Hypoxia-induced expression of complement receptor type 1 (CR1, CD35) in human vascular endothelial cells.

Reoxygenation of hypoxic human umbilical vein endothelial cells (HUVECs) increases protein expression of the complement regulators CD46 and CD55. As the receptor for C3b is known to be present on injured bovine endothelial cells, we investigated whether hypoxia or inflammatory mediators induce complement receptor type 1 (CR1; CD35) expression on HUVECs. CR1 protein expression increased 3.

Local anesthetics inhibit the G protein-mediated modulation of K+ and Ca++ currents in anterior pituitary cells.

The effects of local anesthetics (LAs) on G protein-mediated responses of voltage-dependent K+ (I(K)) and Ca++ currents in rat anterior pituitary tumor (GH3) cells were analyzed by using a whole-cell voltage clamp. Extracellular lidocaine inhibited I(K) with an IC50 of 1.9 mM, comparable to 2.

Reoxygenation of hypoxic human umbilical vein endothelial cells activates the classic complement pathway.

Background: Ischemia-reperfusion injury leads to the activation and endothelial deposition of complement. We investigated whether exposure of human umbilical vein endothelial cells (HUVECs) to hypoxia and/or reoxygenation activates complement and decreases HUVEC-surface expression of the C3 regulatory proteins CD46 and CD55.

Methods And Results: HUVECs were subjected to 0, 12, or 24 hours of hypoxia (O2 = 1%) and then reoxygenated for 3 hours (O2 = 21%) in the presence of 30% human serum.

Propofol and ethanol produce additive hypnotic and anesthetic effects in the mouse.

The sedative and anesthetic effects of ethanol and propofol when these drugs are coadministered are not known. Accordingly, we investigated the nature of the pharmacological interaction between ethanol and propofol during hypnosis and anesthesia in the mouse. Propofol, ethanol, and mixtures of the two were administered through the tail vein in male CD-1 mice (n = 162).

Estrogen-specific target site identified by progesterone-11 alpha-hemisuccinate-(2-[125I]-iodohistamine) in mouse brain membranes.

Using photoaffinity labeling with the progesterone analogue, progesterone-11 alpha-hemisuccinate-(2-[125I]-iodohistamine) ([125I]-his-PG), we identified and characterized a protein band of MW 29 kDa (p29) in mouse cerebellar membranes whose labeling is markedly inhibited by estrogens. Inhibition of the labeling was specific with respect to steroid structure. Labeling was strongly inhibited by estradiol-17 beta, estradiol-17 alpha, and the anti-estrogen tamoxifen and the synthetic estrogen diethylstilbestrol.