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Cancer malignancy is enhanced by glyceraldehyde-derived advanced glycation end-products.

Takino J, Yamagishi S, Takeuchi M - J Oncol (2010)

Bottom Line: A recent study has suggested that glyceraldehyde-derived AGEs (Glycer-AGEs) enhanced the malignancy of melanoma cells, but glucose-derived AGEs did not.The present paper aimed to examine the effect of Glycer-AGEs on cultured lung cancer A549 cells.Glycer-AGEs significantly attenuated cell proliferation.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Pharmacy, Faculty of Pharmaceutical Sciences, Hokuriku University, Ho-3 Kanagawa-machi, Kanazawa 920-1181, Japan.

ABSTRACT
The receptor for advanced glycation end-products (RAGEs) is associated with the malignancy of cancer. A recent study has suggested that glyceraldehyde-derived AGEs (Glycer-AGEs) enhanced the malignancy of melanoma cells, but glucose-derived AGEs did not. However, the effects of Glycer-AGEs on other cancer cells remain poorly understood, and the molecular mechanisms behind the above-mentioned effect have not been clarified. The present paper aimed to examine the effect of Glycer-AGEs on cultured lung cancer A549 cells. RAGE was expressed in A549 cells. Glycer-AGEs significantly attenuated cell proliferation. Furthermore, Glycer-AGEs enhanced the migration capacity of the cells by activating Rac1 via ROS and also increased their invasion capacity. We demonstrated that Glycer-AGEs enhanced the migration and invasion of A549 cells rather than their proliferation. These results suggest that Glycer-AGEs play a critical role in the malignancy of cancer rather than its proliferation and are potential targets for therapeutic intervention.

No MeSH data available.


Related in: MedlinePlus

RAGE expression by Western blot analysis. Cell lysates (30 μg of proteins/lane) were loaded onto a 10% polyacrylamide gel. Size markers (kDa) are shown on the left. Equal protein loading was estimated using anti-β-actin antibody. The arrow indicates full-length RAGE.
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fig1: RAGE expression by Western blot analysis. Cell lysates (30 μg of proteins/lane) were loaded onto a 10% polyacrylamide gel. Size markers (kDa) are shown on the left. Equal protein loading was estimated using anti-β-actin antibody. The arrow indicates full-length RAGE.

Mentions: To investigate whether RAGE proteins are present in human lung adenocarcinoma A549 cells, we carried out Western blot analysis using anti-RAGE antibody (N-16). RAGE proteins of different molecular weights were detected in A549 cells (Figure 1). In full length RAGE cDNA-transfected human hepatocellular carcinoma Hep3B cells, the major band (57 kDa) (indicated by an arrow in Figure 1) represents the full-length RAGE protein. Likewise, the full-length RAGE protein was also detected in A549 and mock transfected Hep3B cells. No bands were detected in a neutralization experiment using blocking peptide (data not shown) so the other bands may represent deglycosylated RAGE proteins.


Cancer malignancy is enhanced by glyceraldehyde-derived advanced glycation end-products.

Takino J, Yamagishi S, Takeuchi M - J Oncol (2010)

RAGE expression by Western blot analysis. Cell lysates (30 μg of proteins/lane) were loaded onto a 10% polyacrylamide gel. Size markers (kDa) are shown on the left. Equal protein loading was estimated using anti-β-actin antibody. The arrow indicates full-length RAGE.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2902753&req=5

fig1: RAGE expression by Western blot analysis. Cell lysates (30 μg of proteins/lane) were loaded onto a 10% polyacrylamide gel. Size markers (kDa) are shown on the left. Equal protein loading was estimated using anti-β-actin antibody. The arrow indicates full-length RAGE.
Mentions: To investigate whether RAGE proteins are present in human lung adenocarcinoma A549 cells, we carried out Western blot analysis using anti-RAGE antibody (N-16). RAGE proteins of different molecular weights were detected in A549 cells (Figure 1). In full length RAGE cDNA-transfected human hepatocellular carcinoma Hep3B cells, the major band (57 kDa) (indicated by an arrow in Figure 1) represents the full-length RAGE protein. Likewise, the full-length RAGE protein was also detected in A549 and mock transfected Hep3B cells. No bands were detected in a neutralization experiment using blocking peptide (data not shown) so the other bands may represent deglycosylated RAGE proteins.

Bottom Line: A recent study has suggested that glyceraldehyde-derived AGEs (Glycer-AGEs) enhanced the malignancy of melanoma cells, but glucose-derived AGEs did not.The present paper aimed to examine the effect of Glycer-AGEs on cultured lung cancer A549 cells.Glycer-AGEs significantly attenuated cell proliferation.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Pharmacy, Faculty of Pharmaceutical Sciences, Hokuriku University, Ho-3 Kanagawa-machi, Kanazawa 920-1181, Japan.

ABSTRACT
The receptor for advanced glycation end-products (RAGEs) is associated with the malignancy of cancer. A recent study has suggested that glyceraldehyde-derived AGEs (Glycer-AGEs) enhanced the malignancy of melanoma cells, but glucose-derived AGEs did not. However, the effects of Glycer-AGEs on other cancer cells remain poorly understood, and the molecular mechanisms behind the above-mentioned effect have not been clarified. The present paper aimed to examine the effect of Glycer-AGEs on cultured lung cancer A549 cells. RAGE was expressed in A549 cells. Glycer-AGEs significantly attenuated cell proliferation. Furthermore, Glycer-AGEs enhanced the migration capacity of the cells by activating Rac1 via ROS and also increased their invasion capacity. We demonstrated that Glycer-AGEs enhanced the migration and invasion of A549 cells rather than their proliferation. These results suggest that Glycer-AGEs play a critical role in the malignancy of cancer rather than its proliferation and are potential targets for therapeutic intervention.

No MeSH data available.


Related in: MedlinePlus