THE STIGMATIC SECRETION OF THE SWEETPOTATO

The stigmatic exudate of sweetpotato, when removed with organic solvents, consisted chiefly of lipid and phenolic compounds. Only traces of sugar were obtained. The esterified lipids were similar in chain length to capric and lauric acids. The two prinicpal phenolic compounds have UV absorption peaks, and bathochromic shifts on ionization with NaOH similar to those of esters of caffeic acid. On acid hydrolysis, caffeic acid was obtained from these and from three minor phenolic compounds. From two of the minor phenolic compounds, glucose was released by hydrolysis. The phenolic content of stigmas increased up to 20–24 hr before anthesis, and then gradually decreased. Neither compatible nor incompatible pollination affects the amount or composition of the stigmatic exudate.     

Habitat use and population biology of the Danube Clouded Yellow butterfly Colias myrmidone (Lepidoptera: Pieridae) in Romania

The Danube Clouded Yellow (Colias myrmidone) is one of the most endangered butterflies in Europe. Its distribution range shrank dramatically in the last few decades due to the extinction of populations in Western and Central Europe. Ecological studies were commenced when populations were already at the verge of extinction, thus our knowledge on the population ecology and habitat use of this butterfly is very limited. Here we report the results of a study on habitat preferences, egg distribution and demography of C. myrmidone in Romania, perhaps the last remaining stronghold of the species in Central Europe. We found that Danube Clouded Yellow adults occurred mainly in mesophilous grasslands created by forest clearing and then maintained by low intensity grazing allowing bushes and forest-edge vegetation to develop and host Chamaecytisus species to grow. Butterflies highly preferred lightly grazed pastures over hay meadows and abandoned grasslands, their density was positively related to host plant density. Egg-laying females preferred habitat patches with relatively high cover of the host plant and tall vegetation. Both apparent survival rate and encounter probability were lower for females than males, and parameter estimations also had much higher errors for females. These indicate that much higher sampling effort is needed to estimate and monitor population parameters for females than for males. Our results provide guidelines for the habitat management and population monitoring of Colias myrmidone, thus may significantly contribute to its successful conservation.     

Overexpression of protein kinase C-epsilon and its regulatory domains in fibroblasts inhibits phorbol ester-induced phospholipase D activity

In fibroblasts, the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) stimulates phospholipase D (PLD)-mediated hydrolysis of both phosphatidylcholine (PtdCho) and phosphatidylethanolamine (PtdEtn) by PKC-alpha-mediated nonphosphorylating and phosphorylating mechanisms. Here we have used NIH 3T3 fibroblasts overexpressing holo PKC-epsilon and its regulatory, catalytic, and zinc finger domain fragments to determine if this isozyme also regulates PLD activity. Overexpression of holo PKC-epsilon inhibited the stimulatory effects of PMA (5-100 nM) on both PtdCho and PtdEtn hydrolysis. Overexpression of PKC-epsilon also was found to inhibit platelet-derived growth factor-induced PLD activity. Expression of the catalytic unit of PKC-epsilon had no effect on PMA-induced PLD activity. In contrast, expression of both the regulatory domain fragment and the zinc finger domain of PKC-epsilon resulted in significant inhibition of PMA-stimulated PtdCho and PtdEtn hydrolysis. Interestingly, although PKC-alpha also mediates the stimulatory effect of PMA on the synthesis of PtdCho by a phosphorylation mechanism, overexpression of holo PKC-epsilon or its regulatory domain fragments did not affect PMA-induced PtdCho synthesis. These results indicate that the PKC-epsilon system can act as a negative regulator of PLD activity and that this inhibition is mediated by its regulatory domain.