Membrane peptidases in the pig choroid plexus and on other cell surfaces in contact with the cerebrospinal fluid
- 1 April 1989
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 259 (1) , 69-80
- https://doi.org/10.1042/bj2590069
Abstract
A comprehensive survey of 11 peptidases, all of which are markers for renal microvillar membranes, has been made in membrane fractions prepared from pig choroid plexus. Two fractionation schemes were explored, both depending on a MgCl2-precipitation step, the preferred one having advantages in speed and yield of the activities. The specific activities of the peptidases in the choroid-plexus membranes were, with the exception of carboxypeptidase M, lower than in renal microvillar membranes: those of aminopeptidase N, peptidyl dipeptidase A (‘angiotensin-converting enzyme’) and gamma-glutamyltransferase were 3-5-fold lower, those of aminopeptidase A and endopeptidase-24.11 were 12-15 fold lower, and those of dipeptidyl peptidase IV and aminopeptidase W were 50-70-fold lower. Carboxypeptidase M had a similar activity in both membranes. Alkaline phosphatase and (Na+ + K+)-activated ATPase were more active in the choroid-plexus membranes. No activity for microsomal dipeptidase, aminopeptidase P and carboxypeptidase P could be detected. Six of the peptidases and (Na+ + K+)-activated ATPase were also studied by immunoperoxidase histochemistry at light- and electron-microscopic levels. Endopeptidase-24.11 and (Na+ + K+)-activated ATPase were uniquely located on the brush border, and the other two peptidases appeared to be much more abundant on the endothelial lining of microvessels. Dipeptidyl peptidase IV and aminopeptidase W were also detected in microvasculature. Pial membranes associated with the brain and spinal cord also stained positively for endopeptidase-24.11, aminopeptidase N and peptidyl dipeptidase A. The immunohistochemical studies indicated the subcellular fractionation did not discriminate between membranes derived from epithelial cells (i.e. microvilli) and those from endothelial cells. The possible significance of these studies in relation to neuropeptide metabolism and the control of cerebrospinal fluid production is discussed.This publication has 47 references indexed in Scilit:
- Basic carboxypeptidases: regulators of peptide hormone activityTrends in Pharmacological Sciences, 1988
- α-Atrial natriuretic peptide binding sites in the rat choroid plexus are increased in the presence of hydrocephalusNeuroscience Letters, 1988
- Ectoenzymes of the kidney microvillar membrane Aminopeptidase P is anchored by a glycosyl‐phosphatidylinositol moietyFEBS Letters, 1988
- Presence of the atrial natriuretic peptide in human cerebrospinal fluidBiochemical and Biophysical Research Communications, 1987
- Brain Barrier Tissues: End Organs for AtriopeptinsScience, 1987
- H2Histamine Receptors on the Epithelial Cells of Choroid PlexusJournal of Neurochemistry, 1986
- Radioautographic Localization of 125I-Atrial Natriuretic Factor Binding Sites in the BrainNeuroendocrinology, 1986
- Endopeptidase‐24.11 and aminopeptidase activity in brain synaptic membranes are jointly responsible for the hydrolysis of cholecystokinin octapeptide (CCK‐8)FEBS Letters, 1984
- β-Adrenergic-Sensitive Adenylate Cyclase in Secretory Cells of Choroid PlexusScience, 1979
- Preparation of highly active (Na+ + K+)-ATPase from the outer medulla of rabbit kidneyBiochemical and Biophysical Research Communications, 1969