CPT1C
- Known as:
- CPT1C
- Catalog number:
- Y214248
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- CPT1C
Related genes to: CPT1C
- Gene:
- CPT1C NIH gene
- Name:
- carnitine palmitoyltransferase 1C
- Previous symbol:
- -
- Synonyms:
- FLJ23809, CPTIC, CPT1P
- Chromosome:
- 19q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 2003-11-27
- Date modifiied:
- 2015-09-11
Related products to: CPT1C
Antibodies: CPT1C HOST: Goat Clonality: pAbBovine Carnitine O-palmitoyltransferase 1, brain isoform(CPT1C) ELISA kitCanine Carnitine O-palmitoyltransferase 1, brain isoform(CPT1C) ELISA kitCanine Carnitine O-palmitoyltransferase 1, brain isoform(CPT1C) ELISA kitCarnitine O-palmitoyltransferase 1, brain isoform,Carnitine O-palmitoyltransferase I, brain isoform,Carnitine palmitoyltransferase 1C,CATL1,CPT IC,CPT1-B,CPT1C,CPTI-B,Homo sapiens,HumanCarnitine O-palmitoyltransferase 1, brain isoform,Carnitine O-palmitoyltransferase I, brain isoform,Carnitine palmitoyltransferase 1C,CPT IC,CPT1-B,Cpt1c,CPTI-B,Mouse,Mus musculusChicken Carnitine O-palmitoyltransferase 1, brain isoform(CPT1C) ELISA kitCPT1A Gene carnitine palmitoyltransferase 1A (liver)CPT1C CPT1-B antibody Ab host: GoatCPT1C CPT1-B (C-term) Ig antibody Ab host: RabbitCPT1C CPT1-B (C-term) Ig antibody Ab host: RabbitCPT1C AntibodyCPT1C (Human) Recombinant Protein (P01)CPT1C / CPT1-B antibody Isotype IgG Host GoatCPT1C / CPT1-B antibody Host Goat Related articles to: CPT1C
- - Source: PubMed
Publication date: 2026/04/13
- Aging poses a growing global health burden, creating an urgent need for effective interventions. This study reveals that fenofibrate, a clinically approved drug for hyperlipidemia, exerts significant anti-aging effects by targeting fundamental aging processes. We demonstrated that fenofibrate treatment delays systemic aging in D galactose-induced aging mice, 18-month-old mice and SAMP8 mice and reverses cellular senescence. Mechanistically, fenofibrate ameliorates age-related lipid accumulation, as evidenced by lipidomic profiling and histological analyses in both cellular and animal models. Notably, we identify carnitine palmitoyl transferase 1 C (CPT1C) as a crucial mediator of fenofibrate's ability to restore mitochondrial function in senescent cells, as validated by comprehensive metabolic analyses. Fenofibrate is a specific peroxisome proliferator activated receptor α (PPARα) agonist. These effects are mediated through PPARα activation, upregulating downstream metabolic regulators CPT1C. Fenofibrate cannot reverse aging in Pparα mice, establishing that its anti-aging effects are strictly PPARα-dependent. Our findings demonstrate that fenofibrate delays aging progression of mice and reverses cellular senescence in the PPARα-dependent way. Fenofibrate attenuates lipid accumulation and mitochondrial dysfunction in senescent cells and aged mice by activating the PPARα-CPT1C axis. This research provided the first evidence that pharmacological PPARα activation can directly modulate natural aging through coordinated improvement of lipid metabolism and mitochondrial function. The clinical relevance is underscored by the safety profile and widespread use of fenofibrate, suggesting its immediate potential as a repurposed anti-aging therapeutic. Furthermore, this work establishes PPARα as a master metabolic regulator of aging processes and reveals CPT1C as a novel therapeutic target for age-related metabolic dysfunction. - Source: PubMed
Publication date: 2026/02/27
Zhou YanyingChen YixinZhu LinlinLi HuilinGao YueXian TuZhao PengfeiFan ShichengCasals NúriaHuang MinBi Huichang - This work conducted a transcriptome analysis of canine intestinal epithelial cells (cIECs) treated with nicotinamide mononucleotide (NMN), a physiologically active nucleotide with a pyridine base known for its anti-aging and anti-inflammatory effects. In our experiment, cIECs were cultured and segregated into a control group (Ctrl) and an NMN-treated group. The finding demonstrated that NMN significantly affects cell proliferation in cIECs in comparison to the Ctrl. The transcriptome analysis indicated a high enrichment of genes associated with the cell cycle, proliferation, cellular senescence, and inflammatory pathways in NMN-treated cIECs, showing that NMN has the capacity to modify these biological processes. Compared to the Ctrl group, NMN treatment significantly increased ATP, SOD, CAT and GSH levels and decreased the activities of ROS and MDA. NMN treatment also significantly increased the activity of the relative complex I, III and V enzymes compared to the Ctrl group. Furthermore, the expression of , , , and were decreased significantly, while , , and were increased significantly in NMN-5μM treatment compared to Ctrl. NMN-treated significantly decreased the expression of , and , while increasing the expression of Kdm5a, Kdm5b and Kdm5c compared to the Ctrl group. Additionally, ChIP-qPCR use discovered that NMN-treatment significantly downregulated the enrichment of EDN-1 at target loci of , , , and compared to the Ctrl group. Expression of the gene suggests that its exert in biological activities by inhibiting inflammatory responses and anti-aging pathways. Then, we detected the transcriptional activation linked histone markers and found that and were significantly downregulated, while was significantly upregulated in the NMN-treatment compared to the Ctrl group. We conclude that NMN regulates EDN-1 expression in cIECs through mechanisms involving NR4A1 and histone modifications, highlighting its potential role in canine intestinal health. - Source: PubMed
Publication date: 2026/02/13
Guo XudongZhu ChuyangAdam Saber YZhu CuipengLiu Hao-YuCai Demin - Malonyl-CoA decarboxylase (MCD) is an enzyme that controls malonyl-CoA levels and regulates fatty acid synthesis and oxidation. Although its physiological relevance in peripheral tissues is well known, the role of MCD in the central nervous system remains poorly understood. MCD is expressed in mitochondria, cytosol, and peroxisomes and may be regulated by PPAR-α, AMPK, and SIRT4 in tissues such as muscle, liver and kidney. In the brain, MCD expression varies during development and can respond to nutritional states. Inherited MCD deficiency (malonic aciduria) leads to the toxic accumulation of malonic acid and predominantly affects the central nervous system. The underlying mechanisms leading to brain damage in MCD patients remain unclear. Conversely, pharmacological modulation of MCD activity has been studied in obesity, diabetes, and ischemic injury, highlighting its therapeutic potential. There are still major gaps regarding MCD cellular distribution, regulatory pathways, and metabolic interaction with CPT1c (carnitine palmitoyltransferase 1c) in neural metabolism. A deeper understanding of the role of MCD in brain physiology and pathology may indicate novel therapeutic strategies targeting metabolic disorders that involve altered malonyl-CoA dynamics. Here, we discuss the current knowns and unknowns regarding MCD physiology, regulation, and pathophysiology, emphasizing brain aspects. - Source: PubMed
Publication date: 2026/02/12
Fonseca-Teixeira MoniqueBrito Elaine SilvaBeltrao-Valente ClaraFerreira Bruna KlippelSchuck Patricia FernandaFerreira Gustavo Costa - Regulation of α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor (AMPAR) function has emerged as a novel strategy for major depressive disorder (MDD); however, the underlying molecular mechanisms remain unclear. Here, we demonstrate that enhanced GluA1 depalmitoylation in the nucleus accumbens mediates depressive-like behaviors following chronic stress, and identify that the dysfunction of carnitine palmitoyltransferase 1 C (CPT1C), a depalmitoylating enzyme that specifically depalmitoylates GluA1, mediated depression-like behaviors in mice. Furthermore, dopamine D2 receptor-expressing medium spiny neurons (D2-MSN)-specific knockdown of CPT1C prevented stress-induced depression-like behaviors, and CPT1C deficiency in D1-MSN abolished the behavioral and synaptic plasticity alterations caused by fluoxetine treatment. More importantly, CPT1C is directly involved in regulating GluA1 synthesis through disinhibiting mTORC1 signaling by targeting tuberous sclerosis complex 2. Collectively, these results newly identify CPT1C as a dual regulator of GluA1 function from protein synthesis, post-translational modification to subcellular localization, and show that CPT1C may serve as a promising novel therapeutic target for MDD. - Source: PubMed
Publication date: 2026/02/25
Tian DanXia Zhi-XuanWang Si-YingCao TingPan YueZhao Yue-LingZheng LingWei Bing-JieYang Shao-WeiChen Wei-KaiZheng Jie-YanSu Zheng-HuaChen ZhouTao Wu-ChengLuo Yi-XiaoLai Zhong-MengLi HongGao Shuang-QiFan HuaShen Zu-Cheng