MRI and MRSI have the potential to identify cancer foci and direct TRUS in patients with a previous negative TRUS biopsy. Further, larger studies are required to quantify the amount of benefit.

Background : A filled bladder acts as an acoustic window for transabdominal ultrasound measurements of intravesical prostatic protrusion and volume. The aim of this study is to evaluate the effects of bladder volume on transabdominal ultrasound measurements of these parameters. Methods : Twenty-two patients undergoing transurethral resection of the prostate (TURP) were studied. Under general anesthesia just before TURP, a transrectal ultrasound measurement of prostate volume was obtained. The bladder was then filled in a stepwise manner with 100, 200, 300, 400 and 500 mL. At each volume, the intravesical prostatic protrusion and prostatic volume were measured transabdominally using ultrasound.Results : There was an obvious trend of decreasing mean transabdominal intravesical prostatic protrusions with increasing bladder volume. The mean transabdominal intravesical prostatic protrusion at bladder volumes 100, 200, 300, 400 and 500 mL was 9.1, 8.8, 7.4, 5.8 and 4.6 mm, respectively. The bladder volume at which maximum prostatic protrusion occurred was between 100 and 200 mL. The mean transabdominal prostate volume at the five increasing bladder volumes was 50.6, 48.7, 49.2, 47.9 and 41.4 mL, and these were correlated to transrectal prostate volume, particularly when the bladder volume was less than 400 mL. Conclusions : Transabdominal ultrasound measurement of prostatic protrusion is dependent on bladder volume. Transabdominal ultrasound measurement of prostatic volume correlates well with the transrectal measurement of the same parameter when the bladder volume is less than 400 mL.

Tumor-specific antibody drugs can serve as cancer therapy with minimal side effects. A humanized antibody, PRL3-zumab, specifically binds to an intracellular oncogenic phosphatase PRL3, which is frequently expressed in several cancers. Here we show that PRL3-zumab specifically inhibits PRL3 + cancer cells in vivo, but not in vitro. PRL3 antigens are detected on the cell surface and outer exosomal membranes, implying an ‘inside-out’ externalization of PRL3. PRL3-zumab binds to surface PRL3 in a manner consistent with that in classical antibody-dependent cell-mediated cytotoxicity or antibody-dependent cellular phagocytosis tumor elimination pathways, as PRL3-zumab requires an intact Fc region and host FcγII/III receptor engagement to recruit B cells, NK cells and macrophages to PRL3 + tumor microenvironments. PRL3 is overexpressed in 80.6% of 151 fresh-frozen tumor samples across 11 common cancers examined, but not in patient-matched normal tissues, thereby implicating PRL3 as a tumor-associated antigen. Targeting externalized PRL3 antigens with PRL3-zumab may represent a feasible approach for anti-tumor immunotherapy.