This is a wonderfully refreshing salad. Lentils are an ideal protein alternative and are high in fiber, folate, thiamin and iron. To give variety of color and texture, we added the chopped red pepper.
Mint not only has antioxidants properties but digestive and antibacterial properties as well.

Lentil Salad with Olives, Mint and Feta 

Serves 4-6
Ingredients:

• 1 cup lentils, rinsed
• Salt and pepper
• 6 cups water
• 2 cups low-sodium chicken or vegetables broth
• 5 garlic clove (peeled and crushed)
• 1 bay leaf
• 4 tablespoons extra-virgin olive oil
• 2 tablespoons white wine vinegar
• ½ cup chopped pitted Kalamata olives
• ½ cup fresh mint leaves, chopped
• 1 large shallot, minced
• ¼ cup feta cheese, crumbled

Directions:

1. Place lentils and 1 teaspoon salt in bowl. Cover with 4 cups warm water and soak for 1 hour. Drain well. This is the brining process which keeps the skin intact.
2. Adjust oven rack to the middle position. Heat oven to 325 degrees F. Place drained lentils, 2 cups water, broth, garlic, bay leaf and ½ teaspoon salt in a saucepan. Cover and bake until lentils are tender but remain intact – 40 to 60 minutes.
3. Whisk oil and vinegar in a bowl.
4. Drain lentils well; remove and discard the garlic and bay leaf. Add drained lentils, olives, mint and shallot in a bowl. Drizzle on the oil and vinegar dressing, season with salt and pepper and toss. Sprinkle with feta cheese to serve.

Source: CooksIllustrated.com is an online recipe subscription with more information as to the science behind the cooking.

Debra DeMille, MS, RD, CSO, is a nutritional counselor at the Abramson Cancer Center at Penn Medicine Pennsylvania Hospital. Dietitians at the Abramson Cancer Center provide educational programs about nutrition that are open to patients as well as the community. Cancer-fighting recipes on this blog are the product of the quarterly series “Cooking Nutritious and Delicious Foods,” which promotes seasonal healthy foods with cancer-fighting properties.

This is a wonderfully refreshing salad. Lentils are an ideal protein alternative and are high in fiber, folate, thiamin and iron. To give variety of color and texture, we added the chopped red pepper.
Mint not only has antioxidants properties but digestive and antibacterial properties as well.

Lentil Salad with Olives, Mint and Feta 

Serves 4-6
Ingredients:

• 1 cup lentils, rinsed
• Salt and pepper
• 6 cups water
• 2 cups low-sodium chicken or vegetables broth
• 5 garlic clove (peeled and crushed)
• 1 bay leaf
• 4 tablespoons extra-virgin olive oil
• 2 tablespoons white wine vinegar
• ½ cup chopped pitted Kalamata olives
• ½ cup fresh mint leaves, chopped
• 1 large shallot, minced
• ¼ cup feta cheese, crumbled

Directions:

1. Place lentils and 1 teaspoon salt in bowl. Cover with 4 cups warm water and soak for 1 hour. Drain well. This is the brining process which keeps the skin intact.
2. Adjust oven rack to the middle position. Heat oven to 325 degrees F. Place drained lentils, 2 cups water, broth, garlic, bay leaf and ½ teaspoon salt in a saucepan. Cover and bake until lentils are tender but remain intact – 40 to 60 minutes.
3. Whisk oil and vinegar in a bowl.
4. Drain lentils well; remove and discard the garlic and bay leaf. Add drained lentils, olives, mint and shallot in a bowl. Drizzle on the oil and vinegar dressing, season with salt and pepper and toss. Sprinkle with feta cheese to serve.

Source: CooksIllustrated.com is an online recipe subscription with more information as to the science behind the cooking.

Debra DeMille, MS, RD, CSO, is a nutritional counselor at the Abramson Cancer Center at Penn Medicine Pennsylvania Hospital. Dietitians at the Abramson Cancer Center provide educational programs about nutrition that are open to patients as well as the community. Cancer-fighting recipes on this blog are the product of the quarterly series “Cooking Nutritious and Delicious Foods,” which promotes seasonal healthy foods with cancer-fighting properties.

Protein phosphatase 2A (PP2A) negatively regulates tumorigenic signaling pathways, in part, by supporting the function of tumor suppressors like p53. The PP2A methylesterase PME-1 limits the activity of PP2A by demethylating its catalytic subunit. Here, we report the finding that PME-1 overexpression correlates with increased cell proliferation and invasive phenotypes in endometrial adenocarcinoma cells, where it helps maintain activated ERK and Akt by inhibiting PP2A. We obtained evidence that PME-1 could bind and regulate protein phosphatase 4 (PP4), a tumor-promoting protein, but not the related protein phosphatase 6 (PP6). When the PP2A, PP4, or PP6 catalytic subunits were overexpressed, inhibiting PME-1 was sufficient to limit cell proliferation. In clinical specimens of endometrial adenocarcinoma, PME-1 levels were increased and we found that PME-1 overexpression was sufficient to drive tumor growth in a xenograft model of the disease. Our findings identify PME-1 as a modifier of malignant development and suggest its candidacy as a diagnostic marker and as a therapeutic target in endometrial cancer. Cancer Res; 74(16); 1–11. ©2014 AACR.

Cancer stem cells, capable of self-renewal and multipotent differentiation, influence tumor behavior through a complex balance of symmetric and asymmetric cell divisions. Mechanisms regulating the dynamics of stem cells and their progeny in human cancer are poorly understood. In Drosophila, mutation of brain tumor (brat) leads to loss of normal asymmetric cell division by developing neural cells and results in a massively enlarged brain composed of neuroblasts with neoplastic properties. Brat promotes asymmetric cell division and directs neural differentiation at least partially through its suppression on Myc. We identified TRIM3 (11p15.5) as a human ortholog of Drosophila brat and demonstrate its regulation of asymmetric cell division and stem cell properties of glioblastoma (GBM), a highly malignant human brain tumor. TRIM3 gene expression is markedly reduced in human GBM samples, neurosphere cultures, and cell lines and its reconstitution impairs growth properties in vitro and in vivo. TRIM3 expression attenuates stem-like qualities of primary GBM cultures, including neurosphere formation and the expression of stem cell markers CD133, Nestin, and Nanog. In GBM stem cells, TRIM3 expression leads to a greater percentage dividing asymmetrically rather than symmetrically. As with Brat in Drosophila, TRIM3 suppresses c-Myc expression and activity in human glioma cell lines. We also demonstrate a strong regulation of Musashi–Notch signaling by TRIM3 in GBM neurospheres and neural stem cells that may better explain its effect on stem cell dynamics. We conclude that TRIM3 acts as a tumor suppressor in GBM by restoring asymmetric cell division. Cancer Res; 74(16); 1–13. ©2014 AACR.

Pentraxin-3 (PTX3) is a member of the pentraxin family of innate immune regulators, which includes C-reactive protein (CRP). PTX3 has been implicated in angiogenesis, proliferation, and immune escape in cancer. In the present study, we evaluated PTX3 tissue expression and serum concentration as a biomarker to discriminate prostatic inflammation and benign prostatic hyperplasia (BPH) from prostate cancer, and to determine whether PTX3 status may predict progression from BPH to prostate cancer. We analyzed 40 patients with biopsy-proven BPH who underwent a second prostate biopsy 12 to 36 months later when they were diagnosed with prostate cancer or inflammation/BPH (n = 20 patients each group). Furthermore, we evaluated PTX3 serum concentrations in an independent set of patients with biopsy-proven inflammation/BPH (n = 61) and prostate cancer (n = 56). We found reduced PTX3 tissue expression in patients with prostatic inflammation/BPH compared with patients who developed prostate cancer. In the latter group, there was an increase in PTX3 tissue expression between the first and second prostate biopsy. PTX3 serum levels were also higher in patients with prostate cancer than in patients with inflammation/BPH. In contrast, there was no difference in serum PSA or CRP levels in these two groups. ROC curve analysis confirmed the reliability of PTX3 serum levels in predicting prostate cancer development, identifying a cutoff value of 3.25 ng/mL with a sensitivity and a specificity of 89.3% and 88.5%, respectively. In summary, our results encourage further evaluation of PTX3 as a tissue biopsy and blood-borne biomarker to discriminate BPH from prostate cancer. Cancer Res; 74(16); 1–9. ©2014 AACR.