Hydration pressure and phase transitions of phospholipids: I. Piezotropic approach

Dehydration reduces the main phase transition pressure of phospholipids. An analysis based on the Gibbs-Duhem equation shows how the shift of the transition pressure is correlated to the hydration pressure.By using Fourier transform infrared (FT-IR) spectroscopy we determined the hydration-dependent phase transition pressure. The application of our new approach gives hydration pressure values which agree with the values obtained with the osmotic stress method.     

Antennal sensory organs in the millipede Eurypauropus ornatus: Fine structure of the flagella and globulus

On the antennal tip of Eurypauropus ornatus are 3 threadlike sensilla—the flagella, and a single spheroid sensillum—the globulus. Each of the 3 flagella is innervated by 2 groups of sensory cells. One group contains 4 cells, the other, 5. All cells of the “four group” and 3 of the “five group” are comprised of single cilia and unbranched dendrites which extend along the lumen of the flagellum. Two cells of the “five group” have double cilia and pairs of unbranched dendrites. One pair also enters the flagellum and the other pair terminates beneath the flagellar base to form a concentric array of lamellae. No pores are present in the cuticular wall. Eight sensory cells innervate the globulus. They are arranged in 3 groups, one triplet and 2 pairs, in addition to a single cell. The single cell contains a pair of cilia whose unbranched dendrites differentiate into tubular bodies that are inserted into the base of the globulus. Each of the other 7 sensory cells has a single cilium. Their unbranched dendrites penetrate into the globulus in 3 groups as described for the sensory cells. The dendrites in each group terminate in an individual pore channel at the globulus tip and completely fuse with the electron-dense material that plugs the pore channel. Based on structural similarities to sensilla having known functions, it is probable that the flagella and the globulus are chemoreceptors, the former responding to odors, the latter sensitive to substances in aqueous solution.     

Sexual differentiation in Mucor: Trisporic acid response mutants and mutants blocked in zygospore development

Spores of a minus strain of Mucor mucedo (Bref.) were treated with 1-methyl-[3-nitro]-1-nitro-soguanidine and mutants were isolated either by testing for zygophore induction with externally supplied trisporic acids (TA) or by mating with wild type plus colonies. Mutants were found defective (Tar^?) or temperature-sensitive (Tar-Ts) in their reaction towards trisporic acids, blocked or temperature-sensitive in their mating with plus strain (Mat^? or Mat-Ts) or temperature-sensitive in zygospore development (Zyg-Ts). The inability to react against externally supplied trisporic acids was not necessarily coupled with an inability to mate with plus strain (phenotype Tar^? Mat⁺). This indicated that the diffusion and uptake of trisporic acids is not a necessary prerequisite to the sexual interaction of Mucor mating types.     

Inositol Phospholipid Hydrolysis by Rat Sciatic Nerve Phospholipase C

Rat sciatic nerve cytosol contains a phosphodiesterase of the phospholipase C type that catalyzes the hydrolysis of inositol phospholipids, with preferences of phosphatidylinositol 4'-phosphate (PIP) greater than phosphatidylinositol (PI) much greater than phosphatidylinositol 4',5'-bisphosphate (PIP2), at a pH optimum of 5.5-6.0 and at maximum rates of 55, 13, and 0.7 nmol/min/mg protein, respectively. Analysis of reaction products by TLC and formate exchange chromatography shows that inositol 1,2-cyclic phosphate (83%) and diacylglycerol are the major products of PI hydrolysis. [32P]-PIP hydrolysis yields inositol bisphosphate, inositol phosphate, and inorganic phosphate, indicating the presence of phosphodiesterase, phosphomonoesterase, and/or inositol phosphate phosphatase activities in nerve cytosol. Phosphodiesterase activity is Ca2+-dependent and completely inhibited by EGTA, but phosphomonoesterase activity is independent of divalent cations or chelating agents. Phosphatidylcholine (PC) and lysophosphatidylcholine (lysoPC) inhibit PI hydrolysis. They stimulate PIP and PIP2 hydrolysis up to equimolar concentrations, but are inhibitory at higher concentrations. Both diacylglycerols and free fatty acids stimulate PI hydrolysis and counteract its inhibition by PC and lysoPC. PIP2 is a poor substrate for the cytosolic phospholipase C and strongly inhibits hydrolysis of PI. However, it enhances PIP hydrolysis up to an equimolar concentration.     

Phosphorylation determines two distinct species of Tau in the central nervous system

The monoclonal antibody, Tau-1, which had previously been used to localize tau to the axonal compartment in brain has been reutilized for light and electron microscopic immunohistochemistry following phosphatase treatment of tissue. We report here that a significant quantity of tau in the central nervous system is phosphorylated in situ at or near the Tau-1 epitope, preventing the binding of the Tau-1 antibody. Upon removal of this/these phosphate group(s), however, Tau-1 was observed in the somatodendritic compartment of neurons as well as in axons. Furthermore, intense staining was also observed in astrocytes and in perineuronal glial cells. This immunoreactivity was present along the lengths of microtubules and on ribosomes (polysomes). Treatment of immunoblots of extracts of whole cerebral cortex with phosphatase confirmed the immunohistochemical results in that a 50-65% increase in Tau-1 binding to the tau region of the blot was noted. Moreover, a novel monoclonal antibody, Tau-2, was also used in these experiments. This antibody binds only to tau and localizes along microtubules in axons, somata, dendrites, and astrocytes and on ribosomes (polysomes) without phosphatase pretreatment.