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However, other immunohistochemical studies using glutaraldehyde fixation and high-affinity monoclonal antibodies have revealed intense cGMP-immunoreactivity in Purkinje cells (Sakaue et al. 1988). A possible explanation for these results might be provided by the discovery that NO induces a large increase in extracellular cGMP, which is then cleared from the extracellular space by a probenecid-sensitive mechanism (Luo et al. 1994; Tjornhammer et al. 1986; Vallebuona & Raiteri 1993). Thus cGMP might be produced primarily in Purkinje cells but rapidly leaves these cells to be accumulated by the Bergmann glia.

S-nitrosylation of proteins may be of great importance in the neurotoxic actions of NO but is unlikely to be involved in the normal intercellular signaling by this molecule. Instead, NO appears to act by mediating agonist-induced increases in cGMP. Data consistent with a role for the NO-cGMP signal transduction system in the long-term depression (LTD) of AMPA responses in Purkinje cells have been obtained by various groups. Ito and Karachot (1990) demonstrated that the desensitization of Purkinje cell responses to AMPA in rat cerebellar slices was abolished by Ca 2 + chelators, hemoglobin, the nitric oxide synthase inhibitor N G nitroarginine, and an inhibitor of cGMP-dependent protein kinase.

In vitro studies using cerebellar slices or cultures, as well as in vivo studies, have demonstrated that NO formation and release occur in the cerebellar cortex in response to NMDA receptor activation. Using intracerebellar microdialysis in awake-behaving animals, we have found that this is associated with a large increase in extracellular cGMP levels in the cerebellar cortex. A similar increase in cGMP efflux is seen in response to activation of AMPA or metabotropic glutamate receptors, or to activation of the climbing fiber input.

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