The cross-linking of the connective tissues in the fetal membranes and plac
enta is important for their tensile strength and elasticity. We have studie
d the expression of lysyl oxidase (LOX) because it is the classical enzyme
responsible for the cross-linking of collagen and elastin. We have also stu
died the two recently described, genetically distinct lysyl oxidase-like ge
nes and proteins, lysyl oxidase-like (LOSL) and lysyl oxidase-like 2 (LOXL2
), of unknown functions. Specific antisera have been used for immunolocaliz
ation in fetal membranes and placentae from early pregnancy terminations an
d after caesarean section at both preterm and term, prior to labour. In add
ition, the steady state mRNA levels of the three genes has been quantitated
in separated amnion, chorion, decidua and placentae collected at term befo
re labour. The immunocytochemistry shows that the spatial expression of the
three lysyl oxidases is similar in early pregnancy in both the fetal membr
anes and placentae. However, by preterm this pattern had diverged and becom
es greatest at term. The expression of the genes found at term was similar
to the results of protein expression obtained by immunocytochemistry, with
the exception of LOXL which had high placental gene expression, but low lev
els of immunolocalized protein. Thus by term, LOX was expressed predominant
ly in the amniotic epithelium, with little espression in the placenta, whil
e LOSL showed highest gene espression in the placenta and lowest expression
in the amnion. LOXL2 expression was again different and was expressed pred
ominantly in the chorionic cytotrophoblast of the membranes with low expres
sion in both the amnion and placentae. These results suggest that these thr
ee members of the lysyl oxidase family may hare similar roles in early preg
nancy during the development of the placenta and fetal membranes, but their
divergence as pregnancy advances to term, may reflect changes in substrate
specificity and connective tissue composition. (C) 2001 Harcourt Publisher
s Ltd.