Induction of spermidine/spermine N1-acetyltransferase by parathyroid hormone in rabbit costal chondrocytes in culture.
Parathyroid hormone (PTH) increased the activity of spermidine/spermine N1-acetyltransferase, a rate-limiting enzyme of polyamine biodegradation, in rabbit costal chondrocytes in culture. The enzyme activity increased in a dose-dependent manner after addition of PTH to the culture, reaching a maximum at 8 h. The increase in the enzyme activity was abolished by cycloheximide or actinomycin D. Dibutyryl cyclic AMP also induced the acetyltransferase to some extent. These results suggest that the induction of spermidine/spermine N1-acetyltransferase by PTH may play some significant role in the expression of the differentiated phenotype of chondrocytes.
Matsui-Yuasa
I
I
Otani
S
S
Morisawa
S
S
Takigawa
M
M
Enomoto
M
M
Suzuki
F
F
D000123:Acetyltransferases / Q000096:biosynthesis*; D000818:Animals; D003994:Bucladesine / Q000494:pharmacology; D002356:Cartilage / Q000201:enzymology*; D002478:Cells, Cultured; D003513:Cycloheximide / Q000494:pharmacology; D003609:Dactinomycin / Q000494:pharmacology; D004790:Enzyme Induction / Q000187:drug effects; D007700:Kinetics; D008297:Male; D010281:Parathyroid Hormone / Q000494:pharmacology*; D010446:Peptide Fragments / Q000494:pharmacology*; D011817:Rabbits; D000099228:Diamine N-Acetyltransferase
D000123:Acetyltransferases; D003994:Bucladesine; D003513:Cycloheximide; D003609:Dactinomycin; D010281:Parathyroid Hormone; D010446:Peptide Fragments; D000099228:Diamine N-Acetyltransferase; C025076:parathyroid hormone (1-34), bovine