Angiotensin-Converting Enzyme from Rabbit Pulmonary Particles

Soffer, Richard L.; Reza, Regino Morones; Caldwell, P. R. B.

doi:10.1073/pnas.71.5.1720

Cited by 59 publications

(22 citation statements)

References 19 publications

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“…), a nonionic detergent used in the initial purification procedure for converting enzyme (14). The appearance of the treated material in the electron microscope is shown in Fig.…”

Section: Methodsmentioning

confidence: 99%

Inhibition of angiotensin converting enzyme activity in cultured endothelial cells by hypoxia.

Stalcup¹,

Lipset²,

Woan³

et al. 1979

J. Clin. Invest.

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A B S T R A C T Endothelial cells in tissue culturedegrade bradykinin and convert angiotensin I to angiotensin II. These are both functions of a single dipeptidyl hydrolase, angiotensin converting enzyme. Monolayer cultures were prepared from human, rabbit, pig, and calf vessels. Angiotensin converting enzyme activity was assessed by adding either bradykinin or angiotensin I to the cells in culture flasks, and measuring residual peptide over time by radioimmunoassay. Peptide degradation was inhibited by the specific converting enzyme inhibitor, SQ 20881. The flasks were equilibrated with varying hypoxic gas mixtures: hypoxia rapidly (<2 min) decreased enzyme activity and room air restored it as rapidly. The extent to which activity was reduced was a direct function of Po2 (r = 0.93, P < 0.001), and there was no enzyme activity below a Po2 of 30 mm Hg. Four preparations were studied with respect to decrease in enzyme activity by hypoxia: (a) intact cells in monolayer, (b) sonicated cells, (c) sonicated cells from which converting enzyme was partially dissolved by a detergent, and (d) purified converting enzyme. Hypoxia had progressively less of an inhibiting effect on the enzyme activity of the preparations as the degree of cell integrity decreased. Hypoxia inhibits angiotensin converting enzyme activity in cultured endothelial cells, but the effect of hypoxia is not on the enzyme per se, but appears to be a unique characteristic of the endothelial cell.

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“…), a nonionic detergent used in the initial purification procedure for converting enzyme (14). The appearance of the treated material in the electron microscope is shown in Fig.…”

Section: Methodsmentioning

confidence: 99%

Inhibition of angiotensin converting enzyme activity in cultured endothelial cells by hypoxia.

Stalcup¹,

Lipset²,

Woan³

et al. 1979

J. Clin. Invest.

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“…Rabbit pulmonary ACE was purified as previously described (18,19). radial processes of follicular cells.…”

Section: Methodsmentioning

confidence: 99%

In vivo interaction of antibodies with cell surface antigens. A mechanism responsible for in situ formation of immune deposits in the zona pellucida of rabbit oocytes.

Matsuo¹,

Caldwell²,

Brentjens³

et al. 1985

J. Clin. Invest.

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It was the aim of this study to test the hypothesis that the interaction of antibodies with antigens expressed on the plasma membrane of cells surrounded by a basement membrane or a basement membrane-like structure results in in situ formation of immune deposits. Ovary was chosen for the experiments because we found that a well-characterized protein, angiotensinconverting enzyme (ACE), is expressed in a diffuse pattern on the plasma membrane of mature oocytes.To investigate the events following the in vivo interaction of oolemma-ACE with its antibody, rabbits were injected with goat anti-rabbit ACE y-globulin or with Fab fragments of goat anti-rabbit ACE IgG in an ear vein for a maximum of 4 d; they were followed for up to 20 d thereafter. Ovary tissue was studied by immunofluorescence, and immunoelectron, light, and transmission electron microscopy.The results of this study document two new findings: First, that ACE is expressed on the oolemma of rabbit oocytes. Second, that the in vivo interaction of divalent antibodies to this cell surface antigen induces formation of granular immune deposits in the adjacent zona pellucida through a mechanism of "patching" and "shedding" of immune complexes, similar to that occurring in in vitro systems characterized by interaction of plasma membrane receptors with soluble ligands. This mechanism might have importance in the pathogenesis of Heymann glomerulonephritis and of other immunological diseases involving antigens expressed on the plasma membrane of cells.

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“…Activity in plasma-converting enzyme is reported to be decreased in chronic lung disease, but the decrease was not quantitatively related to the severity of the lung disease. From these reports, it is presumed that the change in quantity or function of pulmonary converting enzyme is dependent on endothelial cell membranes [58].…”

Section: Pituitary [36] and Male Gonad [36] Was Demonstrated Usimentioning

confidence: 99%

Renin-Angiotensin System

Okuyama

Nonomura

Nakamura

et al. 1988

Archives of Andrology

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A. OKUYAMA, N. NONOMURA, M. NAKAMURA, M. NAMIKI, and T. SONODA Renin, a protease that cleaves the prohormone angiotensinogen thereby releasing angiotensin I, plays a major role in regulating blood pressure and electrolyte balance. Although renin is synthesized mainly in the cortical cells of the kidney, the presence of renin or reninlike activity has been recognized in various extrarenal tissues of humans and animals, including such reproductive organs as LH-containing cells of the anterior pituitary, placentral trophoblasts, and Leydig cells of the male gonad. It has also been learned that the renin in these extrarenal tissues generates angiotensins locally, which may interact with angiotensin I1 receptors in a paracrine or autocrine manner. However, the precise roles of the reninangiotensin system in extrarenal tissue are not yet understood. We demonstrated the renin-angiotensin system in human testis by measuring the plasma renin activity (PRA), plasma angiotensin I1 (PAII), and testosterone in the internal spermatic vein (ISV) simultaneously after treatment with hCG, and elucidated the relationship between the renin-angiotensin system and sex steroids from Leydig cells of the male gonad.

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Angiotensin-Converting Enzyme from Rabbit Pulmonary Particles

Cited by 59 publications

References 19 publications

Inhibition of angiotensin converting enzyme activity in cultured endothelial cells by hypoxia.

Inhibition of angiotensin converting enzyme activity in cultured endothelial cells by hypoxia.

In vivo interaction of antibodies with cell surface antigens. A mechanism responsible for in situ formation of immune deposits in the zona pellucida of rabbit oocytes.

Renin-Angiotensin System

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