Development of the adrenergic phenotype: increase in adrenal messenger RNA coding for phenylethanolamine-N-methyltransferase.

E. Sabban*, M. Goldstein, M. C. Bohn, I. B. Black

*Corresponding author for this work

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21 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)4823-4827
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume79
Issue number15
DOIs
StatePublished - Jan 1 1982

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Phenylethanolamine N-Methyltransferase
Adrenergic Agents
Phenotype
Messenger RNA
Photofluorography
Parturition
Adrenal Medulla
Enzyme Activation
Reticulocytes
Immunoprecipitation
Triticum
Electrophoresis
Proteins
Gels

ASJC Scopus subject areas

  • General

Cite this

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title = "Development of the adrenergic phenotype: increase in adrenal messenger RNA coding for phenylethanolamine-N-methyltransferase.",
abstract = "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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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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