Parathyroid hormone alters collagen synthesis and procollagen mRNA levels in fetal rat calvaria.
AUTOR(ES)
Kream, B E
RESUMO
Parathyroid hormone decreased the incorporation of [3H]proline into collagenase-digestible protein in cultured 21-day fetal rat calvaria but had little effect on the labeling of noncollagen protein. After 24 hr of culture, there was a 50% reduction in collaghen synthesis and a 40% decrease in the level of functional procollagen mRNA as measured in a reticulocyte lystate translation assay. The effect of parathyroid hormone on both parameters was detectable after 6 hr of treatment. In these cultures, there was also a substantial degradation or release of newly synthesized collagen from the calvaria, but parathyroid hormone had little effect on the release of collagen into the medium. These results suggest that parathyroid hormone inhibits collagen synthesis primarily by decreasing the steady-state level of procollagen mRNA.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=350127Documentos Relacionados
- Role of procollagen mRNA levels in controlling the rate of procollagen synthesis.
- Retinoic acid suppresses parathyroid hormone (PTH) secretion and PreproPTH mRNA levels in bovine parathyroid cell culture.
- Endotoxin increases parathyroid hormone-related protein mRNA levels in mouse spleen. Mediation by tumor necrosis factor.
- Effect of insulinlike growth factor I on DNA and protein synthesis in cultured rat calvaria.
- Hormone-induced increase in levels of functional mRNA and α-amylase mRNA in barley aleurones
