The cell-agglutinating activity of soluble β-galactoside-binding proteins (lectins) is developmentally regulated in several mammalian organs. Little is known of the alterations in gene expression that underlie this developmental regulation. Rat lung contains a dimeric β-galactoside-binding protein that exhibits a postnatal peak of hemagglutination activity caused in part by an increased rate of lectin synthesis. We now report rat lung lectin mRNA concentration increased to a peak at age 6 days; dexamethasone treatment aborted this increase. Southern blot analysis is compatible with the presence of more than one lectin gene. However, two lines of evidence indicate that we measured a single gene product: 1) only one lectin of subunit M(r) 14,000 is present in rat lung (Biochemistry 27: 692-699, 1988), and 2) in Northern blot analysis of RNA, the lectin cDNA hybridized with only one mRNA species. Our present findings, taken with prior studies of lectin synthesis, indicate that the postnatal increase in lectin synthesis is mediated pretranslationally and by an increased efficiency of translation. Dexamethasone treatment impairs the increase of lectin mRNA concentration but increases translational efficiency.
|Original language||English (US)|
|Journal||American Journal of Physiology - Cell Physiology|
|State||Published - Jan 1 1989|
ASJC Scopus subject areas
- Cell Biology