Degradation of bradykinin by peritoneal and alveolar macrophages of the guinea pig.
Peptidase inhibitors and identification of the peptide fragments were used for the characterization of the bradykinin metabolism by alveolar and peritoneal macrophages. Both cell types show differences in the rate of inactivation and in the quantity of the metabolites generated. BK(1-5), BK(1-8), and BK(1-7) are the predominant direct metabolites. Metalloendopeptidase 24.15, carboxypeptidase M, and an unidentified peptidase are responsible for their formation. Angiotensin-converting enzyme and neutral endopeptidase 24.11 do not play a crucial role in the degradation of bradykinin by macrophages. In the bronchoalveolar space, other cells than the macrophages are more important to the breakdown of this peptide.
Vietinghoff
G
G
Department of Experimental and Clinical Pharmacology and Toxicology, University of Rostock, Schillingallee 70, D-18055, Germany. gabriele.vietinghoff@med.uni-rostock.de
Paegelow
I
I
D000818:Animals; D001920:Bradykinin / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D005260:Female; D058851:GPI-Linked Proteins; D006168:Guinea Pigs; D016676:Macrophages, Alveolar / Q000378:metabolism*; D017737:Macrophages, Peritoneal / Q000378:metabolism*; D008297:Male; D008666:Metalloendopeptidases / Q000378:metabolism; D015260:Neprilysin / Q000378:metabolism; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D010641:Phenotype; D011480:Protease Inhibitors / Q000494:pharmacology; D013997:Time Factors
D058851:GPI-Linked Proteins; D011480:Protease Inhibitors; D007703:Peptidyl-Dipeptidase A; C058479:carboxypeptidase M; D008666:Metalloendopeptidases; D015260:Neprilysin; C022510:thimet oligopeptidase; D001920:Bradykinin