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Tumor cell and carcinoma-associated fibroblast interaction regulates matrix metalloproteinases and their inhibitors in oral squamous cell carcinoma.

Fullár A, Kovalszky I, Bitsche M, Romani A, Schartinger VH, Sprinzl GM, Riechelmann H, Dudás J - Exp. Cell Res. (2012)

Bottom Line: In addition, these cells also cooperated in activation of MMP pro-enzymes.It is particularly interesting that the fibroblast-produced inactive MMP-2 has been activated by the tumor-cell-produced membrane-type 1 matrix metalloproteinase (MT1-MMP).The crosstalk between cancer- and the surrounding fibroblast stromal-cells is essential for the fine tuning of cancer cells invasivity.

View Article: PubMed Central - PubMed

Affiliation: 1st Department of Pathology and Experimental Cancer Research, Semmelweis University, Üllői út 26, 1085 Budapest, Hungary. fullarsz@gmail.com

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Western blot analysis of MMP-2 (A, B), TIMP-1 (A, C) and TIMP-3 (A, D) related to loading control (β-actin) in PDL fibroblasts in control (1–2) and co-cultured (3–4) conditions. Densitometry of the detected bands normalized to the β-actin band densities. MMP-2 (B), TIMP-1 (C), TIMP-3 (D), *: p < 0.05.
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f0020: Western blot analysis of MMP-2 (A, B), TIMP-1 (A, C) and TIMP-3 (A, D) related to loading control (β-actin) in PDL fibroblasts in control (1–2) and co-cultured (3–4) conditions. Densitometry of the detected bands normalized to the β-actin band densities. MMP-2 (B), TIMP-1 (C), TIMP-3 (D), *: p < 0.05.

Mentions: Gene expression of MMPs-1, -2, -3, -7, -9 and -13 and TIMPs 1–3 was investigated in fibroblasts (PDLs) in control and co-cultured conditions. MMPs-1–3 and TIMPs-1 and -3 were constitutively expressed in PDLs, and their gene expression was significantly upregulated in co-cultured PDLs (Figs. 2A–E; Table 1). The upregulation of MMP-2, TIMP-1 and TIMP-3 gene expression in co-cultured PDLs has also been confirmed at protein level (Figs. 3A–D). MMPs-7, -9 (Table 1) and -13 were not detected in PDLs. TIMP-2 was also constitutively expressed in PDLs, and in co-culture it was not significantly regulated (Table 1).


Tumor cell and carcinoma-associated fibroblast interaction regulates matrix metalloproteinases and their inhibitors in oral squamous cell carcinoma.

Fullár A, Kovalszky I, Bitsche M, Romani A, Schartinger VH, Sprinzl GM, Riechelmann H, Dudás J - Exp. Cell Res. (2012)

Western blot analysis of MMP-2 (A, B), TIMP-1 (A, C) and TIMP-3 (A, D) related to loading control (β-actin) in PDL fibroblasts in control (1–2) and co-cultured (3–4) conditions. Densitometry of the detected bands normalized to the β-actin band densities. MMP-2 (B), TIMP-1 (C), TIMP-3 (D), *: p < 0.05.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3378977&req=5

f0020: Western blot analysis of MMP-2 (A, B), TIMP-1 (A, C) and TIMP-3 (A, D) related to loading control (β-actin) in PDL fibroblasts in control (1–2) and co-cultured (3–4) conditions. Densitometry of the detected bands normalized to the β-actin band densities. MMP-2 (B), TIMP-1 (C), TIMP-3 (D), *: p < 0.05.
Mentions: Gene expression of MMPs-1, -2, -3, -7, -9 and -13 and TIMPs 1–3 was investigated in fibroblasts (PDLs) in control and co-cultured conditions. MMPs-1–3 and TIMPs-1 and -3 were constitutively expressed in PDLs, and their gene expression was significantly upregulated in co-cultured PDLs (Figs. 2A–E; Table 1). The upregulation of MMP-2, TIMP-1 and TIMP-3 gene expression in co-cultured PDLs has also been confirmed at protein level (Figs. 3A–D). MMPs-7, -9 (Table 1) and -13 were not detected in PDLs. TIMP-2 was also constitutively expressed in PDLs, and in co-culture it was not significantly regulated (Table 1).

Bottom Line: In addition, these cells also cooperated in activation of MMP pro-enzymes.It is particularly interesting that the fibroblast-produced inactive MMP-2 has been activated by the tumor-cell-produced membrane-type 1 matrix metalloproteinase (MT1-MMP).The crosstalk between cancer- and the surrounding fibroblast stromal-cells is essential for the fine tuning of cancer cells invasivity.

View Article: PubMed Central - PubMed

Affiliation: 1st Department of Pathology and Experimental Cancer Research, Semmelweis University, Üllői út 26, 1085 Budapest, Hungary. fullarsz@gmail.com

Show MeSH
Related in: MedlinePlus