Gene expression of prohormone and proprotein convertases in the rat CNS: a comparative in situ hybridization analysis

摘要: Posttranslational processing of proproteins and prohormones is an essential step in the formation bioactive peptides, which particular importance nervous system. Following a long search for enzymes responsible protein precursor cleavage, family Kexin/subtilisin-like convertases known as PC1, PC2, furin have recently been characterized mammalian species. Their presence endocrine neuroendocrine tissues has demonstrated. This study examines mRNA distribution these rat CNS compares their expression with previously carboxypeptidase E (CPE) peptidylglycine alpha-amidating monooxygenase (PAM) using situ hybridization histochemistry. Furin was ubiquitously distributed detected both neurons non- neuronal tissue throughout brain higher abundance ependyma, circumventricular organs, islands Calleja, hippocampus, allocortex. The cellular localization PC1 PC2 exclusively highest concentrations neuropeptide-rich regions. In general, more widely expressed than CNS, although many regional variations were detected. identification specific combinations convertase together CPE PAM regions suggests that enzymatic pathways are involved neuropeptide processing, region-specific differences posttranslational processing.