Enzyme-cytochemistry of human chorion laeve at term: enzyme localization on the chorionic trophoblast.
Is the chorion laeve merely a remnant of the chorion frondosum in placental development? Or is it metabolically active, having something to do with maternofetal interactions? In order to answer these questions at least in part, we determined the ultracytochemical localizations of some important enzymes such as nonspecific phosphatase (alkaline phosphatase), specific phosphatase (Ca(++)-ATPase and 5'-nucleotidase) and adenylate cyclase in the human chorion laeve at term. Strong activities of these enzymes were localized by ultracytochemistry on the plasma membrane of the trophoblast in the chorion laeve. These enzyme activities were confirmed by a series of cytochemical-control experiments, i.e., substrate-free control, heat-stability control, and inhibition control by inhibitors of alkaline phosphatase. These observations indicate that the chorionic trophoblast is probably metabolically active and that it might play an important role in the physiology of the fetal membrane.
Matsubara
S
S
Department of Obstetrics and Gynecology, Jichi Medical School, Tochigi, Japan.
Sayama
M
M
Sato
I
I
Tamada
T
T
D015720:5'-Nucleotidase / Q000378:metabolism; D000262:Adenylyl Cyclases / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D002823:Chorion / Q000201:enzymology*; D005260:Female; D006651:Histocytochemistry; D006801:Humans; D014327:Trophoblasts / Q000201:enzymology*
D000469:Alkaline Phosphatase; D015720:5'-Nucleotidase; D000262:Adenylyl Cyclases; D000252:Calcium-Transporting ATPases