Tpi1-flox Mouse
一般名
Tpi1-flox
製品ID
S-CKO-06422
背景情報
C57BL/6JCya
系統ID
CKOCMP-21991-Tpi1-B6J-VA
状況
このマウス系統を論文で使用する場合は、「Tpi1-flox Mouse(カタログ番号S-CKO-06422)はサイアジェンから購入しました。」と引用してください。
製品タイプ
年齢
遺伝子型
性別
数量
標準的な配送方法では、少なくとも3匹のヘテロ接合体キャリアを保証しています。ホモ接合体キャリアや指定された性別の個体の繁殖サービスも利用可能です。
基本情報
系統名
Tpi1-flox
系統ID
CKOCMP-21991-Tpi1-B6J-VA
遺伝子名
製品ID
S-CKO-06422
遺伝子別名
TIM, Tpi, Tpi-1
遺伝子別名
C57BL/6JCya
NCBI ID
修正
Conditional knockout
染色体
Chr 6
表現型
アプリケーション
--
さらに
系統詳細
EnsemblトランスクリプトID
ENSMUST00000172132
NCBIトランスクリプトID
NM_009415
ターゲット領域
Exon 1~4
有効領域の大きさ
~2.1 kb
遺伝子研究の概要
Tpi1, or triosephosphate isomerase 1, is a key glycolytic enzyme. It plays a crucial role in glucose metabolism by catalyzing the interconversion between dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP). This function is fundamental to various metabolic pathways, including those related to energy production and lipid synthesis, and is of great biological importance in normal cellular function and development [1,2,3,5,7,8].
In lung regeneration, dopaminylation of Tpi1 in endothelial cells suppresses ferroptosis, promoting lung regeneration over fibrosis. Suppressing Tpi1 dopaminylation triggers ferroptotic angiocrine signaling, leading to a transition from lung regeneration to fibrosis [1].
In myopia, genetic analyses have identified an enrichment of Tpi1, and promoting scleral glycolysis via Tpi1 can lead to myopia-associated fibroblast-to-myofibroblast transdifferentiation [2].
In osteoarthritis, LDHA-mediated histone lactylation in the Tpi1 promoter enhances its transcription activity, promoting glycolysis in chondrocytes [3].
In glioblastoma, Linc00942 interacts with Tpi1 and PKM2, promoting self-renewal and chemoresistance [4].
In breast cancer, Tpi1 promotes cancer progression by activating the PI3K/AKT/mTOR signaling pathway and stabilizing CDCA5 [5].
In lung adenocarcinoma, Tpi1 promotes metastasis through the MAPK/ERK-induced epithelial-mesenchymal transition process [6].
In Tibetan sheep Sertoli cells, Tpi1 promotes cell proliferation, glycolysis, and inhibits apoptosis, and miR-1285-3p can regulate these processes by targeting Tpi1 [7].
In hepatocellular carcinoma, Rab20 downregulation reduces Tpi1 in extracellular vesicles, promoting aerobic glycolysis and hepatocarcinogenesis [8].
In conclusion, Tpi1 is a vital enzyme in glycolysis, significantly influencing multiple biological processes and disease conditions. Studies, some of which likely involve in vivo models such as KO or CKO mouse models (though not always explicitly stated), have shown its role in lung regeneration, myopia, osteoarthritis, glioblastoma, breast cancer, lung adenocarcinoma, spermatogenesis-related processes, and hepatocarcinogenesis. Understanding Tpi1 function through these models provides insights into disease mechanisms and potential therapeutic targets.
References:
1. Mo, Chunheng, Li, Hui, Yan, Mengli, Cao, Zhongwei, Ding, Bi-Sen. . Dopaminylation of endothelial TPI1 suppresses ferroptotic angiocrine signals to promote lung regeneration over fibrosis. In Cell metabolism, 36, 1839-1857.e12. doi:10.1016/j.cmet.2024.07.008. https://pubmed.ncbi.nlm.nih.gov/39111287/
2. Lin, Xiaolei, Lei, Yi, Pan, Miaozhen, Zhou, Xiangtian, Zhao, Fei. 2024. Augmentation of scleral glycolysis promotes myopia through histone lactylation. In Cell metabolism, 36, 511-525.e7. doi:10.1016/j.cmet.2023.12.023. https://pubmed.ncbi.nlm.nih.gov/38232735/
3. Xia, Junfeng, Qiao, Zongrui, Hao, Xiao, Zhang, Yin. 2024. LDHA-induced histone lactylation mediates the development of osteoarthritis through regulating the transcription activity of TPI1 gene. In Autoimmunity, 57, 2384889. doi:10.1080/08916934.2024.2384889. https://pubmed.ncbi.nlm.nih.gov/39086231/
4. Yang, Changxiao, Li, Ziwei, Tian, Kaifu, Jiang, Chuanlu, Cai, Jinquan. 2024. LncRNA-Mediated TPI1 and PKM2 Promote Self-Renewal and Chemoresistance in GBM. In Advanced science (Weinheim, Baden-Wurttemberg, Germany), 11, e2402600. doi:10.1002/advs.202402600. https://pubmed.ncbi.nlm.nih.gov/39342418/
5. Jin, Xiaoying, Wang, Dandan, Lei, Mengxia, Sun, Weiling, Chen, Xuesong. 2022. TPI1 activates the PI3K/AKT/mTOR signaling pathway to induce breast cancer progression by stabilizing CDCA5. In Journal of translational medicine, 20, 191. doi:10.1186/s12967-022-03370-2. https://pubmed.ncbi.nlm.nih.gov/35509067/
6. Li, Yu, Pan, Bin, Zhang, Feiyang, Zhao, Jun, Li, Chang. 2023. TPI1 promotes MAPK/ERK-induced EMT, cell migration and invasion in lung adenocarcinoma. In Thoracic cancer, 15, 327-338. doi:10.1111/1759-7714.15196. https://pubmed.ncbi.nlm.nih.gov/38130074/
7. An, Xuejiao, Li, Taotao, Chen, Nana, Duan, Xinming, Ma, Youji. 2022. miR-1285-3p targets TPI1 to regulate the glycolysis metabolism signaling pathway of Tibetan sheep Sertoli cells. In PloS one, 17, e0270364. doi:10.1371/journal.pone.0270364. https://pubmed.ncbi.nlm.nih.gov/36137140/
8. Liu, Bonnie Hei Man, Tey, Sze Keong, Mao, Xiaowen, Yun, Jing Ping, Yam, Judy Wai Ping. 2021. TPI1-reduced extracellular vesicles mediated by Rab20 downregulation promotes aerobic glycolysis to drive hepatocarcinogenesis. In Journal of extracellular vesicles, 10, e12135. doi:10.1002/jev2.12135. https://pubmed.ncbi.nlm.nih.gov/34401050/
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