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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

PRL-3 promotes cancer cell-endothelial cell adhesion by associating with JAM2. (A) The mRNA level of JAM2 in the HmEC and EC03 endothelial cells. (B) PRL-3 promotes cancer cell-endothelial cell adhesion by associating with JAM2.
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f4-ol-0-0-4836: PRL-3 promotes cancer cell-endothelial cell adhesion by associating with JAM2. (A) The mRNA level of JAM2 in the HmEC and EC03 endothelial cells. (B) PRL-3 promotes cancer cell-endothelial cell adhesion by associating with JAM2.

Mentions: Cancer metastasis is usually a process in which cancer cells migrate and penetrate the vascular vessels. To investigate this process, different endothelial cell (EC03 and HmEC) were seeded on 96 well plates, and LoVo cells expressing ectopic PRL-3 and control cells were seeded on top and incubated for 15 min. Following this incubation, the cells were washed with PBS 3 times, the number of adhesive cancer cells was estimated by a cytometer. As demonstrated in Fig. 4, the LoVo cells expressing ectopic PRL-3 adhered much more to ECO3 cells compared with the other pairing groups. And reverse transcription-polymerase chain reaction demonstrated that the mRNA expression levels of JAM2 was relatively higher in EC03 cells than in HmEC. These results indicate that ectopic PRL-3 and JAM2 may cooperate to promote cancer cell-endothelial cell adhesion.


PRL-3 promotes cell adhesion by interacting with JAM2 in colon cancer
PRL-3 promotes cancer cell-endothelial cell adhesion by associating with JAM2. (A) The mRNA level of JAM2 in the HmEC and EC03 endothelial cells. (B) PRL-3 promotes cancer cell-endothelial cell adhesion by associating with JAM2.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f4-ol-0-0-4836: PRL-3 promotes cancer cell-endothelial cell adhesion by associating with JAM2. (A) The mRNA level of JAM2 in the HmEC and EC03 endothelial cells. (B) PRL-3 promotes cancer cell-endothelial cell adhesion by associating with JAM2.
Mentions: Cancer metastasis is usually a process in which cancer cells migrate and penetrate the vascular vessels. To investigate this process, different endothelial cell (EC03 and HmEC) were seeded on 96 well plates, and LoVo cells expressing ectopic PRL-3 and control cells were seeded on top and incubated for 15 min. Following this incubation, the cells were washed with PBS 3 times, the number of adhesive cancer cells was estimated by a cytometer. As demonstrated in Fig. 4, the LoVo cells expressing ectopic PRL-3 adhered much more to ECO3 cells compared with the other pairing groups. And reverse transcription-polymerase chain reaction demonstrated that the mRNA expression levels of JAM2 was relatively higher in EC03 cells than in HmEC. These results indicate that ectopic PRL-3 and JAM2 may cooperate to promote cancer cell-endothelial cell adhesion.

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