Protease cytochemistry in the murine rodent, guinea-pig and marmoset placenta.
Plasma membrane and lysosomal proteases, gamma-glutamyl transferase and extracellular matrix proteases were investigated by qualitative cytochemical means in the mature placenta of mice, rats, guinea-pigs and marmosets. These studies revealed similarities, which concerned primarily the lysosomal proteases in different structures of the placenta and all proteases and gamma-glutamyl transferases in the zone of placental shedding. However, species differences predominated. They were observed especially for amino-peptidase A and M, dipeptidyl peptidase IV and gamma-glutamyl transferase in the plasma membranes and extracellular matrix of the placental barrier and decidual cells of all species and the cells of the basal zone in rats and mice. Plasma membrane and extracellular matrix proteases in other parts of the placenta, e.g. the placenta stem of guinea-pigs and basal plate, amniotic and chorionic plate of marmosets occurred only in these species. Elastase substrates hydrolysing endopeptidase I and kallikrein-, thrombin-, plasmin-, plasminogen- and cathepsin B substrates hydrolysing endopeptidase II were not observed in any of these species. A general comparison of the species revealed similarities for the mouse, rat and guinea-pig placental barrier, but not for that of marmosets. The proteases of this zone in the marmoset placenta are more similar to the human situation, but do not correspond to it completely.
Gossrau
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Graf
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D000818:Animals; D002143:Callitrichinae; D002462:Cell Membrane / Q000201:enzymology; D005109:Extracellular Matrix / Q000201:enzymology; D005260:Female; D006168:Guinea Pigs; D008247:Lysosomes / Q000201:enzymology; D051379:Mice; D010447:Peptide Hydrolases / Q000378:metabolism*; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D051381:Rats; D013045:Species Specificity; D005723:gamma-Glutamyltransferase / Q000378:metabolism*
D005723:gamma-Glutamyltransferase; D010447:Peptide Hydrolases