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Endopeptidase-24.11 (neutral endopeptidase, neprilysin, 'enkephalinase', EC 3.4.24.11) and endopeptidase-24.18 (endopeptidase-2, meprin, EC 3.4.24.18) are cell-surface zinc-dependent metallo-endopeptidases able to cleave a variety of bioactive peptides including growth factors. We report the first study of the cellular and tissue distribution of both(More)
Endopeptidase-24.11, a plasma membrane ectoenzyme with the ability to hydrolyse a variety of neuropeptides, has been localized in the pig nervous system by an immunoperoxidase technique. The endopeptidase was mapped in cryostat sections of the fore and mid-brain to the following structures: caudate-putamen, globus pallidus, olfactory tubercle, nucleus(More)
Immunohistochemical techniques have been used to study a group of membrane peptidases in the distal segment of the ulnar nerve of piglets 7 and 14 days after surgical section. Five peptidases were studied, all of which have a wide distribution on the surfaces of many cell types and have roles in metabolising neuropeptides. In normal pig nerves,(More)
The hydrolysis of [Leu]enkephalin and substance P by purified pig kidney endopeptidase (EC 3.4.24.11) and synaptic membranes prepared from pig caudate nuclei has been compared. The hydrolysis of an enkephalin analogue (Tyr-D-Ala-Gly-Phe-Leu) at the Gly-Phe bond was completely inhibited by phosphoramidon. The IC50 concentration (8 nM) was similar to that(More)
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(More)
Brains from piglets were dissected and a block of tissue including the substantia nigra, globus pallidus, and entopeduncular nucleus was homogenized and then fractionated on discontinuous Percoll gradients. Ligand-binding assays using (-)-[3H]nicotine and [3H]quinuclidinyl benzilate served to delineate fractions containing nicotinic and muscarinic(More)
Some of the many cell-surface antigens defined by the CD (cluster differentiation) nomenclature have lately emerged as proteins with well-characterised enzymic activities. One important example is CD10 or CALLA (common acute lymphoblastic leukaemia antigen), which is identical to endopeptidase-24.11, an enzyme with an important role in the hydrolysis of(More)
Endopeptidase-24.11 is a widely distributed cell surface enzyme with a role in inactivating some neuropeptides and peptide hormones. In the central nervous system it has been implicated in the metabolism of enkephalins and tachykinins, neuropeptides which are expressed by neurons projecting to the substantia nigra. Two immunochemical methods have been used(More)
Synaptic membrane preparations from human striatum and human diencephalon were shown to contain a phosphoramidon-sensitive metalloendopeptidase that appeared identical with endopeptidase-24.11. The activity of endopeptidase-24.11 was determined with an enzymic assay employing [D-Ala2,Leu5]enkephalin as substrate, and its distribution in human brain was(More)
An ultrastructural study of endopeptidase-24.11 in the globus pallidus from the brain of a newborn pig is reported. The antigen was localized by an immunoperoxidase method using an affinity-purified polyclonal antibody in which staining was performed on thick vibratome sections prior to osmication and flat embedding. When areas selected by light microscopy(More)