Ras‑related protein Rap2c promotes the migration and invasion of human osteosarcoma cells
Authors: Xiucun Wang
Xiaojin Wu
Jinxia Wu
Jinling Zhang
Dongsheng Pei
Yaojie Pan
Wenqi Du
Lulu Wei
Journal: Oncology Letters (2018)
Discipline: CLINICAL MEDICINE
Keywords: Ras-related protein Rap2c; invasion; matrix metalloproteinase-2; migration; osteosarcoma cell.
Affiliations: Department of Physiology, Xuzhou Medical University, Xuzhou, Jiangsu 221004, P.R. China., Jiangsu Key Laboratory of Biological Cancer Therapy, Xuzhou, Jiangsu 221002, P.R. China., Department of Neurosurgery, The Affiliated Hospital of Xuzhou Medical University, Xuzhou, Jiangsu 221000, P.R. China., Department of Pathology, Xuzhou Medical University, Xuzhou, Jiangsu 221004, P.R. China., Department of Radiation Oncology, The First People's Hospital of Xuzhou, Xuzhou, Jiangsu 221002, P.R. China., Department of Oncology, LinYi People's Hospital Affiliated to Shandong University, Jinan, Shandong 250012, P.R. China., Jiangsu Center for The Collaboration and Innovation of Cancer Biotherapy, Xuzhou Medical University, Xuzhou, Jiangsu 221002, P.R. China.

Abstract:  Ras-related protein (Rap)2a and Rap2b are members of the GTP-binding protein family, and serve an important function in tumor progression. However, the associations between Rap2c and cancer cell functions have not yet been reported. Osteosarcoma is a type of bone cancer; its high degree of invasion is considered to be a major treatment challenge. The present study first investigated the biological role of Rap2c in human osteosarcoma cells and investigated the underlying mechanism of Rap2c on osteosarcoma cell migration and invasion. The results of the present study demonstrated that Rap2c overexpression promoted the migratory and invasive ability of cancer cells, and increased the activity of matrix metalloproteinase-2 (MMP2). Correspondingly, the knockdown of Rap2c inhibited tumor cell migration and invasion, whereas alterations to Rap2c had no effect on osteosarcoma cell proliferation or rate of apoptosis. Furthermore, Rap2c overexpression may decrease the protein level of tissue inhibitor of metalloproteinases 2 and increase the phosphorylation level of protein kinase B (Akt). Collectively, these results indicated that Rap2c has a key function in tumor migration and invasion, and the Akt signaling pathway may be involved in Rap2c-induced MMP2 expression. 

Retracted: No

PubPeer comments:
 Fig 3C has 2 pairs of overlaps ![file] , 
 Corrigendum: [12 April 2021] . ----------------------------------------- Subsequently to the publication of this paper, an interested reader drew to the authorsu2019 attention that two pairs of data panels in Fig. 3C appeared to contain overlapping data (comparing between the si-Ctrl si-Rap2c#2 and the Vector Rap2c panels). The authors have re-examined their original data and realized that the Vector and the Rap2c data panels for Fig. 3C were selected incorrectly. The revised version of Fig. 3, containing the correct data for the Vector and the Rap2c experiments in Fig. 3C, is shown below. The authors regret the inadvertent errors that were made in the preparation of the published figure, and confirm that these errors did not seriously affect the conclusions reported in the paper. The authors are grateful to the editor of Oncology Letters for allowing them the opportunity to publish a Corrigendum, and all the authors agree to this Corrigendum. Furthermore, they apologize to the readership for any inconvenience caused. ![] Figure 3. - Effect of Rap2c overexpression and knockdown on the invasion and migration of U2OS cells. (A) Wound-healing assays were performed in U2OS cells transfected with a Rap2c expression plasmid or siRNA (magnification, u00d7100). *P 0.05 vs. si-Ctrl; **P 0.01 vs. Vector. (B) Cell migration was performed following transfection with siRNA or a pcDNA3.1-Rap2c expression plasmid (magnification, u00d7100). *P 0.05 vs. si-Ctrl or Vector. (C) Cell invasion was measured following transfection with Rap2c expression plasmids or siRNA (magnification, u00d7100). *P 0.05 vs. si-Ctrl or Vector. (D) The relative enzyme activity of cleaved-MMP2 was measured by a gelatin zymography assay following transfection with siRNA or a Rap2c expression plasmid. **P 0.01 vs. si-Ctrl or Vector. siRNA, small interfering RNA; MMP2, matrix metalloproteinase-2; Ctrl, control; Vector, empty vector. ,