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PRL-3 promotes cell adhesion by interacting with JAM2 in colon cancer

View Article: PubMed Central - PubMed

ABSTRACT

Phosphatase of regenerating liver-3 (PRL-3), also termed PTP4A3, is a metastasis-related protein tyrosine phosphatase. Its expression levels are significantly correlated with the progression and survival of a wide range of malignant tumors. However, the mechanism by which PRL-3 promotes tumor invasion and metastasis is not clear. In the present study, the functions of PRL-3 were systemically analyzed in the key events of metastasis including, motility and adhesion. A cell wounding assay, cell spread assay and cell-matrix adhesion assay were carried out to analyze the cell movement and cell adhesion ability of colon cancer, immunoprecipitation and immunofluorescence assay was confirmed the interaction of PRL-3 and JAM2. It was demonstrated that PRL-3 promoted the motility of Flp-In-293 and LoVo colon cancer cells and increased the distribution of cell skeleton proteins on the cell protrusions. In addition, stably expressing PRL-3 reduced the spreading speed of colon cancer cells and cell adhesion on uncoated, fibronectin-coated and collagen I-coated plates. Mechanistically, junction adhesion molecular 2 (JAM2) was identified as a novel interacting protein of PRL-3. The findings of the present study revealed the roles of PRL-3 in cancer cell motility and adhesion process, and provided information on the possibility of PRL-3 increase cell-cell adhesion by associating with JAM2.

No MeSH data available.


Related in: MedlinePlus

PRL3 promotes colon cancer cell motility. (A) Ectopic PRL-3 expressed in 293 and LoVo cancer cells. β-actin served as a loading control (magnification, ×20). (B) PRL-3 promoted cell motility in the cell wound healing assay. (C) Expression of PRL-3 redistributed the cell skeleton protein β-actin and phalloidin. Scale bar, 20 µM.
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f1-ol-0-0-4836: PRL3 promotes colon cancer cell motility. (A) Ectopic PRL-3 expressed in 293 and LoVo cancer cells. β-actin served as a loading control (magnification, ×20). (B) PRL-3 promoted cell motility in the cell wound healing assay. (C) Expression of PRL-3 redistributed the cell skeleton protein β-actin and phalloidin. Scale bar, 20 µM.

Mentions: To examine the motility-promoting potential of PRL-3, myc-tagged PRL-3 was stably expressed in 293 and LoVo cells (Fig. 1A). Next, a wounding closure assay was performed. A line was scraped through the cell monolayer and the closure of these lines was recorded at 24 h intervals. The results demonstrated that the speed of wound healing of 293-PRL-3 and LoVo-PRL-3 were faster than their respective control cells. A total of 48 h or 72 h after wounding, the PRL-3 transfected cells had moved to close the wound, while those of their control cells remained apart (Fig. 1B).


PRL-3 promotes cell adhesion by interacting with JAM2 in colon cancer
PRL3 promotes colon cancer cell motility. (A) Ectopic PRL-3 expressed in 293 and LoVo cancer cells. β-actin served as a loading control (magnification, ×20). (B) PRL-3 promoted cell motility in the cell wound healing assay. (C) Expression of PRL-3 redistributed the cell skeleton protein β-actin and phalloidin. Scale bar, 20 µM.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4998106&req=5

f1-ol-0-0-4836: PRL3 promotes colon cancer cell motility. (A) Ectopic PRL-3 expressed in 293 and LoVo cancer cells. β-actin served as a loading control (magnification, ×20). (B) PRL-3 promoted cell motility in the cell wound healing assay. (C) Expression of PRL-3 redistributed the cell skeleton protein β-actin and phalloidin. Scale bar, 20 µM.
Mentions: To examine the motility-promoting potential of PRL-3, myc-tagged PRL-3 was stably expressed in 293 and LoVo cells (Fig. 1A). Next, a wounding closure assay was performed. A line was scraped through the cell monolayer and the closure of these lines was recorded at 24 h intervals. The results demonstrated that the speed of wound healing of 293-PRL-3 and LoVo-PRL-3 were faster than their respective control cells. A total of 48 h or 72 h after wounding, the PRL-3 transfected cells had moved to close the wound, while those of their control cells remained apart (Fig. 1B).

View Article: PubMed Central - PubMed

ABSTRACT

Phosphatase of regenerating liver-3 (PRL-3), also termed PTP4A3, is a metastasis-related protein tyrosine phosphatase. Its expression levels are significantly correlated with the progression and survival of a wide range of malignant tumors. However, the mechanism by which PRL-3 promotes tumor invasion and metastasis is not clear. In the present study, the functions of PRL-3 were systemically analyzed in the key events of metastasis including, motility and adhesion. A cell wounding assay, cell spread assay and cell-matrix adhesion assay were carried out to analyze the cell movement and cell adhesion ability of colon cancer, immunoprecipitation and immunofluorescence assay was confirmed the interaction of PRL-3 and JAM2. It was demonstrated that PRL-3 promoted the motility of Flp-In-293 and LoVo colon cancer cells and increased the distribution of cell skeleton proteins on the cell protrusions. In addition, stably expressing PRL-3 reduced the spreading speed of colon cancer cells and cell adhesion on uncoated, fibronectin-coated and collagen I-coated plates. Mechanistically, junction adhesion molecular 2 (JAM2) was identified as a novel interacting protein of PRL-3. The findings of the present study revealed the roles of PRL-3 in cancer cell motility and adhesion process, and provided information on the possibility of PRL-3 increase cell-cell adhesion by associating with JAM2.

No MeSH data available.


Related in: MedlinePlus