Kinins pp 217-227 | Cite as

Kininase II (Angiotensin Converting Enzyme) and Endothelial Cells in Culture

  • Una S. Ryan
  • J. W. Ryan
  • A. Chiu
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 70)


It is now well recognized that the lungs process the circulating vasoactive polypeptides, bradykinin and angiotensin I; the former being inactivated while the latter is activated (Ferreira & Vane, 1967; Ng & Vane, 1967; Ryan et al., 1968; 1970b, 1971, 1972). Previously (Ryan et al., 1968, 1969, 1970a & b, 1971; Smith & Ryan, 1972, 1973a), we have postulated that the enzymes responsible for the metabolism of these polypeptides are situated on or close to the luminal surface of the pulmonary endothelial cells. Over the past seven years much evidence from our laboratory (see references above) and those of others (Bakhle, 1968; Sander & Huggins, 1971; Lanzillo & Fanburg, 1974; Soffer et al., 1974) have supported this hypothesis. Recently (Dorer et al., 1972, 1974) have shown that the enzyme that activates angiotensin I (by conversion to angiotensin II) is also responsible in part for the inactivation of bradykinin. As described in the accompanying paper (Ryan, J.W., this volume), we have raised antibodies to this enzyme and are using the antibodies labelled for immunocytochemistry in efforts to provide a definitive test of our hypothesis. This report represents a fine focus on the localization of kininase II using a specific cell type in culture namely, pulmonary endothelial cells.


Endothelial Cell Pulmonary Artery Lipid Droplet Endothelial Cell Culture Pulmonary Artery Endothelial Cell 
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Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Una S. Ryan
    • 1
  • J. W. Ryan
    • 1
  • A. Chiu
    • 1
  1. 1.Papanicolaou Cancer Research InstituteUniversity of Miami School of MedicineMiamiUSA

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