Rbm3-KO Mouse
一般名
Rbm3-KO
製品ID
S-KO-04053
背景情報
C57BL/6NCya
系統ID
KOCMP-19652-Rbm3-B6N-VA
状況
このマウス系統を論文で使用する場合は、「Rbm3-KO Mouse（カタログ番号S-KO-04053）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
Rbm3-KO
系統ID
KOCMP-19652-Rbm3-B6N-VA
遺伝子名
製品ID
S-KO-04053
遺伝子別名
2600016C11Rik
遺伝子別名
C57BL/6NCya
NCBI ID
修正
Conventional knockout
染色体
Chr X
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
ENSMUST00000040010
NCBIトランスクリプトID
NM_016809
ターゲット領域
Exon 2~6
有効領域の大きさ
~1.8 kb
遺伝子研究の概要
Rbm3, also known as cold-inducible protein, is an outstanding cold shock protein. It is rapidly upregulated in cold environments to maintain homeostasis and cell survival, which is a crucial physiological response to cold stress. Rbm3 is involved in multiple cellular physiological processes, including anti-apoptosis, circadian rhythm, cell cycle, reproduction, and tumogenesis. It may also play a role in RNA splicing, similar to heterogeneous nuclear ribonucleoproteins (hnRNPs) [1,5].
Rbm3 deficiency in studies has led to transcriptome-wide pre-mRNA splicing alterations, indicating its role in preserving transcriptome integrity [5]. In various disease models, its functions have been explored. For example, in endometrial cancer cells, sodium butyrate promotes Rbm3 expression, which indirectly downregulates SLC7A11 to stimulate ferroptosis [2]. In prion-diseased mice, an antisense oligonucleotide (ASO)-mediated increase in RBM3 expression led to remarkable neuroprotection, preventing neuronal loss and spongiosis [3]. In prostate cancer bone metastasis models, RBM3 suppresses stemness remodeling by modulating N6-methyladenosine on CTNNB1 mRNA [4]. In cardiomyocytes, downregulation of Rbm3 inhibited autophagy and promoted apoptosis during ischemia-reperfusion, while Rbm3 interacts with Raptor to regulate the autophagy pathway [6]. In an Alzheimer's disease (AD) microenvironment model, reduced Rbm3 in brain microvascular endothelial cells increased blood-brain barrier permeability by affecting tight junction proteins through MEF2C mRNA stability [7].
In summary, Rbm3 is a multifunctional protein involved in various biological processes. Studies using gene-knockout or disease-model-based research have revealed its importance in cancer, neurodegenerative diseases, myocardial infarction, and AD-related blood-brain barrier regulation. These findings provide insights into potential therapeutic strategies targeting Rbm3 for treating these diseases.
References:
1. Hu, Yajie, Liu, Yang, Quan, Xin, Xu, Bin, Li, Shize. 2022. RBM3 is an outstanding cold shock protein with multiple physiological functions beyond hypothermia. In Journal of cellular physiology, 237, 3788-3802. doi:10.1002/jcp.30852. https://pubmed.ncbi.nlm.nih.gov/35926117/
2. Wang, Ziwei, Shu, Wan, Zhao, Rong, Liu, Yan, Wang, Hongbo. 2023. Sodium butyrate induces ferroptosis in endometrial cancer cells via the RBM3/SLC7A11 axis. In Apoptosis : an international journal on programmed cell death, 28, 1168-1183. doi:10.1007/s10495-023-01850-4. https://pubmed.ncbi.nlm.nih.gov/37170022/
3. Preußner, Marco, Smith, Heather L, Hughes, Daniel, Mallucci, Giovanna R, Heyd, Florian. 2023. ASO targeting RBM3 temperature-controlled poison exon splicing prevents neurodegeneration in vivo. In EMBO molecular medicine, 15, e17157. doi:10.15252/emmm.202217157. https://pubmed.ncbi.nlm.nih.gov/36946385/
4. Zhang, Shouyi, Lv, Chengcheng, Niu, Yichen, Zhang, Yong, Zeng, Yu. 2023. RBM3 suppresses stemness remodeling of prostate cancer in bone microenvironment by modulating N6-methyladenosine on CTNNB1 mRNA. In Cell death & disease, 14, 91. doi:10.1038/s41419-023-05627-0. https://pubmed.ncbi.nlm.nih.gov/36750551/
5. Erkelenz, Steffen, Grzonka, Marta, Papadakis, Antonios, Hoeijmakers, Jan H J, Gyenis, Ákos. 2024. Rbm3 deficiency leads to transcriptome-wide splicing alterations. In RNA biology, 21, 1-13. doi:10.1080/15476286.2024.2413820. https://pubmed.ncbi.nlm.nih.gov/39387568/
6. Wang, Nan, Wang, Limeiting, Li, Changyan, Sun, Lin, Lu, Di. 2022. RBM3 interacts with Raptor to regulate autophagy and protect cardiomyocytes from ischemia-reperfusion-induced injury. In Journal of physiology and biochemistry, 79, 47-57. doi:10.1007/s13105-022-00919-z. https://pubmed.ncbi.nlm.nih.gov/36192581/
7. Ding, Ye, Lin, Meiqing, Wang, Jirui, Shang, Xiuli. 2024. RBM3 enhances the stability of MEF2C mRNA and modulates blood-brain barrier permeability in AD microenvironment. In Biochimica et biophysica acta. Molecular cell research, 1871, 119738. doi:10.1016/j.bbamcr.2024.119738. https://pubmed.ncbi.nlm.nih.gov/38670534/
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