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Species differences in the localization of cGMP‐producing and NO‐responsive elements in the mouse and rat hippocampus using cGMP immunocytochemistry
Author(s) -
Van Staveren Wilma C. G.,
Steinbusch Harry W. M.,
Markerinkvan Ittersum Marjanne,
Behrends Sönke,
De Vente Jan
Publication year - 2004
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1111/j.0953-816x.2004.03327.x
Subject(s) - phosphodiesterase , soluble guanylyl cyclase , immunocytochemistry , sodium nitroprusside , nitric oxide synthase , phosphodiesterase 3 , nitric oxide , phosphodiesterase inhibitor , hippocampus , biology , pde10a , cyclic guanosine monophosphate , protein subunit , microbiology and biotechnology , chemistry , biochemistry , medicine , endocrinology , enzyme , guanylate cyclase , gene
The aim of the study was to compare the localization of the nitric oxide (NO)–cGMP pathway in hippocampus of mice and rats using cGMP‐ and soluble guanylyl cyclase (GC) immunocytochemistry and in situ hybridization of the cGMP‐hydrolysing phosphodiesterase types 2, 5 and 9. In vitro incubation of hippocampus slices in the absence of a guanylyl cyclase stimulator or a phosphodiesterase inhibitor resulted in cGMP‐positive astrocytes mainly in the CA1 area in mouse slices. In contrast, no cGMP immunoreactivity was observed under these conditions in the rat hippocampus. Treatment with an NO synthase inhibitor or inhibitors of soluble or particulate GC did not abolish cGMP immunoreactivity in astrocytes. Incubation with the NO donors sodium nitroprusside or diethylamino NONOate, or with the NO‐independent activators of soluble GC, YC‐1 and BAY 41‐2272, in combination with phosphodiesterase inhibitors, resulted in an increase in cGMP immunoreactivity in numerous astrocytes throughout the mouse hippocampus. In contrast, under these conditions cGMP immunoreactivity was primarily observed in varicose fibers in rat hippocampus. Comparison of the cellular localization of the β1 subunit of soluble GC and the mRNAs of PDE2, PDE5 and PDE9 revealed that in both species the β1 subunit was observed in pyramidal and granule cells, which also expressed the mRNAs of the three phosphodiesterase families. Although the β1 subunit was observed in astrocytes, none of the phosphodiesterases were detected in these cells. We conclude that, although the expression profiles of the soluble GC β1 subunit and cGMP‐hydrolysing phosphodiesterase mRNAs were identical, the cellular patterns of cGMP immunoreactivity differ between rat and mouse hippocampus.