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NONSPECIFIC ESTERASE-ACTIVITY EXPRESSED IN WEIBEL-PALADE BODIES OF CLONED GUINEA-PIG AORTIC ENDOTHELIAL-CELLS JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY MONAHANEARLEY, R. A., Isomura, T., Garcia, R. I., GALLI, S. J., Dvorak, H. F., Dvorak, A. M. 1987; 35 (5): 531-539

Abstract

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.

View details for Web of Science ID A1987G874400002

View details for PubMedID 3559181