Lymphocyte transformation by Pim-2 is dependent on nuclear factor-kappaB activation.

Pim-2 is a transcriptionally regulated oncogenic kinase that promotes cell survival in response to a wide variety of proliferative signals. Deregulation of Pim-2 expression has been documented in several human malignancies, including leukemia, lymphoma, and multiple myeloma. Here, we show that the ability of Pim-2 to promote survival of cells is dependent on nuclear factor (NF)-kappaB activation.

The PP2A-associated protein alpha4 is an essential inhibitor of apoptosis.

Despite evidence that protein kinases are regulators of apoptosis, a specific role for phosphatases in regulating cell survival has not been established. Here we show that alpha4, a noncatalytic subunit of protein phosphatase 2A (PP2A), is required to repress apoptosis in murine cells. alpha4 is a nonredundant regulator of the dephosphorylation of the transcription factors c-Jun and p53.

Three immunoassays based on monoclonal antibodies specific for prostate specific antigen (PSA), alpha-1-antichymotrypsin (ACT), and the PSA-ACT complex.

Background: Prostate specific antigen (PSA) has been widely used as a biomarker for the screening and diagnosis of prostate cancer. PSA in serum predominantly exists as a complex with alpha-1-antichymotrypsin (ACT), and measurement of free PSA and the PSA-ACT complex may improve the utility of the serum PSA assay for differential diagnosis of prostate cancer and non-malignant prostate diseases, such as benign prostatic hyperplasia (BPH).

Methods: Monoclonal antibodies (MAbs) against PSA, ACT, and the PSA-ACT complex were produced by immunizing mice with an incubated mixture of PSA and ACT, and characterized by Western blot analyses and several enzyme-linked immunosorbant assay (ELISA) methods.

Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis.

Cross-talk between calpain and caspase proteolytic systems has complicated efforts to determine their distinct roles in apoptotic cell death. This study examined the effect of overexpressing calpastatin, the specific endogenous calpain inhibitor, on the activity of the two proteolytic systems following an apoptotic stimulus. Human SH-SY5Y neuroblastoma cells were stably transfected with full-length human calpastatin cDNA resulting in 20-fold overexpression based on Western blot and 5-fold greater calpain inhibitory activity in cell extracts.

Comparison of calpain and caspase activities in the adult rat brain after transient forebrain ischemia.

The role of calpain and caspase family proteases in postischemic neuronal death remains controversial. This study compared the timing, location, and relative activity of calpains and caspases in the adult rat brain following 10 min of transient forebrain ischemia. Western blots of cortical, striatal, and hippocampal homogenates demonstrated a alpha-spectrin cleavage pattern indicative of predominant calpain activity, which peaked between 24 and 48 h after reperfusion.