Characterization of neuronal and endothelial forms of angiotensin converting enzyme in pig brain.
The molecular forms of angiotensin converting enzyme (ACE; EC 3.4.15.1) in preparations of pig brain cortical microvessels and striatal synaptosomal membranes have been identified by immunoelectrophoretic blot analysis. The cortical microvessels contained only the endothelial form of the enzyme, Mr 180,000, which comigrated with pig kidney ACE on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In contrast, the synaptosomal membranes contained only a smaller form of ACE, Mr 170,000, which represents the neuronal form of the enzyme. No significant differences in inhibitor sensitivity or substrate specificity were detected between the two forms of ACE. In particular, neurokinin A was resistant to hydrolysis by either microvessel or synaptosomal membrane ACE, and the pattern of hydrolysis of substance P by the two preparations was identical.
Williams
T A
TA
Department of Biochemistry and Molecular Biology, University of Leeds, England, U.K.
Hooper
N M
NM
Turner
A J
AJ
D000818:Animals; D001921:Brain / Q000166:cytology / Q000201:enzymology*; D002560:Cerebrovascular Circulation; D003342:Corpus Striatum / Q000201:enzymology; D004730:Endothelium, Vascular / Q000378:metabolism*; D006868:Hydrolysis; D007122:Immunoelectrophoresis; D007527:Isoenzymes / Q000378:metabolism*; D008833:Microcirculation; D009474:Neurons / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D013552:Swine; D013574:Synaptosomes / Q000201:enzymology
D007527:Isoenzymes; D010455:Peptides; D007703:Peptidyl-Dipeptidase A