Apmap-KO Mouse
一般名
Apmap-KO
製品ID
S-KO-20185
背景情報
C57BL/6JCya
系統ID
KOCMP-71881-Apmap-B6J-VB
状況
このマウス系統を論文で使用する場合は、「Apmap-KO Mouse(カタログ番号S-KO-20185)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
Apmap-KO
系統ID
KOCMP-71881-Apmap-B6J-VB
遺伝子名
製品ID
S-KO-20185
遺伝子別名
2310001A20Rik
遺伝子別名
C57BL/6JCya
NCBI ID
修正
Conventional knockout
染色体
Chr 2
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
ENSMUST00000046399
NCBIトランスクリプトID
NM_027977
ターゲット領域
Exon 3
有効領域の大きさ
~1.8 kb
遺伝子研究の概要
Apmap, also known as adipocyte plasma membrane-associated protein, is a glycosyl type II transmembrane protein mainly distributed in the plasma membrane and endoplasmic reticulum of adipocytes. It is an arylesterase that plays a crucial role in adipogenesis. Apmap is involved in multiple biological processes such as lipid transport, epithelial-mesenchymal transition, and may be associated with pathways like Wnt/β-catenin. It also has implications in maintaining endoplasmic reticulum-associated lipid and lipoprotein homeostasis [2,3,6].
In cancer cells, loss-of-function studies using CRISPR knockout screens identified Apmap as a regulator of susceptibility to antibody-dependent cellular phagocytosis (ADCP). Loss of Apmap synergizes with tumour antigen-targeting monoclonal antibodies and/or CD47-blocking monoclonal antibodies to drive increased phagocytosis across various cancer cell types and inhibit tumour growth in mice [1]. In cervical cancer, knockdown of Apmap significantly inhibited the migration ability of cancer cells, indicating its role in promoting epithelial-mesenchymal transition and metastasis through activating the Wnt/β-catenin pathway [3]. In a mouse model of Alzheimer's disease, constitutive deletion of Apmap worsened spatial memory phenotype and led to increased Aβ production and deposition into senile plaques [4]. In Rex rabbits, knockdown of FTO, which can increase Apmap expression, affected intramuscular fat deposition as Apmap promotes adipocyte differentiation [5]. Knockout of full-length Apmap in mice led to an improved metabolic phenotype upon diet-induced obesity, with enhanced insulin sensitivity, preserved glucose tolerance, etc., and Apmap was found to interact with extracellular collagen cross-linking matrix proteins [7].
In conclusion, Apmap has diverse functions in adipogenesis, lipid and lipoprotein homeostasis, and is involved in various disease conditions such as cancer, Alzheimer's disease, and metabolic disorders. Gene knockout mouse models have been instrumental in revealing these functions, providing valuable insights into the underlying mechanisms and potential therapeutic targets for these diseases.
References:
1. Kamber, Roarke A, Nishiga, Yoko, Morton, Bhek, Sage, Julien, Bassik, Michael C. 2021. Inter-cellular CRISPR screens reveal regulators of cancer cell phagocytosis. In Nature, 597, 549-554. doi:10.1038/s41586-021-03879-4. https://pubmed.ncbi.nlm.nih.gov/34497417/
2. Luo, Gang, Mu, Jinzhan, Wang, Shuhui, Dong, Xianggui, Ren, Zhanjun. 2022. Association of blood APMAP content and meat quality trait in Rex rabbits. In Animal biotechnology, 34, 974-979. doi:10.1080/10495398.2021.2007117. https://pubmed.ncbi.nlm.nih.gov/35001846/
3. Zhu, Xiuting, Xiang, Zijin, Zou, Lingxiao, Peng, Xiangdong, Xu, Dabao. 2021. APMAP Promotes Epithelial-Mesenchymal Transition and Metastasis of Cervical Cancer Cells by Activating the Wnt/β-catenin Pathway. In Journal of Cancer, 12, 6265-6273. doi:10.7150/jca.59595. https://pubmed.ncbi.nlm.nih.gov/34539899/
4. Gerber, Hermeto, Mosser, Sebastien, Boury-Jamot, Benjamin, Magara, Fulvio, Fraering, Patrick C. 2019. The APMAP interactome reveals new modulators of APP processing and beta-amyloid production that are altered in Alzheimer's disease. In Acta neuropathologica communications, 7, 13. doi:10.1186/s40478-019-0660-3. https://pubmed.ncbi.nlm.nih.gov/30704515/
5. Luo, Gang, Hong, Tingting, Yu, Lin, Ren, Zhanjun. 2023. FTO Regulated Intramuscular Fat by Targeting APMAP Gene via an m6A-YTHDF2-dependent Manner in Rex Rabbits. In Cells, 12, . doi:10.3390/cells12030369. https://pubmed.ncbi.nlm.nih.gov/36766716/
6. Paul, Blessy, Merta, Holly, Ugrankar-Banerjee, Rupali, Farber, Steven A, Henne, W Mike. 2024. Paraoxonase-like APMAP maintains endoplasmic reticulum-associated lipid and lipoprotein homeostasis. In bioRxiv : the preprint server for biology, , . doi:10.1101/2024.01.26.577049. https://pubmed.ncbi.nlm.nih.gov/38328083/
7. Pessentheiner, Ariane R, Huber, Katharina, Pelzmann, Helmut J, Bilban, Martin, Bogner-Strauss, Juliane G. 2017. APMAP interacts with lysyl oxidase-like proteins, and disruption of Apmap leads to beneficial visceral adipose tissue expansion. In FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 31, 4088-4103. doi:10.1096/fj.201601337R. https://pubmed.ncbi.nlm.nih.gov/28559441/
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精子検査
凍結前の精子濃度を測定し、精子の生存能力の判定します。
凍結後の精子では、各バッチから1本の凍結保存された精子を選び出し、体外受精に使用します。
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グローバル由来:
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