Pulmonary angiotensin converting enzyme activity in elastase induced emphysema.
Pulmonary emphysema would be expected to reduce angiotensin converting enzyme (ACE) activity due to diminished capillary bed. However, transpulmonary angiotensin conversion has been found to be unaffected or marginally reduced in emphysema. In the present study we examined the activity of ACE in an experimental model of emphysema. Vmax and Km of ACE were determined in lung homogenates of six hamsters with elastase-induced emphysema and seven control hamsters. In the emphysematous lungs, ACE activity was significantly elevated due to marked increase in Vmax (19.2 +/- 1.7 vs. 4.9 +/- 1.6 nmol/min/mg protein for emphysematous and control lungs, P < 0.01). The Km of ACE was unaffected by emphysema. We suggest that the increase in ACE activity may be an adaptive change to enable adequate metabolic activity in the face of progressive reduction in pulmonary capillary surface area in emphysema.
Itzkowitz
D
D
Department of Internal Medicine B, Bnai-Zion Medical Center, Haifa, Israel.
Mor
L
L
Bomzon
A
A
Oliven
A
A
D000595:Amino Acid Sequence; D000809:Angiotensins / Q000378:metabolism; D000818:Animals; D001835:Body Weight; D006224:Cricetinae; D007700:Kinetics; D008168:Lung / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D008647:Mesocricetus; D008969:Molecular Sequence Data; D009929:Organ Size; D010196:Pancreatic Elastase / Q000494:pharmacology; D010446:Peptide Fragments / Q000378:metabolism; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D011656:Pulmonary Emphysema / Q000201:enzymology*
D000809:Angiotensins; D010446:Peptide Fragments; D007703:Peptidyl-Dipeptidase A; D010196:Pancreatic Elastase