A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

Depletion of a subset of 70K stress proteins in yeast mutants shows that they are involved in the post-translational import of precursor polypeptides into both mitochondria and the lumen of the endoplasmic reticulum. The identification of such a basic function may explain the remarkable evolutionary conservation of the gene family encoding these proteins.     

Fc receptor phosphorylation during receptor-mediated control of B-cell activation

It is well known that Fc receptors for IgG (FcRII) on macrophages mediate the endocytosis of antibody-antigen complexes and signal the release of inflammatory and cytotoxic agents. FcRII are also expressed at high levels on B cells where they are less involved in endocytosis than in modulating B-cell activation by membrane immunoglobulins. Although crosslinking of membrane immunoglobulins can result in B-cell differentiation and proliferation through stimulation of phospholipase C, mobilization of intracellular Ca2+, and activation of protein kinase C, crosslinking FcR with membrane immunoglobulins confers a dominant inhibitory signal that prevents or aborts activation. This form of regulation may have a role in the induction of tolerance by IgG and in controlling the B-cell repertoire by anti-idiotypes. The different functions of FcR on B cells and macrophages may reflect the fact that these cell types express closely related but distinct FcR isoforms. We have recently found that the main lymphocyte FcR isoform, FcRII-B1, is unable to mediate endocytosis by way of coated pits and coated vesicles owing to an in-frame insertion of 47 amino acids in its cytoplasmic tail. Here we show that this insert, absent from the FcRII-B2 macrophage isoform, also contains serine phosphorylation sites that may have a role in the ability of FcR to regulate B-cell activation through membrane immunoglobulins.     

Changes in intracellular pH and cell volume during the early phase of DMSO-induced differentiation of friend erythroleukemia cells

Summary Changes in intracellular pH and water volume were measured after treatment of Friend erythroleukemia cells with 1.5% DMSO. It was found that a continuous decrease in pH_i occurred, beginning 1 h after induction and a decline in pH_i of 0.18 was measured after 9 h. In addition a decline in cellular water volume, of 12% only 15 min after induction, and 23% after 9 h, was observed.11 December 1986Acknowlegments. This work was supported by the Deutsche Forschungsgemeinschaft.     

Silymarin,an inhibitor of prostaglandin synthetase

Summary Silybin (I), silydianin (II) and silychristin (III), the main constituents of silymarin, inhibit the formation of prostaglandins in vitro. The inhibition is log-linearly dependent on the concentration of the effectors.F. Fiebrich, Thesis, University of Vienna 1977.H. Koch, Dt. ApothZtg118, 1844 (1978); reported in part at the Colloquium Pharmaceuticum in Münster, 21st November 1978.