Document Detail


Peptidases in human bronchoalveolar lining fluid, macrophages, and epithelial cells: dipeptidyl (amino)peptidase IV, aminopeptidase N, and dipeptidyl (carboxy)peptidase (angiotensin-converting enzyme).
MedLine Citation:
PMID:  9422334     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The modulation of proteolytic activity is an important factor in regulating the metabolism and function of peptide hormones. In this study, the activities of dipeptidyl (carboxy)peptidase (angiotensin-converting enzyme [ACE]), aminopeptidase N (APN), and dipeptidyl (amino)peptidase IV (DPP IV) were measured in the blood, the human bronchial epithelial and alveolar cells, bronchoalveolar macrophages, and the soluble phase of bronchoalveolar lavage (BAL) samples obtained from normal human volunteers and patients with pulmonary pathologic conditions. BAL fluid expressed ACE activity and very low levels of APN and DPP IV activities in the volunteer population, but higher levels could be measured in samples from patients. In patients, increased APN corresponded to a high granulocyte count, while DPP IV and ACE were associated with a high percentage of lymphocytes. Neither AIDS nor smoking induced an increased level of these enzymes. Immunohistochemical staining of bronchoalveolar smears with anti-human ACE monoclonal antibody showed that only macrophages expressed this enzyme. Enzyme histochemistry for DPP IV and APN showed that all leukocytes expressed these activities. APN, DPP IV, and ACE activities were also found in cell extracts of bronchoalveolar macrophages. In extracts of bronchial epithelial and alveolar cells, only APN and DPP IV activities were detected. Kinetic properties of the soluble enzymes in lavage supernatants were comparable to those of serum enzymes. These results demonstrate that soluble forms of cellular enzymes found in BAL fluid are regulated independently of blood and that different cell types may release these enzymes.
Authors:
L Juillerat-Jeanneret; J D Aubert; P Leuenberger
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of laboratory and clinical medicine     Volume:  130     ISSN:  0022-2143     ISO Abbreviation:  J. Lab. Clin. Med.     Publication Date:  1997 Dec 
Date Detail:
Created Date:  1998-01-27     Completed Date:  1998-01-27     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0375375     Medline TA:  J Lab Clin Med     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  603-14     Citation Subset:  AIM; IM; X    
Affiliation:
Department of Internal Medicine, Centre Hospitalier Universitaire Vandois, and the Institute of Pathology, Lausanne, Switzerland.
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MeSH Terms
Descriptor/Qualifier:
Adult
Aged
Antigens, CD13 / metabolism*
Antigens, CD26 / metabolism*
Bronchoalveolar Lavage Fluid / chemistry*
Cells, Cultured
Epithelial Cells / enzymology
Female
Histocytochemistry
Humans
Hydroxamic Acids / pharmacology
Kinetics
Lisinopril / pharmacology
Lung / enzymology*
Lung Diseases / enzymology*
Macrophages, Alveolar / enzymology*
Male
Middle Aged
Oligopeptides / pharmacology
Peptidyl-Dipeptidase A / metabolism*
Protease Inhibitors / pharmacology
Chemical
Reg. No./Substance:
0/Hydroxamic Acids; 0/Oligopeptides; 0/Protease Inhibitors; 13434-13-4/actinonin; 83915-83-7/Lisinopril; 90614-48-5/diprotin A; EC 3.4.11.2/Antigens, CD13; EC 3.4.14.5/Antigens, CD26; EC 3.4.15.1/Peptidyl-Dipeptidase A

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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