TGF-β1 and TGF-β2 strongly enhance the secretion of plasminogen activator inhibitor-1 and matrix metalloproteinase-9 of the human prostate cancer cell line PC-3

Konrad, Lutz; Scheiber, Jonas A.; Schwarz, Lena; Schrader, Andres Jan; Hofmann, Rainer

doi:10.1016/j.regpep.2009.04.012

Cited by 33 publications

(24 citation statements)

References 33 publications

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“…In most experiments, the changes of gene expression and protein synthesis caused by EMD or biomechanical loading were significant but not very pronounced. However, it has been shown that even two‐ or three‐fold changes in molecules, such as TGF‐β1, may result in phenotype and functional changes of cells 37‐39 . Whether the magnitude of effects observed in our study is sufficient to be clinically significant remains to be elucidated.…”

Section: Discussionmentioning

confidence: 74%

Interactions of Enamel Matrix Derivative and Biomechanical Loading in Periodontal Regenerative Healing

Nokhbehsaim

Deschner

Bourauel

et al. 2011

Journal of Periodontology

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Section: Discussionmentioning

confidence: 74%

Interactions of Enamel Matrix Derivative and Biomechanical Loading in Periodontal Regenerative Healing

Nokhbehsaim

Deschner

Bourauel

et al. 2011

Journal of Periodontology

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“…The TGF-β family includes TGF-β1, TGF-β2, and TGF-β3, which exhibit different and non-overlapping actions in vitro [5]. TGF-β1 and TGF-β2 mostly contribute to cancer progression by acting in both tumor cells and stromal cells [6], [7], and a loss of sensitivity to growth inhibition by TGF-β is thought to occur in most cancer cells. Meanwhile, cancer cells gain an advantage by selective reduction of the tumor-suppressive activity of TGF-β and augmentation of its oncogenic activity [8], [9].…”

Section: Introductionmentioning

confidence: 99%

Transforming Growth Factor-β1 and -β2 in Gastric Precancer and Cancer and Roles in Tumor-Cell Interactions with Peripheral Blood Mononuclear Cells In Vitro

Miao

Zeng

et al. 2013

PLoS ONE

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Transforming growth factor-β1 (TGF-β1) and -β2 are correlated with poorer prognosis in gastric cancer (GC), which act in both tumor and immune cells. However, their expressions in precancer and tumor-cell interactions with peripheral blood mononuclear cells (PBMCs) remain unclear. Protein levels of TGF-β1 and -β2 were analyzed by immunohistochemistry and corresponding mRNA levels were determined by quantitative real-time polymerase chain reaction in 93 surgical and biopsy specimens. Serum TGF-β concentration was detected by enzyme-linked immunosorbent assays. AGS and MKN45 cell lines were directly or indirectly cocultured with PBMCs in vitro. TGF-β and Smad molecules were detected after cocultures and the growths of GC cells and PBMCs were assessed by cell proliferation assay. The results showed positive staining for TGF-β1 was detected in 20% of control samples, 52.3% of precancer, 59.1% of early GC and 66.7% of advanced GC samples, correlated with lesion progression (χ2 = 9.487, P = 0.002). All tissues were positive for TGF-β2. TGF-β1 mRNA levels were increased in advanced cancers, while TGF-β2 increased earlier. TGF-β1 mRNA levels were higher in tumor than in peritumor, which positively correlated with Smad2 and Smad7. Serum TGF-β levels were significantly higher in patients with early and advanced cancers compared to controls (TGF-β1∶50.08±4.38 and 45.76±5.00 vs. 27.78±6.11 ng/mL; TGF-β2∶133.61±21.90 and 111.34±15.76 vs. 59.41±15.42 ng/mL, both P<0.05). The levels of TGF-β1 mRNA and cytokine secretion were higher in GC cells after direct coculture compared to indirect culture. TGF-β1 was decreased and TGF-β2 was increased in PBMCs after cocultures. Moreover, TGF-β1 inhibited the viability of PBMCs but not cancer cells. Collectively, neoplastic transformation may be an early event involving the increase of TGF-β1 in the general and local environment. TGF-β1 production is promoted by the direct interaction between GC cells and PBMCs, which might facilitate cancer development.

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“…Plasminogen activator inhibitor-1, which is the most potent endogenous inhibitor of fibrinolysis, is up-regulated by transforming growth factors (TGF) in the human prostate [10].…”

Section: Introductionmentioning

confidence: 99%

“…While several studies have supported the hypothesis that obesity, as well as insulin resistance, is a novel risk factor for prostate cancer prognosis [7,8,10], no study has been carried out to associate all the aforementioned markers to biomarkers of prostate volume among apparently healthy men. This study attempted to determine whether there exists a relation between biomarkers of obesity and insulin resistance and known prostate pathology biomarkers among apparently cancer-free adult men.…”

Section: Introductionmentioning

confidence: 99%

Visceral obesity and inflammation markers in relation to serum prostate volume biomarkers among apparently healthy men

Alokail

Al-Daghri²,

Al‐Attas³

et al. 2011

European Journal of Clinical Investigation

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TGF-β1 and TGF-β2 strongly enhance the secretion of plasminogen activator inhibitor-1 and matrix metalloproteinase-9 of the human prostate cancer cell line PC-3

Cited by 33 publications

References 33 publications

Interactions of Enamel Matrix Derivative and Biomechanical Loading in Periodontal Regenerative Healing

Interactions of Enamel Matrix Derivative and Biomechanical Loading in Periodontal Regenerative Healing

Transforming Growth Factor-β1 and -β2 in Gastric Precancer and Cancer and Roles in Tumor-Cell Interactions with Peripheral Blood Mononuclear Cells In Vitro

Visceral obesity and inflammation markers in relation to serum prostate volume biomarkers among apparently healthy men

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