Stereoselectivity in mammalian chemical communication: Male mouse pheromones

Two male mouse pheromones, 3,4-dehydro-exo-brevicomin (DHB) and 2-sec-butyldihydrothiazole (SBT), are chiral molecules which were previously tested in their respective bioasays as racemic mixtures. The focus of this study has been to determine the absolute configuration of their natural forms and its relation to stereospecific biological action. DHB was established as the R,R-enantiomer possessing biological activity. Due to an extremely easy racemization of SBT under very mild conditions, enantioselectivity of its transmission and its action at the receptor site appear to be of secondary importance.     

The electrophysiological effects of ionophore X-537A on cardiac Purkinje fibres

Summary Using classical microelectrode techniques in canine cardiac Purkinje fibres, calcium ionophore X-537A was shown to shorten the action potential, hyperpolarizing the membrane and lowering the plateau, suggesting that intracellular calcium controls membrane permeability to potassium in this preparation.This work was supported by grant No. HL 05726 from the U.S. Public Health Service, National Heart Institute, Bethesda, Md.I thank Dr.N. Krasnow for his valuable advice in carrying out this work.     

Effect of conditioned media on nerve cell differentiation

Summary Glial conditioned medium strongly stimulates the morphological maturation of cultured neuronal cells, while fibroblast and meningeal conditioned media have weaker effects.Acknowledgment. We acknowledge the expert technical assistance of Mrs M.F. Knoetgen.     

Estrogen receptor in uteri of mice of different H-2 genotypes.

A relationship between the amount of available estradiol receptors in uteri of inbred mice and their H-2 genotype is suggested by study in congenic animals.     

Regulation of non-muscle myosin assembly by calmodulin-dependent light chain kinase

The presence of actin and myosin in non-muscle cells suggests that they may be involved in a wide range of cellular contractile activities. The generally accepted view is that interaction between actin and myosin in these cells and in vertebrate smooth muscle, is regulated by the level of phosphorylation of the 20,000-molecular weight (MW) light chain. In the absence of calcium, this light chain is not phosphorylated and the myosin cannot interact with actin. Calcium activates a specific calmodulin-dependent kinase which phosphorylates the light chain, initiating actin-myosin interaction. Although most studies on the role of phosphorylation have concentration on the regulation of actin-activated myosin Mg-ATPase activity, phosphorylation of the light chain also seems to control the assembly of smooth muscle myosin into filaments. Using purified smooth muscle light chain kinase, we have confirmed this observation. We report here studies of myosins isolated from the two non-muscle sources, thymus cells and platelets. We observed that these myosins are assembled into filaments at physiological ionic strength and Mg-ATP concentrations, only when the 20,000-MW light chain is phosphorylated.