HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Add to Personal Folders Download to citation manager Author home page(s): Kunio Asada Shinjiro Sasaki Permission Requests Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Nishimoto, M. Articles by Miyazaki, M. Search for Related Content PubMed PubMed Citation Articles by Nishimoto, M. Articles by Miyazaki, M. Related Collections Cardiac - pharmacology Coronary disease

J Thorac Cardiovasc Surg 2001;121:729-734
© 2001 The American Association for Thoracic Surgery

Surgery for Acquired Cardiovascular Disease

Chymase-dependent angiotensin II formation in the saphenous vein versus the internal thoracic artery

From the Department of Pharmacology^a and the Department of Thoracic and Cardiovascular Surgery,^b Osaka Medical College, Takatsuki City, Osaka, Japan.

Supported in part by Grant-in-Aid 12770048 for Encouragement of Young Scientists and Grant-in-Aid 11470027 for Scientific Research (B) from the Ministry of Education, Science, Sports and Culture, Japan.

Received for publication May 4, 2000. Revisions requested Aug 22, 2000; revisions received Oct 10, 2000. Accepted for publication Oct 10, 2000. Address for reprints: Mizuo Miyazaki, MD, PhD, Department of Pharmacology, Osaka Medical College, 2-7 Daigaku-cho, Takatsuki City, Osaka 569-8686, Japan.

Abstract

Objectives: 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.
Conclusion: 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.

This article has been cited by other articles:

				Y. Soga, S. Takai, H. Okabayashi, A. Nagasawa, T. Yokota, K. Nishimura, M. Miyazaki, and M. Komeda Human gastroepiploic artery has greater chymase activity than the internal thoracic artery Eur. J. Cardiothorac. Surg., December 1, 2006; 30(6): 877 - 880. [Abstract] [Full Text] [PDF]

				S. A Doggrell and J. C Wanstall Vascular chymase: pathophysiological role and therapeutic potential of inhibition Cardiovasc Res, March 1, 2004; 61(4): 653 - 662. [Abstract] [Full Text] [PDF]

				C. F. Santos, M. A. V. Caprio, E. B. Oliveira, M. C. O. Salgado, D. N. Schippers, D. H. Munzenmaier, and A. S. Greene Functional role, cellular source, and tissue distribution of rat elastase-2, an angiotensin II-forming enzyme Am J Physiol Heart Circ Physiol, July 11, 2003; 285(2): H775 - H783. [Abstract] [Full Text] [PDF]

				K. Tsunemi, S. Takai, M. Nishimoto, A. Yuda, D. Jin, M. Sakaguchi, Y. Sawada, K. Asada, K. Kondo, S. Sasaki, et al. Lengthy suppression of vascular proliferation by a chymase inhibitor in dog grafted veins J. Thorac. Cardiovasc. Surg., September 1, 2002; 124(3): 621 - 625. [Full Text] [PDF]