Carboxypeptidase D is a potential candidate to carry out redundant processing functions of carboxypeptidase E based on comparative distribution studies in the rat central nervous system.

摘要: Abstract Post-translational processing is essential for the biological activation of many proteins and peptides. After precursor cleavage at specific single residues or pairs basic by proprotein convertases, C-terminal are removed. Carboxypeptidase E was thought to be only enzyme responsible. Recent studies with carboxypeptidase E-deficient mice, Cpe fat / , indicated existence E-like carboxypeptidases, such as D. In order define potential redundant functions in vivo we compared distributions both carboxypeptidases rat central nervous system selected endocrine tissues. D messenger RNA abundantly expressed glial cells gray white matter, while neurons several brain regions, piriform cortex, basolateral amygdala hippocampus, also high levels RNA. Co-localization RNAs observed spinal cord Immunohistochemistry showed intracellular distribution a perinuclear pattern. The extensive neuronal indicates important role peptide processing, possibly working together furin, ubiquitously convertase. co-localization suggests that may, least partially, compensate mice.