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Molecular Pharmacology

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Research ArticleArticle

Analysis of the Pharmacological and Molecular Heterogeneity of I2-Imidazoline-Binding Proteins using Monoamine Oxidase-Deficient Mouse Models

Anne Remaury, Rita Raddatz, Catherine Ordener, Sandra Savic, Jean C. Shih, Kevin Chen, Isabelle Seif, Edward De Maeyer, Stephen M. Lanier and Angelo Parini
Molecular Pharmacology November 2000, 58 (5) 1085-1090; DOI: https://doi.org/10.1124/mol.58.5.1085
Anne Remaury
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Rita Raddatz
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Catherine Ordener
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Sandra Savic
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Jean C. Shih
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Kevin Chen
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Isabelle Seif
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Edward De Maeyer
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Stephen M. Lanier
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Angelo Parini
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Abstract

The I2 subgroup of imidazoline-binding sites was identified as monoamine oxidases (MAOs), but it is unclear whether there are I2-binding sites located on proteins distinct from MAOs. To address this issue, we characterized I2-binding proteins in liver and brain of wild-type and MAO A- and MAO B-deficient mice. I2-binding sites were identified using [3H]idazoxan and the photoaffinity adduct 2-[3-azido-4-[125I]iodophenoxyl]methylimidazoline ([125I]AZIPI). [3H]Idazoxan labeled binding sites with ligand recognition properties typical of I2sites in both brain and liver of wild-type mice. High-affinity, specific [3H]idazoxan binding were not altered in MAO A knockout (KO) mice. In contrast, [3H]idazoxan binding was completely abolished in both liver and brain of MAO B KO mice. In wild-type mice, [125I]AZIPI photolabeled three proteins with apparent molecular masses of ∼28 (liver), ∼61 (brain), and ∼55 kDa (liver and brain). The photolabeling of each protein was blocked by the imidazoline cirazoline (10 μM). Photolabeling of the ∼61- and ∼55-kDa proteins was not observed in MAO A and B KO mice, respectively. In contrast, photolabeling of the liver ∼28-kDa protein was still observed in MAO-deficient mice, indicating that this protein is unrelated to MAOs. These data indicate that I2 imidazoline-binding sites identified by [3H]idazoxan reside solely on MAO B. The binding sites on MAO A and the liver ∼28-kDa protein may represent additional subtypes of the family of the imidazoline-binding sites.

Footnotes

    • Received December 29, 1999.
    • Accepted August 2, 2000.
  • Send reprint requests to: Angelo Parini, M.D., Ph.D., INSERM U388, Institut Louis Bugnard, CHU Rangueil, 31403 Toulouse Cedex 4, France. E-mail: Parini{at}inserm.rangueil.fr

  • This work was supported by Institut National de la Santéet de la Recherche Médicale, the Région Midi-Pyrénées, the Center National de la Recherche Scientifique, the Curie Institute, the National Institute of Mental Health Grant R37 MH39085 (MERIT Award) and NS35875 (S.M.L.), KO5 MH00796 (Research Scientist Award), RO1 MH37020, and the Welin Professorship, T32-HL-7260 (R.R., S.M.L.) and F32 NS10332 (R.R.). A.R. is the recipient of a grant from I.R.I. Servier (France).

  • The American Society for Pharmacology and Experimental Therapeutics
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Molecular Pharmacology: 58 (5)
Molecular Pharmacology
Vol. 58, Issue 5
1 Nov 2000
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Research ArticleArticle

Analysis of the Pharmacological and Molecular Heterogeneity of I2-Imidazoline-Binding Proteins using Monoamine Oxidase-Deficient Mouse Models

Anne Remaury, Rita Raddatz, Catherine Ordener, Sandra Savic, Jean C. Shih, Kevin Chen, Isabelle Seif, Edward De Maeyer, Stephen M. Lanier and Angelo Parini
Molecular Pharmacology November 1, 2000, 58 (5) 1085-1090; DOI: https://doi.org/10.1124/mol.58.5.1085

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Research ArticleArticle

Analysis of the Pharmacological and Molecular Heterogeneity of I2-Imidazoline-Binding Proteins using Monoamine Oxidase-Deficient Mouse Models

Anne Remaury, Rita Raddatz, Catherine Ordener, Sandra Savic, Jean C. Shih, Kevin Chen, Isabelle Seif, Edward De Maeyer, Stephen M. Lanier and Angelo Parini
Molecular Pharmacology November 1, 2000, 58 (5) 1085-1090; DOI: https://doi.org/10.1124/mol.58.5.1085
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