Identification of target proteins ofN-acetylglucosaminyl transferase V in human colon cancer and implications of protein tyrosine phosphatase kappa in enhanced cancer cell migration

PROTEOMICS ◽  
2006 ◽  
Vol 6 (4) ◽  
pp. 1187-1191 ◽  
Author(s):  
Yong-Sam Kim ◽  
Hye-Yeon Kang ◽  
Jin-Young Kim ◽  
Sejeong Oh ◽  
Cheorl-Ho Kim ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Cell Migration ◽  
Cancer Cell ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Human Colon ◽  
Cancer Cell Migration ◽  
Human Colon Cancer ◽  
Target Proteins ◽  
Protein Tyrosine

scholarly journals Wnt5a promotes human colon cancer cell migration and invasion but does not augment intestinal tumorigenesis in Apc 1638N mice

2013 ◽  
Vol 34 (11) ◽  
pp. 2629-2638 ◽  
Author(s):  
Elvira R.M. Bakker ◽  
Asha Mooppilmadham Das ◽  
Werner Helvensteijn ◽  
Patrick F. Franken ◽  
Sigrid Swagemakers ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Cell Migration ◽  
Cancer Cell ◽  
Human Colon ◽  
Colon Cancer Cell ◽  
Migration And Invasion ◽  
Cancer Cell Migration ◽  
Human Colon Cancer Cell ◽  
Human Colon Cancer ◽  
Intestinal Tumorigenesis

scholarly journals GDNF increases cell motility in human colon cancer through VEGF–VEGFR1 interaction

2013 ◽  
Vol 21 (1) ◽  
pp. 73-84 ◽  
Author(s):  
Ssu-Ming Huang ◽  
Tzu-Sheng Chen ◽  
Chien-Ming Chiu ◽  
Leang-Kai Chang ◽  
Kuan-Fu Liao ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Cell Migration ◽  
Cancer Cells ◽  
Cancer Cell ◽  
Transcriptional Activity ◽  
Human Colon ◽  
Colon Cancer Cell ◽  
Cancer Cell Migration ◽  
Colon Cancer Cells ◽  
Human Colon Cancer

Glial cell line-derived neurotrophic factor (GDNF), a potent neurotrophic factor, has been shown to affect cancer cell metastasis and invasion. However, the molecular mechanisms underlying GDNF-induced colon cancer cell migration remain unclear. GDNF is found to be positively correlated with malignancy in human colon cancer patients. The migratory activities of two human colon cancer cell lines, HCT116 and SW480, were found to be enhanced in the presence of human GDNF. The expression of vascular endothelial growth factor (VEGF) was also increased in response to GDNF stimulation, along with VEGF mRNA expression and transcriptional activity. The enhancement of GDNF-induced cancer cell migration was antagonized by a VEGF-neutralizing antibody. Our results also showed that the expression of VEGF receptor 1 (VEGFR1) was increased in response to GDNF stimulation, whereas GDNF-induced cancer cell migration was reduced by a VEGFR inhibitor. The GDNF-induced VEGF expression was regulated by the p38 and PI3K/Akt signaling pathways. Treatment with GDNF increased nuclear hypoxia-inducible factor 1 α (HIF1α) accumulation and its transcriptional activity in a time-dependent manner. Moreover, GDNF increased hypoxia responsive element (HRE)-containing VEGF promoter transcriptional activity but not that of the HRE-deletion VEGF promoter construct. Inhibition of HIF1α by a pharmacological inhibitor or dominant-negative mutant reduced the GDNF-induced migratory activity in human colon cancer cells. These results indicate that GDNF enhances the migration of colon cancer cells by increasing VEGF–VEGFR interaction, which is mainly regulated by the p38, PI3K/Akt, and HIF1α signaling pathways.

scholarly journals Differential inhibition of gelatinase activity in human colon adenocarcinoma cells by Aloe vera and Aloe arborescens extracts

2020 ◽  
Vol 20 (1) ◽  
Author(s):  
Ana Lima ◽  
Paula Batista-Santos ◽  
Eduarda Veríssimo ◽  
Patrícia Rebelo ◽  
Ricardo Boavida Ferreira
Keyword(s):  
Colon Cancer ◽  
Cell Proliferation ◽  
Wound Healing ◽  
Cell Migration ◽  
Cancer Cell ◽  
Bioactive Compounds ◽  
Human Colon ◽  
Cancer Cell Proliferation ◽  
Cancer Cell Migration ◽  
Different Types

Abstract Background Aloe’s reported bioactivities (anticancer, anti-inflammatory and wound healing) suggest they might inhibit a subgroup of matrix metalloproteinases (MMPs) called gelatinases (MMP-2 and MMP-9). The goal of the present study was to compare the MMP inhibitory potential of two Aloe species, A. vera and A. arborescens. Methods Different types of extraction were tested and specific bioactive compounds were quantified. Cancer cell invasion inhibitory activities were measured in vitro using the wound healing assay in human colon cancer cells (HT29). Effects on gelatinase activities were further assessed by dye-quenched gelatin and gelatin zymography. Results Different types of extraction yielded significantly different levels of bioactivities and of bioactive compounds, which might be due to a greater amount of extractable bioactive compounds such as anthraquinones. Both A. arborescens and A. vera have potential as inhibitory agents in cancer cell proliferation via MMP-9 and MMP-2 enzymatic activity inhibition, being able to reduce colon cancer cell proliferation and migration but A. arborescens showed to be a more effective inhibitor of cancer cell migration than A. vera. Conclusion This work opens novel perspectives on the mode of action of Aloe species in cancer cell migration and may provide clues as to why there are so many conflicting results on Aloe’s activities.

scholarly journals Tyrosine phosphatase PTPRD suppresses colon cancer cell migration in coordination with CD44

2011 ◽  
Vol 2 (3) ◽  
pp. 457-463 ◽  
Author(s):  
KOSUKE FUNATO ◽  
YUSUKE YAMAZUMI ◽  
TAKEAKI ODA ◽  
TETSU AKIYAMA
Keyword(s):  
Colon Cancer ◽  
Cell Migration ◽  
Cancer Cell ◽  
Tyrosine Phosphatase ◽  
Colon Cancer Cell ◽  
Cancer Cell Migration

Oxyresveratrol Inhibits Human Colon Cancer Cell Migration through Regulating Epithelial-Mesenchymal Transition and MicroRNA

2021 ◽  
Author(s):  
Ting-Ann Lin ◽  
Wei-Sheng Lin ◽  
Ya-Chun Chou ◽  
Nagabhushanam Kalyanam ◽  
Chi-Tang Ho ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Colon Cancer ◽  
Cell Migration ◽  
Epithelial Mesenchymal Transition ◽  
Human Colon ◽  
Colon Cancer Cell ◽  
Cancer Cell Migration ◽  
Human Colon Cancer Cell ◽  
Human Colon Cancer ◽  
Mesenchymal Transition

The major cause of death in Colorectal cancer (CRC) patients is metastasis. Moreover, lots of studies have emphasized that the epithelial-mesenchymal transition (EMT) is a pivotal step in metastasis. Both...

scholarly journals Development and validation of nanobodies specific to the oncogenic phosphatase Protein Tyrosine Phosphatase 4A3 (PTP4A3 or PRL-3)

2020 ◽  
Author(s):  
Caroline N. Smith ◽  
Min Wei ◽  
Zachary A. Williamson ◽  
Yelena Chernyavskaya ◽  
K. Martin Chow ◽  
...  
Keyword(s):  
Cancer Progression ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Human Colon ◽  
Human Colon Cancer ◽  
Protein Tyrosine ◽  
Dual Specificity ◽  
Cancer Cell Survival ◽  
Tool Set ◽  
Patient Prognosis

AbstractProtein Tyrosine Phosphatase 4A3 (PTP4A3 or PRL-3) is an oncogenic dual specificity phosphatase that drives tumor metastasis, promotes cancer cell survival, has been linked to poor patient prognosis in a variety of tumor types. The mechanisms by which PRL-3 promotes tumor progression are not well understood, which is in part due to lack of tools to study this protein. The development of small molecule inhibitors that are specific to PRL-3 has proven difficult, as the PRL family is >80% homologous. As research tools, antibodies directed against PRL-3 have been more successful, although they are limited to certain assay types. To address this, we have designed, purified, and tested alpaca-derived PRL-3 single domain antibodies, or nanobodies. We have identified 7 unique nanobodies that bind to PRL-3 in ELISA with no activity towards PRL-1 and PRL-2. Anti-PRL-3 nanobodies immunoprecipitated PRL-3 from cell lysates and were used to define PLR-3 localization in human colon cancer cells in immunofluorescence cell staining experiments. These anti-PRL-3 nanobodies represent an important expansion of the tool set used for the study of PRL-3, and can be used to better define the role of PRL-3 in cancer progression while serving as a useful first step in the development of biologics to target PRL-3 in the clinic.

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