopathy with exercise-induced muscle stiffness as the main feature. Measurement of SERCA activity is an important in vitro functional assay to aid in confirming the pathogenicity of variants in this gene. Furthermore, measurement of SERCA activity is used to study physiological and pathological excitation-contraction (de)coupling. For both, a robust assay is of the utmost importance. We aimed to fully reassess the SERCA activity assay, establish new reference values, and validate the assay by measurement of Brody disease muscle samples. All different SERCA assay parameters were extensively re-evaluated and optimized, including time linearity, the effect of sonication and pH, and the effects of homogenate, KCl/Imidazole, ATP, MgCl, and CaCl concentrations. With the optimized assay, SERCA activity was assessed in muscle samples from healthy controls ( = 28) and patients with Brody disease ( = 4). We were able to provide new reference values and demonstrate marked decreased SERCA activity in Brody disease muscle samples (30.0 ± 4.2 mU/mg protein) compared to controls (86.7 ± 25.1 mU/mg protein). We developed a robust enzyme assay to measure SERCA activity with high discriminative power to distinguish patients with Brody disease from controls. Thus, this assay provides a reliable method of studying this important calcium pump for both clinical and scientific purposes. - Source: PubMed
Publication date: 2026/03/24
Molenaar J PSnoeck M MTreves SStoltenborg B JWethly K COosterhof AKamsteeg E JSternberg DDoorduin Jvan Engelen B GVoermans N CRodenburg R J - Brody myopathy is a rare autosomal recessive disorder caused by mutations in the ATP2A1 gene, which encodes for sarcoplasmic reticulum Ca++-ATPase (SERCA1) pump in the fast twitch skeletal muscle fibers. - Source: PubMed
Publication date: 2026/04/01
Edmund Sara - Paeoniae Radix Alba Carbonisata (PRAC), carbonized decoction pieces of the traditional Chinese medicine Paeoniae Radix Alba, has been used in clinical practice for hepatoprotective purposes. Hepatic amyloidosis (HA), a severe complication of systemic AA amyloidosis, is characterized by the deposition of fibrillar amyloid proteins leading to progressive hepatic dysfunction. However, its role in HA remains unclear. Amyloid lysozyme (LYSO-6) was used to induce the NCTC1469 cell injury model and the HA mouse model. The effects of PRAC extract (PRAC-E) on liver injury were then evaluated using biochemical assays, enzyme-linked immunosorbent assay (ELISA), Congo red (CR) staining, Hematoxylin and Eosin (H&E) staining, and immunohistochemical staining. Liver transcriptomics combined with Western blotting was used to analyze the expression levels of key proteins in the cGMP/PKG/ATP2A1 signaling axis. UHPLC-Q-Exactive Orbitrap MS combined with network pharmacology was used to characterize the chemical components of PRAC-E and identify its core active constituents against HA. Quantitative analysis of core components was performed by UHPLC-QTRAP-MS/MS. Molecular docking predicted the binding stability of core components and key targets. The results showed that PRAC-E significantly alleviated HA. Collectively, PRAC-E restored calcium pump activity, corrected calcium homeostasis imbalance, reduced inflammatory factor levels, regulated Phosphodiesterase 5A (PDE5A), and activated the cGMP/PKG/ATP2A1 signaling axis. The main components of PRAC-E were phenolic acids, terpenoids, and flavonoids. Among these, six core components (SCCs) related to HA were Gallate (16.96 mg/g), Paeoniflorin (14.27 mg/g), Albiflorin (7.20 mg/g), Benzoyl paeoniflorin (5.33 mg/g), Methyl gallate (0.78 mg/g), and Catechin (0.09 mg/g). Molecular docking analysis demonstrated that SCCs formed stable complexes (∆ ≤ -6.2 kcal/mol) with ATP2A1. - Source: PubMed
Publication date: 2026/03/11
Liu GangqiangWang ZeruiXu HuihuiJia JinyuXue ZhongGe WeiJi XueqingCui LijianHuang Yun