Extracellular Matrix Influencing HGF/c-MET Signaling Pathway: Impact on Cancer Progression

Noriega-Guerra, Heydi; Freitas, Vanessa M.

doi:10.3390/ijms19113300

Cited by 47 publications

(32 citation statements)

References 121 publications

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“…Therefore, understanding the mechanisms underlying the invasion, proliferation, and cell transfer of breast cancer and the discovery of new therapeutic molecular targets are extremely important. AQP3 and c-Met are overexpressed in various malignant tumours, such as breast cancer (2,3,9,17). Here, our study demonstrated that AQP3 and c-Met were overexpressed in 52.5% and 83.1% of breast cancer tissue specimens, respectively.…”

Section: Discussionsupporting

confidence: 51%

“…c-Met is a receptor of hepatocyte growth factor (HGF). Noriega-Guerra H et al (2) concluded that c-Met is related to the development and metastasis of a number of malignancies, including breast cancer. c-Met binds to HGF, resulting in the autophosphorylation and overexpression of c-Met, and this interaction participates in embryonic development, wound repair, tissue regeneration, cell differentiation, etc.…”

Section: Introductionmentioning

confidence: 99%

“…c-Met binds to HGF, resulting in the autophosphorylation and overexpression of c-Met, and this interaction participates in embryonic development, wound repair, tissue regeneration, cell differentiation, etc. under physiological conditions but promotes the proliferation, invasion, migration, antiapoptotic processes, and angiogenesis of cancer cells under pathological conditions (2). High HGF/c-Met signalling promotes breast cancer progression (3), and the activation of c-Met leads to phosphorylation of its downstream proteins (mainly gab1, followed by gab2), followed by the activation of signal transduction proteins such as PI3K, FAK, JUN, ERK, and STATs (4)(5)(6)(7).…”

Section: Introductionmentioning

confidence: 99%

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Cellular-Mesenchymal to Epithelial Transition Factor Upregulates Aquaporin 3 Expression in Human Breast Cancer Cells

Zhu

Chen

Zhou

et al. 2020

Preprint

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Background Aquaporin 3 (AQP3) and Cellular-mesenchymal to epithelial transition factor (c-Met) are both overexpressed in human breast cancer and highly related to proliferation and migration. However, it is still unclear whether c-Met is associated with AQP3. The study objective was to explore the relationship between c-Met and AQP3 in human breast cancer. Methods We used immunohistochemistry to determine the expression of AQP3 and c-Met in breast cancer tissue specimens and analysed whether there was any correlation between the two molecules. Real-time quantitative polymerase chain reaction and Western blotting were used to detect AQP3 expression in MCF-7 and MDA-MB-231 cells after human hepatocyte growth factor (hHGF) treatment and/or transfection with c-Met silencing small interfering (si)RNA. Additionally, cell migration was examined with a wound scratch assay. Results Based on the immunohistochemical results combined with the clinicopathological data of 59 breast cancer patients, c-Met exhibited a significant correlation with AQP3 in breast cancer tissue. Studies have shown that hHGF can increase c-Met phosphorylation, and we discovered that the hHGF-induced increase in AQP3 expression was dose dependent. However, after reducing c-Met expression with c-Met-specific siRNA, AQP3 expression decreased accordingly. Additionally, the wound scratch assay showed that AQP3-specific siRNA or c-Met-specific siRNA significantly inhibited breast cancer cell migration, which was promoted by hHGF. Conclusions Our study indicated that AQP3 expression was regulated by c-Met in human breast cancer. These discoveries may help us comprehend the mechanisms underlying breast cancer development and invasion and offer another possibility for targeted treatment of breast cancer.

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Section: Discussionsupporting

confidence: 51%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cellular-Mesenchymal to Epithelial Transition Factor Upregulates Aquaporin 3 Expression in Human Breast Cancer Cells

Zhu

Chen

Zhou

et al. 2020

Preprint

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“…Other isoforms, such as GPC3, -4 and -5, have been shown to interact with either Wnt ligands or growth factors and to mediate the migration of tumoral cells in breast, lung, and hepatocellular cancers [54][55][56][57][58][59]. The ability of either Wnt signaling or several growth factors signaling to influence cellular motility is well known [60,61]. Therefore, we suggest that GPC1 is crucial for cell motility in GBM, as the PG may bind proteins intrinsically linked with migration.…”

Section: Discussionmentioning

confidence: 85%

Glypican-1 in human glioblastoma: implications in tumorigenesis and chemotherapy

Listik

Toma

2020

Oncotarget

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Glioblastoma is one of the most common malignant brain tumors, with which patients have a mean survival of 24 months. Glypican-1 has been previously shown to be overexpressed in human glioblastoma and to be negatively correlated with patient's survival. This study aimed to investigate how glypican-1 influences the tumoral profile of human glioblastoma using in vitro cell line models. By downregulating the expression of glypican-1 in U-251 MG cells, we observed that the cellular growth and proliferation were highly reduced, in which cells were significantly shifted towards G0 as opposed to G1 phases. Cellular migration was severely affected, and glypican-1 majorly impacted the affinity towards laminin-binding of glioblastoma U-251 MG cells. This proteoglycan was highly prevalent in glioblastoma cells, being primarily localized in the cellular membrane and extracellular vesicles, occasionally with glypican-3. Glypican-1 could also be found in cell-cell junctions with syndecan-4 but was not identified in lipid rafts in this study. Glypican-1-silenced cells were much more susceptible to temozolomide than in U-251 MG itself. Therefore, we present evidence not only to support facts that glypican-1 is an elementary macromolecule in glioblastoma tumoral microenvironment but also to introduce this proteoglycan as a promising therapeutic target for this lethal tumor.

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“…In many types of cancer, the HGF/c-Met system is important for malignant potential, cancer cell invasion, metastasis, and determining clinical outcomes (4,5). In fact, cancer cell proliferation, cell cycle, migration, and angiogenesis were previously suggested as HGF/c-Met-related pathological mechanisms, based on in vivo and in vitro studies (6)(7)(8). Furthermore, c-Met is closely associated with the regulation of various cancer-related molecules such as cyclooxygenase (COX)-2, heme oxygenase (HO)-1, and vascular endothelial growth factor (VEGF)-A in various types of malignancies (9)(10)(11)(12).…”

Section: Introductionmentioning

confidence: 99%

Pathological roles of c‑Met in bladder cancer: Association with cyclooxygenase‑2, heme oxygenase‑1, vascular endothelial growth factor‑A and programmed death ligand�1

et al. 2020

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c-Met is a receptor tyrosine kinase that binds a specific ligand, namely hepatocyte growth factor (HGF). The HGF/c-Met system is important for malignant aggressiveness in various types of cancer, including bladder cancer (BC). However, although phosphorylation is the essential step required for biological activation of c-Met, pathological roles of phosphorylated c-Met at the clinical and molecular levels in patients with BC are not fully understood. In the present study, the expression levels of c-Met and the phosphorylation of two of its tyrosine residues (pY1234/pY1235 and pY1349) were immunohistochemically examined in 185 BC tissues. The associations between these expression levels and cancer cell invasion, metastasis, and cyclooxygenase-2 (COX-2), heme oxygenase-1 (HO-1), VEGF-A and programmed death ligand 1 (PD-L1) levels were investigated. c-Met was associated with muscle invasion (P= 0.021), as well as the expression levels of HO-1 (P= 0.028) and PD-L1 (P<0.001), whereas pY1349 c-Met was associated with muscle invasion (P=0.003), metastasis (P=0.025), and COX-2 (P=0.017), HO-1 (P=0.031) and PD-L1 (P= 0.001) expression. By contrast, pY1234/1235 c-Met was associated with muscle invasion and metastasis (P= 0.006 and P= 0.012, respectively), but not with the panel of cancer-associated molecules. Furthermore, COX-2 and PD-L1 expression were associated with muscle invasion and metastasis, respectively (P= 0.045 and P= 0.036, respectively). Hence, c-Met serves important roles in muscle invasion by regulating HO-1 and PD-L1, whereas its phosphorylation at Y1349 is associated with muscle invasion and metastasis via the regulation of COX-2, HO-1 and PD-L1 in patients with BC. Furthermore, phosphorylation at Y1234/1235 may lead to muscle invasion and metastasis via alternate mechanisms associated with c-Met and pY1349 c-Met.

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Extracellular Matrix Influencing HGF/c-MET Signaling Pathway: Impact on Cancer Progression

Cited by 47 publications

References 121 publications

Cellular-Mesenchymal to Epithelial Transition Factor Upregulates Aquaporin 3 Expression in Human Breast Cancer Cells

Cellular-Mesenchymal to Epithelial Transition Factor Upregulates Aquaporin 3 Expression in Human Breast Cancer Cells

Glypican-1 in human glioblastoma: implications in tumorigenesis and chemotherapy

Pathological roles of c‑Met in bladder cancer: Association with cyclooxygenase‑2, heme oxygenase‑1, vascular endothelial growth factor‑A and programmed death ligand�1

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