Abstract
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 |
|---|---|
| Journal | American Journal of Physiology - Cell Physiology |
| Volume | 256 |
| Issue number | 3 |
| State | Published - Jan 1 1989 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Cell Biology
- Clinical Biochemistry
- Physiology
Cite this
Rat lung lectin gene expression is regulated developmentally and by dexamethasone. / Clerch, L. B.; Whitney, P.; Massaro, D.
In: American Journal of Physiology - Cell Physiology, Vol. 256, No. 3, 01.01.1989.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Rat lung lectin gene expression is regulated developmentally and by dexamethasone
AU - Clerch, L. B.
AU - Whitney, P.
AU - Massaro, D.
PY - 1989/1/1
Y1 - 1989/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0024557348&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024557348&partnerID=8YFLogxK
M3 - Article
C2 - 2923190
AN - SCOPUS:0024557348
VL - 256
JO - American Journal of Physiology - Cell Physiology
JF - American Journal of Physiology - Cell Physiology
SN - 0363-6143
IS - 3
ER -