Aamp, short for angio-associated migratory cell protein, is a ubiquitously expressed protein. It plays significant roles in cell migration, angiogenesis, and is involved in various signaling pathways such as RhoA/Rho kinase signaling [3]. Aamp has been associated with multiple biological processes and is of great importance in understanding cancer progression and angiogenesis-related diseases [2,3,4]. Genetic models can be valuable for further exploring its functions.

In cancer research, Aamp has been found to promote colorectal cancer metastasis. It stabilizes RhoA by suppressing SMURF2-mediated ubiquitination and degradation of RhoA, accelerating CRC cell migration and invasion [2]. In non-small cell lung cancer, Aamp is upregulated and promotes cell migration and invasion by interacting with CDC42 and promoting its activation [6]. In glioma, Aamp was identified as a binding partner of B7-H3, potentially opening new targeted therapy possibilities against the pro-tumorigenic B7-H3 [1]. For angiogenesis, AAMP is crucial as siRNA-mediated knockdown and antibody blockade of AAMP impaired VEGF-induced endothelial cell tube formation and aortic ring angiogenic sprouting, and it regulates angiogenesis through RhoA/Rho kinase signaling [3]. In endothelial barrier function, AAMP is a novel negative regulator, regulating the stability and activity of RhoA and RhoB [5].

In conclusion, Aamp is a key protein involved in cell migration, angiogenesis, and cancer-related processes. Studies using various models have revealed its importance in diseases like colorectal cancer, non-small cell lung cancer, and glioma, as well as in angiogenesis and endothelial barrier function regulation. These findings contribute to our understanding of disease mechanisms and potential therapeutic targets.

References:

1. Ciprut, Sara, Berberich, Anne, Knoll, Maximilian, Wick, Wolfgang, Lemke, Dieter. 2022. AAMP is a binding partner of costimulatory human B7-H3. In Neuro-oncology advances, 4, vdac098. doi:10.1093/noajnl/vdac098. https://pubmed.ncbi.nlm.nih.gov/35919070/

2. Wu, Yuhui, Liu, Bofang, Lin, Weiqiang, Han, Weidong, Xie, Jiansheng. 2021. AAMP promotes colorectal cancermetastasis by suppressing SMURF2-mediatedubiquitination and degradation of RhoA. In Molecular therapy oncolytics, 23, 515-530. doi:10.1016/j.omto.2021.11.007. https://pubmed.ncbi.nlm.nih.gov/34901393/

3. Hu, Jianjun, Qiu, Juhui, Zheng, Yiming, Xie, Xiang, Wang, Guixue. 2015. AAMP Regulates Endothelial Cell Migration and Angiogenesis Through RhoA/Rho Kinase Signaling. In Annals of biomedical engineering, 44, 1462-74. doi:10.1007/s10439-015-1442-0. https://pubmed.ncbi.nlm.nih.gov/26350504/

4. Wang, Yang, Liu, Ting, Zhang, Ke, Huang, Rong-Hai, Jiang, Li. 2023. Pan-cancer analysis from multi-omics data reveals AAMP as an unfavourable prognostic marker. In European journal of medical research, 28, 258. doi:10.1186/s40001-023-01234-z. https://pubmed.ncbi.nlm.nih.gov/37501187/

5. Podieh, Fabienne, Overboom, Max C, Knol, Jaco C, Jimenez, Connie R, Hordijk, Peter L. 2024. AAMP and MTSS1 Are Novel Negative Regulators of Endothelial Barrier Function Identified in a Proteomics Screen. In Cells, 13, . doi:10.3390/cells13191609. https://pubmed.ncbi.nlm.nih.gov/39404373/

6. Yao, Shun, Shi, Feifei, Mu, Ning, Liu, Xiangguo, Su, Ling. 2020. Angio-associated migratory cell protein (AAMP) interacts with cell division cycle 42 (CDC42) and enhances migration and invasion in human non-small cell lung cancer cells. In Cancer letters, 502, 1-8. doi:10.1016/j.canlet.2020.11.050. https://pubmed.ncbi.nlm.nih.gov/33279622/