Chymase-dependent angiotensin II formation in the saphenous vein versus the internal thoracic artery.
OBJECTIVE
The great saphenous vein graft is known to be less patent than the internal thoracic artery graft. Recently, we reported that chymase-dependent angiotensin II formation plays an important role in the development of intimal hyperplasia in dog grafted veins. In this study we investigated the levels of angiotensin II-forming enzymes, angiotensin-converting enzyme, and chymase in human saphenous veins and internal thoracic arteries.


METHODS
The saphenous vein and internal thoracic artery specimens were obtained from coronary artery bypass grafts of patients during surgical procedures (saphenous vein, n = 16; internal thoracic artery, n = 16). Activities of angiotensin-converting enzyme and chymase were determined by using the extract from the saphenous vein or internal thoracic artery. Sections of the saphenous vein or internal thoracic artery were stained with van Gieson's elastin stain and were immunostained with anti-human chymase antibody.


RESULTS
The activities of angiotensin-converting enzyme in the saphenous vein and internal thoracic artery were 0.34 +/- 0.12 and 0.32 +/- 0.17 mU/mg protein, respectively, and the difference was not significant. The chymase activity in the saphenous vein was significantly higher than that in the internal thoracic artery (saphenous vein, 10.1 +/- 0.81 mU/mg protein; internal thoracic artery, 6.21 +/- 1.86 mU/mg protein). Chymase-positive cells in the saphenous vein were located in both the media and adventitia, and those in the internal thoracic artery were located only in the adventitia. The number of chymase-positive cells in the saphenous vein was about 2.6 times that in the internal thoracic artery.


CONCLUSIONS
The chymase activity, but not the angiotensin-converting enzyme activity, was significantly higher in the saphenous vein, suggesting that the high levels of chymase activity may be related to the poorer performance of the saphenous vein for use as a bypass conduit.
Nishimoto
M
M
Department of Pharmacology and the Department of Thoracic and Cardiovascular Surgery, Osaka Medical College, 2-7 Daigaku-cho, Takatsuki City, Osaka, Japan.
Takai
S
S
Sawada
Y
Y
Yuda
A
A
Kondo
K
K
Yamada
M
M
Jin
D
D
Sakaguchi
M
M
Asada
K
K
Sasaki
S
S
Miyazaki
M
M
D000368:Aged; D000369:Aged, 80 and over; D000804:Angiotensin II / Q000276:immunology / Q000378:metabolism*; D000911:Antibodies, Monoclonal / Q000032:analysis; D053818:Chymases; D001026:Coronary Artery Bypass / Q000379:methods; D003327:Coronary Disease / Q000601:surgery; D005260:Female; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology; D008297:Male; D008323:Mammary Arteries / Q000166:cytology / Q000201:enzymology* / Q000637:transplantation; D008875:Middle Aged; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D012501:Saphenous Vein / Q000166:cytology / Q000201:enzymology* / Q000637:transplantation; D012697:Serine Endopeptidases / Q000276:immunology / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D007074:Immunoglobulin G; D000804:Angiotensin II; D007703:Peptidyl-Dipeptidase A; D012697:Serine Endopeptidases; D053818:Chymases