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AMP deaminase in rat brain: Localization in neurons and ependymal cells
Author(s) -
Knecht Kerstin,
Wiesmüller KarlHeinz,
Gnau Volker,
Jung Günther,
Meyermann Richard,
Todd Kathryn G.,
Hamprecht Bernd
Publication year - 2001
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.10059
Subject(s) - choroid plexus , ependymal cell , biology , immunocytochemistry , immunostaining , microbiology and biotechnology , in situ hybridization , amp deaminase , biochemistry , enzyme , messenger rna , central nervous system , immunohistochemistry , adenosine deaminase , endocrinology , immunology , gene
The purine nucleotide cycle enzyme AMP deaminase (AMPD) catalyzes the irreversible hydrolytic deamination of AMP. The physiological function of the purine nucleotide cycle in the brain is unknown. In situ hybridization and immunocytochemical studies were performed to identify the regional and cellular expression of AMPD in rat brain with the goal of elucidating the neural function of the purine nucleotide cycle. AMPD messenger RNA was detected in ventricular ependymal cells and cells of the choroid plexus and in neurons of distinct brain areas. Although only low antibody titers were obtained by immunization with the purified sheep brain AMPD, immunization of mice with synthetic lipopeptide vaccines containing oligopeptides derived from a known partial complementary DNA sequence of the enzyme yielded an antiserum suitable for immunocytochemistry. Immunostaining of cells in culture showed that neurons but not astroglial cells express appreciable amounts of the enzyme. Results of immunocytochemical staining performed on rat brain slices were in accord with the localization of AMPD messenger RNA, thus confirming the expression of AMPD in neurons of the brain stem, hippocampus, cerebellar nuclei and mesencephalic nuclei, as well as in ventricular ependymal cells and their cilia. © 2001 Wiley‐Liss, Inc.