TY - JOUR
T1 - Development of the adrenergic phenotype
T2 - increase in adrenal messenger RNA coding for phenylethanolamine-N-methyltransferase.
AU - Sabban, E.
AU - Goldstein, M.
AU - Bohn, M. C.
AU - Black, I. B.
PY - 1982/1/1
Y1 - 1982/1/1
N2 - Mechanisms regulating the developmental increase in the activity of adrenal phenylethanolamine-N-methyltransferase (PNMTase), an index of the adrenergic phenotype, were examined. Immunotitration indicated that the increase in catalytic activity in rat adrenal from birth to adulthood was attributable to increased numbers of PNMTase molecules, not enzyme activation. To determine whether the ontogenetic increase in PNMTase protein was associated with elevation of mRNA coding for PNMTase, cell-free translation was performed on total cellular mRNA obtained from adrenals at different ages. Translation in wheat-germ and reticulocyte lysate systems, followed by immunoprecipitation of the PNMTase product, NaDodSO4 gel electrophoresis, and fluorography, showed an 8-fold increase in the proportion of specific PNMTase mRNA relative to total mRNA in rat adrenals from birth to adulthood. Moreover, bovine adrenal medullae exhibited a 100-fold increase in PNMTase mRNA levels between embryonic life and adulthood. Consequently, the ontogenetic increase in adrenal PNMTase appears to be due to a developmental rise in specific mRNA coding for the protein.
AB - Mechanisms regulating the developmental increase in the activity of adrenal phenylethanolamine-N-methyltransferase (PNMTase), an index of the adrenergic phenotype, were examined. Immunotitration indicated that the increase in catalytic activity in rat adrenal from birth to adulthood was attributable to increased numbers of PNMTase molecules, not enzyme activation. To determine whether the ontogenetic increase in PNMTase protein was associated with elevation of mRNA coding for PNMTase, cell-free translation was performed on total cellular mRNA obtained from adrenals at different ages. Translation in wheat-germ and reticulocyte lysate systems, followed by immunoprecipitation of the PNMTase product, NaDodSO4 gel electrophoresis, and fluorography, showed an 8-fold increase in the proportion of specific PNMTase mRNA relative to total mRNA in rat adrenals from birth to adulthood. Moreover, bovine adrenal medullae exhibited a 100-fold increase in PNMTase mRNA levels between embryonic life and adulthood. Consequently, the ontogenetic increase in adrenal PNMTase appears to be due to a developmental rise in specific mRNA coding for the protein.
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U2 - 10.1073/pnas.79.15.4823
DO - 10.1073/pnas.79.15.4823
M3 - Article
C2 - 6956894
AN - SCOPUS:0020172360
SN - 0027-8424
VL - 79
SP - 4823
EP - 4827
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 15
ER -