Lactase-phlorizin hydrolase (LPH) is expressed on the intestinal brush
border and is responsible for the hydrolysis of lactose, the chief su
gar in mammalian milk. The enzymic activity of LPH peaks soon after bi
rth in most mammals and declines to much lower levels before adolescen
ce. The molecular basis of this pattern of expression has not been cle
arly established. We have measured relative amounts of LPH mRNA in int
estine from sheep with ages across a developmental spectrum, including
third trimester fetal lambs, newborn lambs and adult sheep. LPH mRNA
levels in the jejunum decline similar to 50-fold between infancy and a
dulthood, in parallel with the reduction in both lactase specific acti
vity and immunologically reactive lactase protein expression in sheep
jejunum. LPH mRNA is present in high concentration in the duodenum of
newborn lambs, but steadily declines by day 34 and is dramatically red
uced in adults. Because the changes in LPH mRNA: protein, and enzymic
activity are generally parallel, we conclude that the developmental re
gulation of LPH in sheep is probably mediated primarily at the mRNA le
vel.