Subcellular localization of pulmonary antiotensin-converting enzyme (kininase II)

Ryan, James W.; Ryan, Una S.; Schultz, Duane R.; Whitaker, Cecil; Chung, Alfred

doi:10.1042/bj1460497

Cited by 296 publications

(99 citation statements)

References 9 publications

(13 reference statements)

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“…Two probable markers are available for the alveolar endothelial cells; physiological evidence suggests that membrane-bound carbonic anhydrase is concentrated in endothelial cells (Klocke, 1978;Crandall & O'Brasky, 1978;Effros et al, 1978) and angiotensin converting enzyme is situated along the luminal surface of pulmonary endothelial cells (Ryan et al, 1975). Morphometric data on the developing rat lung have been published .…”

Section: Discussionmentioning

confidence: 99%

Postnatal development of rat lung. Changes in lung lectin, elastin, acetylcholinesterase and other enzymes

Powell

Whitney

1980

Biochemical Journal

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The development of rat lung from a primitive gas-exchange organ to the mature respiratory organ is in large part a postnatal phenomenon that has been well characterized by morphological and morphometric methods. The alveolarization of the lung is achieved during the first 3 weeks of life. Cholinergic innervation of rat lung also appears postnatally. We have monitored the presence or activity of several proteins during postnatal rat lung development. Newborn-rat lung contains negligible amounts of acetylcholinesterase, but the specific activity of acetylcholinesterase reaches adult values by postnatal day 10-11. Neonatal-rat lung does not contain significant amounts of ,B-galactoside-binding protein [Powell (1980) Biochem. J. 187, 123-1291. The activity of this endogenous lung lectin was apparent at about day 6, was maximal between days 10 and 13 before declining 8-10-fold to reach adult values. Elastin has been implicated from morphological evidence as critical to lung restructuring. We have quantified the amount of desmosine and isodesmosine per g wet wt. of lung. The concentration of elastin, by this criterion, was low and stationary until postnatal day 7; a dramatic increase in elastin concentration occurred between days 10 and 20, when adult values were reached. The peak of lung-lectin activity was coincident with the maturation of acetylcholinesterase and the beginning of rapid elastin cross-linking. The specific activities of angiotensin-converting enzyme, carbonic anhydrase, choline kinase and glucose 6-phosphate dehydrogenase were also monitored.

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Section: Discussionmentioning

confidence: 99%

Postnatal development of rat lung. Changes in lung lectin, elastin, acetylcholinesterase and other enzymes

Powell

Whitney

1980

Biochemical Journal

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“…To establish a connection with previous electron microscopic immunocytochemical findings, we used several antibodies directed against integral membrane proteins known to be expressed at the level of endothelium in lung and/or other organs, e.g., thrombomodulin (Horvat and Palade, 1993), functional thrombin receptor (Horvat and Palade, 1995), podocalyxin (Horvat et al, 1986), and the angiotensin-converting enzyme (ACE;Ryan et al, 1975). Figure 6A shows the results obtained and compares the distribution of these antigens with that of caveolin.…”

Section: Presence Of Endothelial-specific Markersmentioning

confidence: 99%

Immunoisolation and partial characterization of endothelial plasmalemmal vesicles (caveolae).

Stan

Roberts

Predescu

et al. 1997

MBoC

193

174

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Plasmalemmal vesicles (PVs) or caveolae are plasma membrane invaginations and associated vesicles of regular size and shape found in most mammalian cell types. They are particularly numerous in the continuous endothelium of certain microvascular beds (e.g., heart, lung, and muscles) in which they have been identified as transcytotic vesicular carriers. Their chemistry and function have been extensively studied in the last years by various means, including several attempts to isolate them by cell fractionation from different cell types. The methods so far used rely on nonspecific physical parameters of the caveolae and their membrane (e.g., size-specific gravity and solubility in detergents) which do not rule out contamination from other membrane sources, especially the plasmalemma proper. We report here a different method for the isolation of PVs from plasmalemmal fragments obtained by a silica-coating procedure from the rat lung vasculature. The method includes sonication and flotation of a mixed vesicle fraction, as the first step, followed by specific immunoisolation of PVs on anticaveolin-coated magnetic microspheres, as the second step. The mixed vesicle fraction is thereby resolved into a bound subfraction (B), which consists primarily of PVs or caveolae, and a nonbound subfraction (NB) enriched in vesicles derived from the plasmalemma proper. The results so far obtained indicate that some specific endothelial membrane proteins (e.g., thrombomodulin, functional thrombin receptor) are distributed about evenly between the B and NB subfractions, whereas others are restricted to the NB subfraction (e.g., angiotensin converting enzyme, podocalyxin). Glycoproteins distribute unevenly between the two subfractions and antigens involved in signal transduction [e.g., annexin II, protein kinase Ca, the Ga subunits of heterotrimeric G proteins (as, aq, ai2, ai3)

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“…Histochemical studies with antibody prepared against pure enzyme established that the protein was a constituent of the luminal surface of pulmonary vascular endothelial cells (8), and subsequent investigations (9) revealed that the enzyme was also a specific vascular endothelial component in other organs.…”

Section: Discussionmentioning

confidence: 99%

“…It also liberates Phe-Arg and Ser-Pro from bradykinin (4, 5), thereby inactivating this vasodepressor nonapeptide. The enzyme is a glycoprotein (5, 6) that is localized on the luminal surface of vascular endothelial cells in anatomic juxtaposition to the circulation (7)(8)(9). Specific chemical inhibitors of its activity (10-12) can reverse experimental renovascular hypertension (13-17) and can reduce blood pressure in a substantial fraction of human hypertensive disease (18, 19).…”

mentioning

confidence: 99%

Reversal of renovascular hypertension by antibodies specific for angiotensin-converting enzyme.

Markle¹,

Sonnenblick

Conroy

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

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Goat antibodies developed against pure rabbit pulmonary an iotensin-converting enzyme (pe tidyl dipeptidase, EC 3.4.1) were administered intravenousyto rats with two-kidney Goldblatt hypertension and to normotensive animals. In the hypertensive model these antibodies were associated with a sustained, immune-dependent decrease of blood pressure to normal values. A smaller, but also immune-specific, reduction of blood pressure was observed in the normotensive group. The data suggest that heterologous antibody directed against angiotensin-converting enzyme may provide a biologically specific probe for examining the contribution of the renin-angiotensin system to normal and pathologic circulatory states. Angiotensin-converting enzyme (EC 3.4.15.1) is a COOHterminal peptidyl dipeptidase that catalyzes release of His-Leu from angiotensin I (1) to yield angiotensin II, the biologically active vasopressor octapeptide of the renin-angiotensin system (2, 3). It also liberates Phe-Arg and Ser-Pro from bradykinin (4, 5), thereby inactivating this vasodepressor nonapeptide. The enzyme is a glycoprotein (5, 6) that is localized on the luminal surface of vascular endothelial cells in anatomic juxtaposition to the circulation (7)(8)(9). Specific chemical inhibitors of its activity (10-12) can reverse experimental renovascular hypertension (13-17) and can reduce blood pressure in a substantial fraction of human hypertensive disease (18, 19). These considerations suggest that converting enzyme provides an unusual opportunity for exploring the possibility that the activity of an enzyme can be inhibited by specific anticatalytic antibody in vivo and that a pathologic process can thus be immunologically controlled.To investigate this possibility we isolated pure rabbit pulmonary converting enzyme (5, 6) and then developed goat antibodies against it (20). When these antibodies were administered intravenously to rabbits, even in relatively small amounts, they caused an immune-dependent lethal reaction that could not be explained solely on the basis of their anticatalytic effect (21 The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisenmnt" in accordance with 18 U. S. C. §1734 solely to indicate this fact.In order to circumvent this lethal reaction we examined immunologic homology of the rabbit enzyme with enzymes from other species by using the antibodies to rabbit enzyme as a probe (24). We found that these antibodies inhibited rat converting activity in vitro and were well tolerated by this heterologous recipient animal even at very high dosage. It has not yet been established whether the lethal effect in rabbits as contrasted with rats is a universal complication of administration of antibody to converting enzyme to homologous recipient animals or a species-specific phenomenon associated with the rabbit. The recent isolation of pure canine converting enzyme and goat antibodies directed against it (25) provides another experimental system ...

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Subcellular localization of pulmonary antiotensin-converting enzyme (kininase II)

Cited by 296 publications

References 9 publications

Postnatal development of rat lung. Changes in lung lectin, elastin, acetylcholinesterase and other enzymes

Postnatal development of rat lung. Changes in lung lectin, elastin, acetylcholinesterase and other enzymes

Immunoisolation and partial characterization of endothelial plasmalemmal vesicles (caveolae).

Reversal of renovascular hypertension by antibodies specific for angiotensin-converting enzyme.

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