The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1 carcinoma-associated antigen with GSK3 beta and beta-catenin

The DF3/MUC1 mucin-like glycoprotein is aberrantly overexpressed in most human carcinomas. The cytoplasmic domain of MUC1 interacts with glycogen synthase kinase 3 beta (GSK3 beta) and thereby decreases binding of MUC1 and beta-catenin. The present studies demonstrate that MUC1 associates with the c-Src tyrosine kinase. c-Src phosphorylates the MUC1 cytoplasmic domain at a YEKV motif located between sites involved in interactions with GSK3 beta and beta-catenin. The results demonstrate that the c-Src SH2 domain binds directly to pYEKV and inhibits the interaction between MUC1 and GSK3 beta. Moreover and in contrast to GSK3 beta, in vitro and in vivo studies demonstrate that c-Src-mediated phosphorylation of MUC1 increases binding of MUC1 and beta-catenin. The findings support a novel role for c-Src in regulating interactions of MUC1 with GSK3 beta and beta-catenin.     

Retrograde evolution of Albaillella during the Permian-Triassic crisis

In the present paper, we discuss the evolution of an upper Permian anagenetic lineage of polycystine radiolarians belonging to the genus Albaillella. This genus is characterized by increasing curvature of the shell during the upper Permian and the trend is reversed (proteromorphic retrogradation) in the Lower Triassic with the sudden appearance of forms that are homeomorphic to the earliest Permian representative of the genus. These primitive-looking forms are derived from their immediate ancestors by retrograde evolution, a phenomenon which has been described as proteromorphosis.     

Effective Purification of Nonspecific Cross-Reacting Antigens with Phosphatidylinositol-Specific Phospholipase C

ABSTRACT

Two molecular species of nonspecific cross-reacting antigens, NCA-90 and NCA-50 with mol. wts. of 90,000 and 50,000, respectively, wereeffectively extracted with phosphatidylinositol-specific phospholipase C (PI-PLC) from human lung tissues, followed by extraction with perchloric acid, immunoaffinity chromatography with anti-NCA adsorbent, and gel filtration on a TSK G3000SW column. The yields of NCA were about 2 times more than those obtained by the usual method without PI-PLC. Addition of 0.05 unit of PI-PLC to 1 g of lung tissue and incubation at 37°C for 1 h with continuous shaking seem to be practically sufficient for NCA extraction. The immunochemical properties of the NCAs thus obtained were found to be identical to those of NCAs obtained by the ordinary method.