![]() ![]() In this study, we obtained data of LASP-1 interacting proteins from public databases and published studies and assessed their biological functions, associated pathways, and interaction networks via bioinformatics analysis. However, the binding partners involved in the development of HBV-related hepatocellular carcinoma mediated by LASP-1 are not completely understood. identified that vimentin is a new binding partner of LASP-1 in HCC cells 18. Furthermore, we previously discovered that HBV X protein (HBX) was responsible for the upregulation of LASP-1 in HCC cells 17. indicate that the increase of LASP-1 in HCC tissues is related to hepatitis B virus (HBV) infection 14. In addition, the results from Wang H et al. In addition, different cellular factors, such as P53 and uPA, participate in the regulation of LASP-1 expression in HCC cells 15, 16. LASP-1 over-expression is also observed in hepatocellular carcinoma (HCC) and associated with poor clinical prognosis of the disease 14. Taken together, these results indicate that elucidating the interaction of LASP-1 with its binding partners will help us to further understand the molecular mechanism of LASP-1 on the development of different types of cancer. Furthermore, the interaction of LASP-1 with S100A11 is required for EMT as well as progression of CRC 13. In addition, a study from the same group showed that LASP-1 not only interacts with S100 calcium binding protein A11 (S100A11) but also increases its expression in CRC cells. reported that LASP-1 interacts with 14–3–3σ in colorectal cancer (CRC) cells and contributes to the progression and metastasis of CRC via the inhibition of 14-3-3σ expression 12. However, the precise molecular functions and physiological processes associated with LASP-1 interactors have been not fully clarified. To date, several binding partners of LASP-1, such as VASP, zyxin, Krp1, and CXCR2 1, have been reported. These unique domains facilitate its interaction with a variety of proteins. Structurally, LASP-1 contains an N-terminal LIM domain, two nebulin-like repeats named R1 and R2 domain, and a C-terminal SH3 domain 1, 11. Given the importance of LASP-1 function and its clinical relevance in different cancers, LASP-1 might be used as a potential molecular target for the clinical treatment of patients with different tumours. Moreover, current clinical studies suggest that over-expression of LASP-1 could serve as a prognostic marker and is correlated with increased clinical stage, lymph node metastasis, and poor survival of cancer patients 1. Functional experiments of LASP-1 indicate that it plays critical roles in cell migration, invasion, proliferation, epithelial-mesenchymal transition (EMT), cell cycle and signalling pathways 1, 4, 5, 8, 9, 10. ![]() LIM and SH3 domain protein (LASP-1) is a scaffold protein that has been identified to facilitate the development of several types of human cancers 1, including breast carcinoma 2, prostate carcinoma 3, colorectal carcinoma 4, gastric cancer 5, oesophageal squamous cell carcinoma 6, and gallbladder cancer 7. Taken together, these results could help enrich our understanding of LASP-1 interactors and their relationships with HBV-related HCC. Besides, numerous LASP-1 interactors were associated with various clinical factors and related to the survival and recurrence of HBV-related HCC. In the disease, LASP-1 and its interactors were further predicted to be regulated by a complex interaction network composed of different transcription factors. In addition, LASP-1 and several its interactors are significantly altered in HBV-related HCC through microarray analysis and could form a complex co-expression network. ![]() Through an integrated network analysis of the interaction and pathways of LASP-1 interactors, cross-talk between different proteins and associated pathways was found. Via bioinformatics analysis, we found that LASP-1 interactors were related to distinct molecular functions and associated with various biological processes. We obtained information regarding LASP-1 interactors from public databases and published studies. Although the role of LASP-1 in hepatocarcinogenesis has been reported, the implication of LASP-1 interactors in HBV-related hepatocellular carcinoma (HCC) is not clearly evaluated. LIM and SH3 domain protein (LASP-1) is responsible for the development of several types of human cancers via the interaction with other proteins however, the precise biological functions of proteins interacting with LASP-1 are not fully clarified. ![]()
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