title: Endopeptidase-24.11 is striosomally ordered in pig brain and, in contrast to aminopeptidase N and peptidyl dipeptidase A ('angiotensin converting enzyme'), is a marker for a set of striatal efferent fibres.
abstract: Endopeptidase-24.11 (sometimes referred to as 'enkephalinase') is a key cell-surface enzyme in the metabolism of neuropeptides. A previous immunohistochemical study mapped the enzyme in pig brain and indicated a striosomal ordering of the enzyme within the striatum. This point has now been confirmed by staining adjacent sections for acetylcholinesterase (by histochemistry) and endopeptidase-24.11 (by an immunoperoxidase method). While there were some general similarities in the mapping of these two hydrolases, e.g. in the caudate-putamen, globus pallidus, olfactory tubercle, substantia nigra and striatonigral tract, there were differences in intensity and in the microscopic distribution, e.g. as in striosomes for which acetylcholinesterase was diminished. Two other membrane peptidases, peptidyl dipeptidase A ('angiotensin converting enzyme') and aminopeptidase N, were also mapped by the same immunohistochemical method. Peptidyl dipeptidase A had some similarities with endopeptidase-24.11, e.g. in its concentration within the striatal nuclei, but clear differences were also apparent, in particular the absence of staining of the former in the globus pallidus and olfactory tubercle. Immunostaining for aminopeptidase N, in contrast to the other peptidases, was observed as a diffuse staining throughout the gray matter. At the microscopic level, two important differences were that staining for aminopeptidase N and peptidyl dipeptidase A was very intense throughout the vasculature of the brain and that striatal efferent bundles of unmyelinated fibres staining positively for endopeptidase-24.11 were depleted of the other two peptidases. All three peptidases were identified in the pia mater. Thus, endopeptidase-24.11, unlike peptidyl dipeptidase A and aminopeptidase N, is a marker for a set of striatal efferent fibres in pig brain.
authors.affiliation: MRC Membrane Peptidase Research Group, Department of Biochemistry, University of Leeds, U.K.
authors.forename: K
authors.initials: K
authors.lastname: Barnes
authors.forename: R
authors.initials: R
authors.lastname: Matsas
authors.forename: N M
authors.initials: NM
authors.lastname: Hooper
authors.forename: A J
authors.initials: AJ
authors.lastname: Turner
authors.forename: A J
authors.initials: AJ
authors.lastname: Kenny
mesh_terms: D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D018826:CD13 Antigens; D003342:Corpus Striatum / Q000201:enzymology*; D006651:Histocytochemistry; D007150:Immunohistochemistry; D015260:Neprilysin / Q000378:metabolism*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D013552:Swine
chemical_list: D000626:Aminopeptidases; D018826:CD13 Antigens; D007703:Peptidyl-Dipeptidase A; D015260:Neprilysin