Ras-transformation reduce FAM20C expression and osteopontin phosphorylation

Schytte, Gitte N; Christensen, Brian; Bregenov, Ida; Sørensen, Esben S.

doi:10.1042/bsr20194378

Cited by 2 publications

(2 citation statements)

References 33 publications

(48 reference statements)

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“…It is therefore possible that the OPN secreted from A549 and H460 cells may be phosphorylated by FAM20C. However, in ras -transformed fibroblasts and ras -transformed mammary cell lines, OPN is less phosphorylated along with a reduced expression of FAM20C compared with their non-transformed cells [ 34 ]. In addition, the rescue of the FAM20C expression in the ras -transformed fibroblasts with FAM20C transfection did not recover the phosphorylation of OPN [ 34 ], although the FAM20C expression in HEK293T cells could phosphorylate OPN [ 27 ].…”

Section: Discussionmentioning

confidence: 99%

Phosphorylated Osteopontin Secreted from Cancer Cells Induces Cancer Cell Motility

et al. 2021

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Osteopontin (OPN) plays a pivotal role in cancer cell invasion and metastasis. Although OPN has a large number of phosphorylation sites, the functional significance of OPN phosphorylation in cancer cell motility remains unclear. In this study, we attempted to investigate whether phosphorylated OPN secreted from cancer cells affect cancer cell migration. Quantitative PCR and Western blot analyses revealed that MDA-MB435S, A549, and H460 cells highly expressed OPN, whereas the OPN expression levels in H358, MIAPaca-2, and Panc-1 cells were quite low or were not detected. Compared with the cancer cell lines with a low OPN expression, the high OPN-expressing cancer cell lines displayed a higher cell migration, and the cell migration was suppressed by the anti-OPN antibody. This was confirmed by the OPN overexpression in H358 cancer cells with a low endogenous OPN. Phos-tag ELISA showed that phosphorylated OPN was abundant in the cell culture media of A549 and H460 cells, but not in those of MDA-MB435S cells. Moreover, the A549 and H460 cell culture media, as well as the MDA-MB435S cell culture media with a kinase treatment increased cancer cell motility, both of which were abrogated by phosphatase treatment or anti-OPN antibodies. These results suggest that phosphorylated OPN secreted from cancer cells regulates cancer cell motility.

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Section: Discussionmentioning

confidence: 99%

Phosphorylated Osteopontin Secreted from Cancer Cells Induces Cancer Cell Motility

et al. 2021

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“…The phosphorylation of S 162 adjacent to the integrin-binding sites in the sequence 159 RGDSVVYGLR 168 is carried out by FAM20C, also present in the microsomes [ 63 ]. The levels of FAM20C can vary, and, in the presence of expressed Ras, the levels of FAM20C and OPN phosphorylation are reduced [ 64 ]. The importance of these various post-translational modifications for the different OPN functions has not been fully explored.…”

Section: Opn Post-translational Modificationsmentioning

confidence: 99%

Thrombin Cleavage of Osteopontin and the Host Anti-Tumor Immune Response

Leung

Myles

Morser

2023

Cancers

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Osteopontin (OPN) is a multi-functional protein that is involved in various cellular processes such as cell adhesion, migration, and signaling. There is a single conserved thrombin cleavage site in OPN that, when cleaved, yields two fragments with different properties from full-length OPN. In cancer, OPN has tumor-promoting activity and plays a role in tumor growth and metastasis. High levels of OPN expression in cancer cells and tumor tissue are found in various types of cancer, including breast, lung, prostate, ovarian, colorectal, and pancreatic cancer, and are associated with poor prognosis and decreased survival rates. OPN promotes tumor progression and invasion by stimulating cell proliferation and angiogenesis and also facilitates the metastasis of cancer cells to other parts of the body by promoting cell adhesion and migration. Furthermore, OPN contributes to immune evasion by inhibiting the activity of immune cells. Thrombin cleavage of OPN initiates OPN’s tumor-promoting activity, and thrombin cleavage fragments of OPN down-regulate the host immune anti-tumor response.

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Ras-transformation reduce FAM20C expression and osteopontin phosphorylation

Cited by 2 publications

References 33 publications

Phosphorylated Osteopontin Secreted from Cancer Cells Induces Cancer Cell Motility

Phosphorylated Osteopontin Secreted from Cancer Cells Induces Cancer Cell Motility

Thrombin Cleavage of Osteopontin and the Host Anti-Tumor Immune Response

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