Bovine lymphocyte antigens: serological relationships with erythrocyte and spermatozoan antigens.

Bovine lymphocytotoxicity tests with 20 unabsorbed bovine blood group sera revealed extensive reactivity which in the majority of cases had no indication of blood group relationship. Six of these sera were absorbed with selected lymphocytes to produce eleven antisera of reduced specificity. Again, most of the sera had reaction patterns which could not be related to the hemolytic patterns of any known blood group antibodies. However, five comparisons involving unabsorbed antisera and two comparisons involving absorbed antisera provided statistical evidence of similarities between their lymphocytotoxic reaction patterns and the hemolytic reaction patterns of certain blood group antibodies. Several of the sera appeared to contain related cytotoxic specificities, and three such absorbed sera may have contained an anti-J specificity. All six examined monospecific isoimmune blood group antisera contained lymphocytic reactivities not related to their hemolytic specificities. Two normal sera containing naturally occurring anti-J had no cytotoxic activity. Anti-semen sera likewise were devoid of lymphocytotoxic activity.     

EDC3 phosphorylation regulates growth and invasion through controlling P‐body formation and dynamics

Regulation of mRNA stability and translation plays a critical role in determining protein abundance within cells. Processing bodies (P‐bodies) are critical regulators of these processes. Here, we report that the Pim1 and 3 protein kinases bind to the P‐body protein enhancer of mRNA decapping 3 (EDC3) and phosphorylate EDC3 on serine (S)161, thereby modifying P‐body assembly. EDC3 phosphorylation is highly elevated in many tumor types, is reduced upon treatment of cells with kinase inhibitors, and blocks the localization of EDC3 to P‐bodies. Prostate cancer cells harboring an EDC3 S161A mutation show markedly decreased growth, migration, and invasion in tissue culture and in xenograft models. Consistent with these phenotypic changes, the expression of integrin β1 and α6 mRNA and protein is reduced in these mutated cells. These results demonstrate that EDC3 phosphorylation regulates multiple cancer‐relevant functions and suggest that modulation of P‐body activity may represent a new paradigm for cancer treatment.