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), an...

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Bibliographic Details
Published in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2000-08, Vol.21 (8), p.1249-1255
Main Authors: Vietinghoff, Gabriele, Paegelow, Inge
Format: Article
Language:English
Subjects:
Angiotensin-converting enzyme
Animals
Bradykinin
Bradykinin - metabolism
Bronchoalveolar lavage fluid
Carboxypeptidase M
Chromatography, High Pressure Liquid
Female
GPI-Linked Proteins
Guinea Pigs
Kinin metabolism
Macrophages
Macrophages, Alveolar - metabolism
Macrophages, Peritoneal - metabolism
Male
Metalloendopeptidase 24.15
Metalloendopeptidases - metabolism
Neprilysin - metabolism
Neutral endopeptidase 24.11
Peptidyl-Dipeptidase A - metabolism
Phenotype
Protease Inhibitors - pharmacology
Time Factors
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Summary: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.
ISSN:0196-9781
1873-5169
DOI:10.1016/S0196-9781(00)00266-7