Den′ichi Mizuno

In Vitro Induction of Antibody‐Dependent Cytotoxic Macrophages by the Local Anesthetic Lidocaine

Normal macrophages were activated to antibody‐dependent cytotoxic effector cells by in vitro treatment with the local anesthetic lidocaine. Experiments on the dose‐response and time course of the effect of lidocaine showed that incubation of normal macrophages with 10 mM lidocaine for 10 min at 28 C was enough for induction of antibody‐dependent cellular cytotoxicity. The activation by lidocaine was accompanied by enhanced phagocytosis of sheep red blood cells (SRBC) sensitized with anti‐SRBC antiserum, but not enhanced ingestion of polystyrene latex particles (PLP). These findings suggest that lidocaine, which has various effects on cell membranes, induces some perturbation of macrophage membranes, resulting in activation of Fc receptor functions in antibody‐dependent cytotoxicity and phagocytosis.

SEPARATION OF A STIMULATORY FACTOR OF RNA POLYMERASE II FROM PROTEIN KINASE ACTIVITY OF EHRLICH ASCITES TUMOR CELLS

The regulation of eukaryotic gene expression is one of the most exciting problems in modern biology. Since Roeder and Rutter reported the multiple forms of eukaryotic RNA polymerase [l] , extensive studies have been done on the purification of these enzymes. Along with the purification of the enzymes, there have been many papers reporting the factors stimulating these enzymes, especially RNA polymerase II [2-61. These factors are expected to play important roles in the regulation of eukaryotic transcription. In order to elucidate the function of these factors, we purified one of these factors, named S-II, from Ehrlich ascites tumor cells [7] . This factor is a basic protein having molecular weight of 38 000 and stimulates only RNA polymerase II and distinctly insensitive to RNA polymerase I. The stimulation cannot be detected when poly [d(A-T) is used as template under the conditions where more than tenfold stimulation is obtained with homologous DNA as template. Recently, Dahmus showed that a stimulatory factor of RNA polymerase II from Novikoff hepatoma cells, named HLF2, contained protein kinase activity [8] . He proposed that phosphorylation of RNA polymerase II by this factor was required for the subsequent stimulation of RNA synthesis. In this paper we report results showing that S-II could not be copuritied with protein kinase and that protein kinase activity was not essential for the stimulation of RNA polymerase II. 2. Methods

Translational activity and fidelity of purified ribosomes from aging mouse livers.

Since early years of modern molecular biology, it has been suggested that there must be some functional changes in the flow of genetic information which are almost universal to any type of cells, and hence very likely to be a general cause of functional deterioration during the aging of animals (1,2). In fact, various aspects of transcription and translation have been studied in relation to both the aging of tissues in vivo and cells in culture (3, 4).