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Nonspecific esterase activity expressed in Weibel-Palade bodies of cloned guinea pig aortic endothelial cells [published erratum appears in J Histochem Cytochem 1987 Oct;35(10):1171]

RA Monahan-Earley, T Isomura, RI Garcia, SJ Galli, HF Dvorak and AM Dvorak

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.

Volume 35, Issue 5, pp. 531-539, 05/01/1987
Copyright © 1987 by The Histochemical Society


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