Identification of protein phosphatase 2A as the major tyrosine hydroxylase phosphatase in adrenal medulla and corpus striatum: evidence from the effects of okadaic acid

Jan Haavik, Donald L. Schelling, David G. Campbell, Kristoffer K. Andersson, Torgeir Flatmark, Philip Cohen

Research output: Contribution to journalArticle

86 Citations (Scopus)

Abstract

(i) The major sites on bovine adrenal tyrosine hydroxylase (TH) phosphorylated by calmodulin-dependent multiprotein kinase (CaM-MPK) and cyclic AMP-dependent protein kinase were shown to be Ser-19 and Ser-40, respectively, while Ser-40 was also phosphorylated slowly by CAM-MPK. (ii) Type 2A and type 2C phosphatases accounted for ≈90% and ≈ 10% of TH phosphatase activity, respectively, in extracts of adrenal medulla and corpus striatum assayed at near physiological free Mg2+(1 mM), while type 1 and type 2B phosphatases had negligible activity towards TH. (iii) Incubation of adrenal chromaffin cells with okadaic acid increased TH phosphorylation by 206% and activity by 77%, establishing that type 2A phosphatases play a major role in regulating TH in vivo.

Original languageEnglish
Pages (from-to)36-42
Number of pages7
JournalFEBS Letters
Volume251
Issue number1-2
DOIs
Publication statusPublished - 17 Jul 1989

Fingerprint

Corpus Striatum
Protein Phosphatase 2
Okadaic Acid
Adrenal Medulla
Tyrosine 3-Monooxygenase
Phosphoric Monoester Hydrolases
Chromaffin Cells
Calcium-Calmodulin-Dependent Protein Kinases
Phosphorylation
Computer aided manufacturing
Cyclic AMP-Dependent Protein Kinases

Keywords

  • Calmodulin
  • cyclic AMP
  • Okadaic acid
  • Protein kinase
  • Protein phosphatase
  • Protein sequencing
  • Tyrosine hydroxylase

Cite this

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title = "Identification of protein phosphatase 2A as the major tyrosine hydroxylase phosphatase in adrenal medulla and corpus striatum: evidence from the effects of okadaic acid",
abstract = "(i) The major sites on bovine adrenal tyrosine hydroxylase (TH) phosphorylated by calmodulin-dependent multiprotein kinase (CaM-MPK) and cyclic AMP-dependent protein kinase were shown to be Ser-19 and Ser-40, respectively, while Ser-40 was also phosphorylated slowly by CAM-MPK. (ii) Type 2A and type 2C phosphatases accounted for ≈90{\%} and ≈ 10{\%} of TH phosphatase activity, respectively, in extracts of adrenal medulla and corpus striatum assayed at near physiological free Mg2+(1 mM), while type 1 and type 2B phosphatases had negligible activity towards TH. (iii) Incubation of adrenal chromaffin cells with okadaic acid increased TH phosphorylation by 206{\%} and activity by 77{\%}, establishing that type 2A phosphatases play a major role in regulating TH in vivo.",
keywords = "Calmodulin, cyclic AMP, Okadaic acid, Protein kinase, Protein phosphatase, Protein sequencing, Tyrosine hydroxylase",
author = "Jan Haavik and Schelling, {Donald L.} and Campbell, {David G.} and Andersson, {Kristoffer K.} and Torgeir Flatmark and Philip Cohen",
year = "1989",
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Identification of protein phosphatase 2A as the major tyrosine hydroxylase phosphatase in adrenal medulla and corpus striatum : evidence from the effects of okadaic acid. / Haavik, Jan; Schelling, Donald L.; Campbell, David G.; Andersson, Kristoffer K.; Flatmark, Torgeir; Cohen, Philip.

In: FEBS Letters, Vol. 251, No. 1-2, 17.07.1989, p. 36-42.

Research output: Contribution to journalArticle

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