LIM and SH3 protein 1 regulates cell growth and chemosensitivity of human glioblastoma via the PI3K/AKT pathway

Zhong, Chuanhong; Chen, Yitian; Tao, Bei; Peng, Lilei; Peng, Tangming; Yang, Xiaobo; Xia, Xiangguo; Chen, Ligang

doi:10.1186/s12885-018-4649-2

Cited by 26 publications

(34 citation statements)

References 23 publications

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“…18 Previous studies prove that LASP1 regulates cell proliferation in glioblastoma and gallbladder cancer through the PI3K/Akt pathway. 13,20 Our results showed that LASP2 knockdown significantly suppressed PI3K/Akt pathway. 740Y-P, abolished the inhibitory effects of LASP2 knockdown on cervical cancer, implying that the effects of LASP2 were mediated by the PI3K/Akt pathway.…”

Section: Discussionmentioning

confidence: 70%

Knockdown of LASP2 inhibits the proliferation, migration, and invasion of cervical cancer cells

Zhang

2019

J of Cellular Biochemistry

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LIM and SH3 protein 2 (LASP2) belongs to nebulin family. It has been proven that LASP2 is involved in several cancers; however, its role in cervical cancer is unclear. Herein, we showed that LASP2 was highly expressed in cervical cancer tissues and cell lines. To knockdown LASP2 in cervical cancer cells, small interfering RNAs (siRNAs) targeting LASP2 (si‐LASP2) were used. We found that cell proliferation, migration/invasion were markedly reduced after si‐LASP2 transfection. A significant increase in E‐cadherin expression, and decrease in N‐cadherin and vimentin expressions were observed in si‐LASP2 transfected cervical cancer cells. Knockdown of LASP2 caused significant inhibitory effect on the PI3K/Akt pathway. Treatment with the activator of the PI3K/Akt pathway, 740Y‐P, abolished the effects of si‐LASP2 transfection on cervical cancer cells. These findings suggested that LASP2 may be an oncogene through regulating the PI3K/Akt pathway in cervical cancer.

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Section: Discussionmentioning

confidence: 70%

Knockdown of LASP2 inhibits the proliferation, migration, and invasion of cervical cancer cells

Zhang

2019

J of Cellular Biochemistry

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“…Decreased pAKT1-S473 phosphorylation after LASP1 depletion has been observed before in several tumor cell lines, glioblastoma [21], gall bladder [22] and nasopharyngeal carcinoma [23], while LASP1 overexpression induces phosphorylation in colorectal cancer cells [24] and non-small cell lung cancer [25]. However, the underlying mechanisms are still controversial.…”

Section: Introductionmentioning

confidence: 87%

Phosphorylation-Dependent Differences in CXCR4-LASP1-AKT1 Interaction between Breast Cancer and Chronic Myeloid Leukemia

Butt

Stempfle

Lister

et al. 2020

Cells

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The serine/threonine protein kinase AKT1 is a downstream target of the chemokine receptor 4 (CXCR4), and both proteins play a central role in the modulation of diverse cellular processes, including proliferation and cell survival. While in chronic myeloid leukemia (CML) the CXCR4 is downregulated, thereby promoting the mobilization of progenitor cells into blood, the receptor is highly expressed in breast cancer cells, favoring the migratory capacity of these cells. Recently, the LIM and SH3 domain protein 1 (LASP1) has been described as a novel CXCR4 binding partner and as a promoter of the PI3K/AKT pathway. In this study, we uncovered a direct binding of LASP1, phosphorylated at S146, to both CXCR4 and AKT1, as shown by immunoprecipitation assays, pull-down experiments, and immunohistochemistry data. In contrast, phosphorylation of LASP1 at Y171 abrogated these interactions, suggesting that both LASP1 phospho-forms interact. Finally, findings demonstrating different phosphorylation patterns of LASP1 in breast cancer and chronic myeloid leukemia may have implications for CXCR4 function and tyrosine kinase inhibitor treatment.

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“…LIM and SH3 protein 1 (LASP1), a structural scaffolding protein and adhesion adaptor protein, was initially identified in breast cancer and was located at 17q12 [19]. Previous studies showed that LASP1 was upregulated in many malignant tumors including nasopharyngeal carcinoma, breast cancer, glioblastoma and colorectal cancer and contributed to tumor proliferation, invasion and metastasis [20][21][22][23]. In addition, LASP1 is upregulated in pancreatic ductal adenocarcinoma and is essential for HIF1α-induced invasion and metastasis [24].…”

Section: Introductionmentioning

confidence: 99%

ANLN-induced EZH2 upregulation promotes pancreatic cancer progression by mediating miR-218-5p/LASP1 signaling axis

Wang

Dai

Gong

et al. 2019

J Exp Clin Cancer Res

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Background: Pancreatic cancer is a highly lethal malignancy with poor prognosis. Anillin (ANLN), an actin binding protein, is upregulated and plays an important role in many malignant tumors. However, the precise role of ANLN in pancreatic cancer remains unclear. Methods: The expression of ANLN and its association with pancreatic cancer patient survival were analyzed using an online database and confirmed by immunohistochemistry. The ANLN protein expression in pancreatic cancer cell lines was detected by Western blot. Cell proliferation, colony formation and transwell assays in vitro and in vivo tumor growth were used to determine the role of ANLN in pancreatic cancer. Gene expression microarray analysis and a series of in vitro assays were used to elucidate the mechanisms of ANLN regulating pancreatic cancer progression.Results: We found that the ANLN expression was significantly upregulated in pancreatic cancer tissues and cell lines. The high expression of ANLN was associated with tumor size, tumor differentiation, TNM stage, lymph node metastasis, distant metastasis and poor prognosis in pancreatic cancer. ANLN downregulation significantly inhibited cell proliferation, colony formation, migration, invasion and tumorigenicity in nude mice. Meanwhile, we found that ANLN knockdown inhibited several cell-cell adhesion related genes, including the gene encoding LIM and SH3 protein 1 (LASP1). LASP1 upregulation partially reversed the tumor-suppressive effect of ANLN downregulation on pancreatic cancer cell progression. Moreover, we found that ANLN downregulation induced the expression of miR-218-5p which inhibited LASP1 expression through binding to its 3'UTR. We also found that ANLN-induced enhancer of zeste homolog 2 (EZH2) upregulation was involved in regulating miR-218-5p/LASP1 signaling axis. EZH2 upregulation or miR-218-5p downregulation partially reversed the tumor-suppressive effect of ANLN downregulation on pancreatic cancer cell progression. Conclusion: ANLN contributed to pancreatic cancer progression by regulating EZH2/miR-218-5p/LASP1 signaling axis. These findings suggest that ANLN may be a candidate therapeutic target in pancreatic cancer.

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LIM and SH3 protein 1 regulates cell growth and chemosensitivity of human glioblastoma via the PI3K/AKT pathway

Cited by 26 publications

References 23 publications

Knockdown of LASP2 inhibits the proliferation, migration, and invasion of cervical cancer cells

Knockdown of LASP2 inhibits the proliferation, migration, and invasion of cervical cancer cells

Phosphorylation-Dependent Differences in CXCR4-LASP1-AKT1 Interaction between Breast Cancer and Chronic Myeloid Leukemia

ANLN-induced EZH2 upregulation promotes pancreatic cancer progression by mediating miR-218-5p/LASP1 signaling axis

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