scholarly journals Nonspecific esterase activity expressed in Weibel-Palade bodies of cloned guinea pig aortic endothelial cells.

1987 ◽  
Vol 35 (5) ◽  
pp. 531-539 ◽  
Author(s):  
R A Monahan-Earley ◽  
T Isomura ◽  
R I Garcia ◽  
S J Galli ◽  
H F Dvorak ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Guinea Pig ◽  
Esterase Activity ◽  
Nonspecific Esterase ◽  
Aortic Endothelial Cells ◽  
Membrane Bound ◽  
Von Willebrand ◽  
Naphthyl Acetate ◽  
Nonspecific Esterase Activity ◽  
Aortic Endothelial

We studied the localization of nonspecific esterase activities in cloned guinea pig aortic endothelial cells using ultrastructural cytochemistry. Weibel-Palade bodies (WPB), which are known to contain von Willebrand protein, were positive for esterase, defining a heretofore unrecognized activity of these organelles. Esterase activity was also found localized to the external surface of the plasma membrane, to cytoplasmic lipid bodies, and to the outer (cytoplasm-facing) surface of certain membrane-bound cytoplasmic vacuoles. Localization of esterase activity to these four discrete sites probably reflects the presence of a number of endothelial cell enzymes capable of hydrolyzing alpha-naphthyl acetate or butyrate. The physiological substrate and biological function of these enzyme activities are not presently understood.

scholarly journals Cultured Normal and von Willebrand Porcine Aortic Endothelial Cells-An in Vitro Model for Studying the Nature and Site of Platelet-Endothelial Component Interaction

1977 ◽  
Author(s):  
F.M. Booyse ◽  
D.N. Fass ◽  
E.J.W. Bowie
Keyword(s):  
Endothelial Cells ◽  
In Vitro Model ◽  
Divalent Cations ◽  
Aortic Endothelial Cells ◽  
Vitro Model ◽  
Wall Interaction ◽  
Von Willebrand ◽  
Porcine Aortic Endothelial Cells ◽  
Aortic Endothelial

Normal and von Willebrand(vWd) porcine aortic endothelial cells(EC) have been maintained and subcultured for10-12 months(14-18 passages) without any apparent change in characteristic growth morphology or ultrastructure. Immunofluorescence staining ofthese EC for ristocetin-Willebrand factor(RWF), using monospecific rabbit antiporcine RWF(aRWF), showed differences in the extent and nature of intercellular staining and the apparent absence of extracellular EC associated RWF-containing material(filaments)in vWd cells. Platelet-endothelial(damaged) interaction was decreased in normal EC cultures by pretreatment of the cultures with aRWF, no platelet interaction was seen with untreated vWd EC. These cultures were used as an in vitro model system(optimal pH, divalent cations, protein, exposure time and rotation speed)for studying the nature, extent and differencesin the platelet-microfi1ament interaction in normal and vWd EC. Preliminary data on the microfilament site of attachment of washed platelets or antibody-coupled beads, the interaction of platelets with matrix-bound purified RWF and the presence of immunologically identifiable RWF-containing filaments in normal and vWd EC suggest a possible role for endothelial-bound RWF in platelet-vessel wall interaction.

scholarly journals Membrane-bound Progesterone Receptor Expression in Human Aortic Endothelial Cells

2003 ◽  
Vol 51 (8) ◽  
pp. 1049-1055 ◽  
Author(s):  
Brenda H. Welter ◽  
Elizabeth L. Hansen ◽  
Karla J. Saner ◽  
Yangzhan Wei ◽  
Thomas M. Price
Keyword(s):  
Cell Cycle ◽  
Endothelial Cells ◽  
Plasma Membrane ◽  
Progesterone Receptor ◽  
Progesterone Receptors ◽  
Vascular Endothelial ◽  
Aortic Endothelial Cells ◽  
Membrane Bound ◽  
Human Aortic Endothelial Cells ◽  
Aortic Endothelial

Observational studies demonstrate that estradiol and progesterone affect vasoreactivity. In animal studies, progesterone treatment causes immediate relaxation of precontracted arteries with inhibition of calcium influx in vascular endothelial and smooth muscle cells, suggesting a non-genomic mechanism of action. In this study we investigated the presence of novel membrane-bound progesterone receptors in human aortic endothelial cells and correlated the expression with cell-cycle stage. Western blotting analysis with an antibody directed to the hormone-binding domain of the classic progesterone receptors shows predominant bands at 100 and 60 kD, whereas analysis with an antibody to the DNA-binding region shows only the 100-kD band. In contrast, classic nuclear progesterone receptors B and A are identified at 116 and 94 kD in similarly processed T47D cells. Both novel bands localize to the membrane fraction after differential centrifugation. Plasma membrane-bound progesterone receptor was further shown with immunofluorescent antibody and ligand-binding studies in a small percentage of human aortic endothelial cells. Fluorescent activated cell sorting demonstrated that approximately 8% of the human aortic endothelial cells expressed a plasma membrane progesterone receptor and that a greater percentage of the expressing cells were in the G2/M-phase of the cell cycle. Treatment with progesterone conjugated to BSA did not show any significant cell-cycle changes. Plasma membrane-bound progesterone receptor in vascular endothelial cells may regulate the non-genomic actions of progesterone, and expression of the receptor appears to vary with cell cycle stage.

scholarly journals DISTRIBUTION OF ESTERASES IN THE MYONEURAL JUNCTION OF THE STRIATED MUSCLE OF THE RAT

1967 ◽  
Vol 15 (7) ◽  
pp. 399-403 ◽  
Author(s):  
O. ERÄNKÖ ◽  
H. TERÄVÄINEN
Keyword(s):  
Esterase Activity ◽  
Striated Muscle ◽  
Acetylcholinesterase Activity ◽  
Nonspecific Esterase ◽  
Selective Inhibitors ◽  
Myoneural Junction ◽  
Terminal Axon ◽  
Naphthyl Acetate ◽  
Nonspecific Esterase Activity

Distribution of esterases in the myoneural junction of the striated muscle of the rat was studied using acetylthiocholine, butyrylthiochobine and α-naphthyl acetate as substrates, together with selective inhibitors. Acetylcholinesterase activity was observed in the peripheral complex of synaptic folds. Nonspecific cholinesterase was detected in the peripheral complex of synaptic folds and the teloglia with approximately equal activities. Nonspecific esterase activity, present in tissues incubated with eserine, was marked in the terminal axon and was also present in the teloglia and synaptic folds.

scholarly journals Ultrastructural cytochemical and autoradiographic demonstration of nonspecific esterase(s) in guinea pig basophils.

1987 ◽  
Vol 35 (3) ◽  
pp. 351-360 ◽  
Author(s):  
A M Dvorak ◽  
R A Monahan-Earley ◽  
H F Dvorak ◽  
S J Galli
Keyword(s):  
Cell Surface ◽  
Guinea Pig ◽  
Esterase Activity ◽  
Plasma Membranes ◽  
Nonspecific Esterase ◽  
Lipid Bodies ◽  
Cytoplasmic Granules ◽  
Acetate Esterase ◽  
Alpha Naphthyl Acetate Esterase ◽  
Naphthyl Acetate

We used ultrastructural autoradiographic and cytochemical methods to localize esterase activities in unstimulated guinea pig basophils and in basophils undergoing degranulation or recovery from degranulation. We used tritium-labeled diisopropylfluorophosphate (DFP) as a probe for serine enzymes and localized this probe by ultrastructural autoradiography to cytoplasmic granules of immature or mature unstimulated basophils, as well as to granules released by degranulating basophils. Ultrastructural cytochemistry using alpha naphthyl acetate (ANA) as substrate localized nonspecific esterase activity to extruded granules, either within the interiors of degranulation sacs or within granules completely separated from degranulating basophils. Extruded granules retained their esterase activity for as long as 24 hr after antigen-induced degranulation. The plasma membranes of unstimulated or degranulating basophils, as well as of basophils recovering from degranulation, displayed prominent cell surface ANA esterase ectoenzyme activity. Lipid bodies, organelles present in the cytoplasm of both control and recovering basophils, were also alpha naphthyl acetate esterase (ANAE)-positive. Thus, cytochemical and autoradiographic techniques localized esterase and/or [3H]-DFP-binding activities to cytoplasmic granules, lipid bodies, and cell surface of basophils, and these enzyme activities persisted during both degranulation and recovery from degranulation.

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