Preserved forearm endothelial responses with acute exposure to progesterone: A randomized cross-over trial of 17-beta estradiol, progesterone, and 17-beta estradiol with progesterone in healthy menopausal women.

Regularly menstruating women are relatively protected from cardiovascular disease. Epidemiological and endothelial function studies attribute this protection to estradiol (E(2)), but both progesterone (P) and E(2) are normally present. A range of vascular effects of added progestins have been described, from neutral to detrimental, but the effects of P per se on endothelial function in humans have not been reported. We therefore investigated the acute effects of E(2), P, and E(2) combined with P, on endothelium-dependent and -independent forearm blood flow responses. Using venous occlusion plethysmography, forearm blood flow (FBF) was measured during acute brachial artery infusions, achieving physiologic levels of 17-beta-E(2), P, and 17-beta-E(2) with P in healthy menopausal women with no cardiovascular disease risk factors. Vehicle or hormones were infused, in random order, on 4 days, 1 week apart. Flow responses were measured during coinfusions of hormone with the endothelium-dependent vasodilator acetylcholine and the endothelium-independent vasodilator sodium nitroprusside. Twenty-seven healthy menopausal women were studied, and all had normal baseline endothelial responses. Small ( approximately 15%), statistically nonsignificant increases in endothelium-dependent flow responses were seen after all acute hormone treatments. No impairment in response was seen with P alone or in combination with 17-beta-E(2). In healthy menopausal women without cardiovascular disease risk factors and without baseline defects in endothelial function, acute exposure to physiologic levels of 17-beta-E(2), P, and 17-beta-E(2) with P produced equivalent endothelium-dependent responses. These data suggest that P does not have detrimental vascular effects in humans.

Immediate Activation of Respiration in Petroselinum crispum L. in Response to the Phytophthora megasperma f. sp. Glycinea Elicitor.

Treatment of parsley (Petroselinum crispum L.) cell cultures with the Phytophthora megasperma elicitor isolated from the fungus Phytophthora megasperma f. sp. Glycinea caused an immediate increase in the rate of respiratory CO2 evolution in the dark. The respiratory response was biphasic, showing a rapid enhancement in the first 20 min and then a slower increase until a steady rate was attained 60 min posttreatment. The enhanced rate of CO2 evolution corresponded to the activation of phosphofructokinase and glucose-6-phosphate dehydrogenase, key enzymes in the regulation of carbohydrate flow to glycolysis and the oxidative pentose phosphate (OPP) pathway, respectively. The increased rate of CO2 evolution and the activation of phosphofructokinase and glucose-6-phosphate dehydrogenase were maintained for the duration of the experiments, indicating long-term stimulation of respiration through both glycolysis and the OPP pathway. A 23% decrease in the C6:C1 ratio of 14CO2 evolution from labeled glucose 60 min after the addition of Phytophthora megasperma elicitor is consistent with an increased contribution of the OPP pathway to cellular respiration. Long-term activation of the OPP pathway following elicitation could serve to maintain the pools of substrates necessary during activation of the shikimic acid pathway, leading to the production of defensive compounds.

Purification and Characterization of Phosphoglycolate Phosphatase from the Cyanobacterium Coccochloris peniocystis.

The properties and role of the enzyme phosphoglycolate phosphatase in the cyanobacterium Coccochloris peniocystis have been investigated. Phosphoglycolate phosphatase was purified 92-fold and had a native molecular mass of approximately 56 kilodaltons. The enzyme demonstrated a broad pH optimum of pH 5.0 to 7.5 and showed a relatively low apparent affinity for substrate (K(m) = 222 micromolar) when compared to that from higher plants. The enzyme required both an anion and divalent cation for activity. Mn(2+) and Mg(2+) were effective divalent cations while Cl(-) was the most effective anion tested. The enzyme was specific for phosphoglycolate and did not show any activity toward a variety of organic phosphate esters. Growth of the cells on high CO(2) and transfer to air did not result in any significant change in phosphoglycolate phosphatase activity. Competitive inhibition of C. peniocystis triose phosphate isomerase by phosphoglycolate was demonstrated (K(i) = 12.9 micromolar). These results indicate the presence of a specific noninducible phosphoglycolate phosphatase whose sole function may be to hydrolyze phosphoglycolate and prevent phosphoglycolate inhibition of triose phosphate isomerase.