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更新于：2025-05-07

SLC25A20

更新于：2025-05-07

基本信息

别名

CAC、CACT、carnitine-acylcarnitine carrier

+ [5]

简介

Mediates the electroneutral exchange of acylcarnitines (O-acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-carnitines) with free carnitine ((R)-carnitine or L-carnitine) across the mitochondrial inner membrane, via a ping-pong mechanism (Probable) (PubMed:12892634, PubMed:18307102). Key player in the mitochondrial oxidation pathway, it translocates the fatty acids in the form of acylcarnitines into the mitochondrial matrix, where the carnitine palmitoyltransferase 2 (CPT-2) activates them to undergo fatty acid beta-oxidation (Probable). Catalyzes the unidirectional transport (uniport) of carnitine at lower rates than the antiport (exchange) (PubMed:18307102).

关联

项与 SLC25A20 相关的药物

KN-510713

靶点

ACAA1 x SLC25A20

作用机制

ACAA1 inhibitors [+1]

在研机构

National Cancer Center Korea [+1]

原研机构

New Cancer Cure-Bio Co.,Ltd.

在研适应症

胰腺癌

非在研适应症-

最高研发阶段临床1/2期

首次获批国家/地区-

首次获批日期1800-01-20

KN-510

靶点

SLC25A20

作用机制

SLC25A20 blockers

在研机构

New Cancer Cure-Bio Co.,Ltd. [+1]

原研机构

New Cancer Cure-Bio Co.,Ltd.

在研适应症

晚期恶性实体瘤 [+1]

非在研适应症-

最高研发阶段临床1期

首次获批国家/地区-

首次获批日期1800-01-20

项与 SLC25A20 相关的临床试验

NCT06012708

/ Completed临床1期

An Open-label, Dose-escalation and Dose-finding, Phase 1 Study to Evaluate the Safety, Tolerability, and Pharmacokinetics of KN510, KN713 as Combination Therapy in Patients With Advanced Solid Tumors

To evaluate the safety and tolerability of the combination therapy of KN510 and KN713 and determine the MTD and RP2D in patients with advanced solid tumors.

开始日期2023-09-11

申办/合作机构

New Cancer Cure-Bio Co.,Ltd.

100 项与 SLC25A20 相关的临床结果

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100 项与 SLC25A20 相关的转化医学

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0 项与 SLC25A20 相关的专利（医药）

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257

项与 SLC25A20 相关的文献（医药）

2025-05-01·International Journal of Biological Macromolecules

Whole genome sequencing revealed genetic structure, domestication, and selection of Chinese indigenous ducks

Article

作者: Xiong, Rui ; Li, Jiawei ; Zhu, Yihao ; Tan, Hongli ; Huang, Yuxuan ; Gong, Yujie ; Fang, Xinyan ; Min, Huang ; Jing, Zhou ; Ouyang, Jing ; Hao, Chen ; Zheng, Sumei ; Wang, Yanan ; Wu, Liping ; Miao, Junjie ; Wu, Yan ; Yan, Xueming ; Tang, Hongbo ; Wang, Lei ; Xuan, Rui ; Luo, Keyi

The genetic architecture and domestication history of Chinese indigenous ducks, particularly those with distinct traits like the Longsheng duck (LSD), are not well characterized. This study used whole-genome resequencing data from 540 ducks across 30 populations to explore the genetic diversity and structure of these ducks. Our findings suggest extensive interspecific hybridization between mallard and spot-billed duck. Comparing with other Chinese ducks, LSD is a distinct breed with moderate genetic diversity. Selective signal analysis identified several key genes impacting neural development, fat metabolism, immunity, and circadian rhythms like SLC25A20 and PER2. These genes showed strong selective pressures that parallelled other domestication processes. Additionally, EDNRB2 was identified as a potential gene influencing the unique coloration of LSD's plumage, bill, and webbed feet, associated with distinct mutations in non-coding regions. Comparative analysis with other indigenous breeds further pinpointed genes associated with LSD-specific traits, including plumage color, reproductive capabilities, and fat deposition, such as MITF, SPATA2, EIF2S2, PLIN3, ATP1B1, and CCDC80. Our findings clarify the population genetics of Chinese indigenous ducks. They also highlight key genes and mutations that shape the unique characteristics of LSD. These insights pave the way for further research into the genetic resources and domestication patterns of Chinese ducks.

2025-04-14·ChemBioChem

Lanthanides Gd and Tm Can Inhibit Carnitine/Acylcarnitine Transporter: Insights from All‐Atoms Simulations

Article

作者: Tonazzi, Annamaria ; Marino, Tiziana ; Prejanò, Mario ; Indiveri, Cesare ; Giangregorio, Nicola

AbstractRecent experimental evidence highlighted the inhibition of carnitine/acylcarnitine carrier (CAC), an important mitochondrial transmembrane protein for living organisms, by the early lanthanide Pr3+. A possible explanation of such a behaviour was found in the preference of the cation for amino acids like aspartate and glutamate containing a carboxylate in the side chain, laying in the inter‐membrane space. Interaction of the cation with these residues can cause halt the transfer of the protein‘s substrates between the matrix and cytoplasm thus opening to new scenarios concerning the CAC‐metal interactions and its relative inhibition. In the present work, the panel of metals binding the CAC protein is predictively expanded including Gd3+ and Tm3+, selected as representative species of middle and late lanthanides, respectively. A more realistic membrane‐containing model of the protein was built and the comparative analysis of the molecular dynamics (MD) simulations of CAC apo‐form with its complexed systems, named CAC−Pr, CAC−Gd and CAC−Tm, was performed. The analysis of the trajectories revealed that the inhibition is caused by the coordination of D132 and E179 to the cations and that such interactions generate a reorganization of important salt‐bridges inside the framework of CAC. In detail, MD simulations highlighted that a spontaneous conformational change from cytoplasmatic‐state (c‐state) to matrix‐state (m‐state) induced by cations and that, in this condition, the protein channel is occluded, thus explaining the inhibition.

2025-03-01·Ecotoxicology and Environmental Safety

Metabolic characterizations of PFOS-induced disruptions in early embryonic development

Article

作者: Xu, Bo ; Huang, Lei ; Zhu, Mengyuan ; Xu, Yuntian ; Chen, Minjian ; Jiang, Yingtong

BACKGROUNDPerfluorooctane sulfonates (PFOS) are persistent environmental pollutants linked to developmental toxicity, but the mechanisms remain unclear. This study investigates the metabolic changes induced by PFOS exposure during early embryonic development and integrates metabolomic, transcriptomic, and molecular docking analyses to explore underlying mechanisms.METHODSMouse embryoid bodies (mEBs) were exposed to PFOS for 2 days, 4 days and 6 days. Metabolomic profiling was conducted to identify differential metabolites. Transcriptomic data were integrated with metabolomics using Cytoscape to map metabolic pathway alterations. Molecular docking simulations were performed to assess PFOS binding to key enzymes.RESULTSPFOS exposure resulted in significant alterations in lipid (Erucic acid, L-carnitine), amino acid (L-methionine, creatine, hippuric acid, and spermine), and nucleotide metabolism (e.g., hypoxanthine). Integrated transcriptomic and metabolomic analysis revealed disrupted pathways included SLC25A20 regulated L-carnitine metabolism. Molecular docking simulations indicated that PFOS binds to methionine synthase and hypoxanthine guanine phosphoribosyl transferase, potentially inhibiting their function and disrupting metabolic homeostasis for L-methionine and hypoxanthine during embryonic development.CONCLUSIONPFOS exposure disrupts key metabolic pathways critical for embryogenesis, including lipid, amino acid, and nucleotide metabolism. Molecular docking and transcriptomic integration highlight enzyme targeting as a potential mechanism of PFOS-induced developmental toxicity. These findings provide novel insights into the molecular and metabolic disruptions caused by PFOS, with implications for understanding its developmental toxicity.