Enzyme-cytochemically detectable NADPH-diaphorase activity is present in the endoplasmic reticulum and nuclear envelope of the syncytiotrophoblast of the human placenta.

S Matsubara, T Takizawa, T Takayama, H Minakami, I Sato

Index: Eur. J. Histochem. 43(3) , 247-51, (1999)

Full Text: HTML

Abstract

We investigated the subcellular localization of nicotinamide adenine dinucleotide phosphate diaphorase (NADPH-d) activity, a histo- and cyto-chemical marker of nitric oxide synthase, in human placental trophoblast obtained from women with normal term pregnancies. Tetrazolium salt BSPT was used as the capturing agent. Precipitates of BSPT-formazan indicative of NADPH-d reaction were observed on the membranes of endoplasmic reticulum and nuclear envelope of syncytiotrophoblasts. Our results indicate these two intracytoplasmic organellae are the sites of nitric oxide generation in the syncytiotrophoblasts of normal term human placenta.