Evaluation of Antihypertensive and Antihyperlipidemic Effects of Bamboo Shoot Angiotensin Converting Enzyme Inhibitory Peptide in Vivo

2012 ◽  
Vol 60 (45) ◽  
pp. 11351-11358 ◽  
Author(s):  
Lianliang Liu ◽  
Lingyi Liu ◽  
Baiyi Lu ◽  
Daozong Xia ◽  
Ying Zhang
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Bamboo Shoot ◽  
Converting Enzyme ◽  
Inhibitory Peptide

A novel angiotensin-converting enzyme inhibitory peptide from rabbit meat protein hydrolysate: Identification, molecular mechanism, and antihypertensive effect in vivo

2021 ◽  
Author(s):  
Junbo Chen ◽  
Xiaodong Yu ◽  
Wangxiang Huang ◽  
Chen Wang ◽  
Qiyi He
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Antihypertensive Effect ◽  
Protein Hydrolysate ◽  
Converting Enzyme ◽  
Inhibitory Effects ◽  
Inhibitory Peptide ◽  
Rabbit Meat ◽  
Natural Foods ◽  
Ace Inhibitory

Bioactive peptides exhibiting angiotensin-converting enzyme (ACE) inhibitory effects and extracted from natural foods have potential as healthy and safe therapeutics for high blood pressure. A novel ACE inhibitory tetrapeptide Trp-Gly-Ala-Pro...

Immunotargeting of catalase to lung endothelium via anti-angiotensin-converting enzyme antibodies attenuates ischemia-reperfusion injury of the lung in vivo

2007 ◽  
Vol 293 (1) ◽  
pp. L162-L169 ◽  
Author(s):  
Kai Nowak ◽  
Sandra Weih ◽  
Roman Metzger ◽  
Ronald F. Albrecht ◽  
Stefan Post ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Weight Ratio ◽  
Dry Weight ◽  
Serum Levels ◽  
Converting Enzyme ◽  
Pulmonary Endothelium ◽  
Preferential Expression

Limitation of reactive oxygen species-mediated ischemia-reperfusion (I/R) injury of the lung by vascular immunotargeting of antioxidative enzymes has the potential to become a promising modality for extension of the viability of banked transplantation tissue. The preferential expression of angiotensin-converting enzyme (ACE) in pulmonary capillaries makes it an ideal target for therapy directed toward the pulmonary endothelium. Conjugates of ACE monoclonal antibody (MAb) 9B9 with catalase (9B9-CAT) have been evaluated in vivo for limitation of lung I/R injury in rats. Ischemia of the right lung was induced for 60 min followed by 120 min of reperfusion. Sham-operated animals (sham, n = 6) were compared with ischemia-reperfused untreated animals (I/R, n = 6), I/R animals treated with biotinylated catalase (CAT, n = 6), and I/R rats treated with the conjugates (9B9-CAT, n = 6). The 9B9-CAT accumulation in the pulmonary endothelium of injured lungs was elucidated immunohistochemically. Arterial oxygenation during reperfusion was significantly higher in 9B9-CAT (221 ± 36 mmHg) and sham (215 ± 16 mmHg; P < 0.001 for both) compared with I/R (110 ± 10 mmHg) and CAT (114 ± 30 mmHg). Wet-dry weight ratio of I/R (6.78 ± 0.94%) and CAT (6.54 ± 0.87%) was significantly higher than of sham (4.85 ± 0.29%; P < 0.05), which did not differ from 9B9-CAT (5.58 ± 0.80%). The significantly lower degree of lung injury in 9B9-CAT-treated animals compared with I/R rats was also shown by decreased serum levels of endothelin-1 (sham, 18 ± 9 fmol/mg; I/R, 42 ± 12 fmol/mg; CAT, 36 ± 11 fmol/mg; 9B9-CAT, 26 ± 9 fmol/mg; P < 0.01) and mRNA for inducible nitric oxide synthase (iNOS) [iNOS-GAPDH ratio: sham, 0.15 ± 0.06 arbitrary units (a.u.); I/R, 0.33 ± 0.08 a.u.; CAT, 0.26 ± 0.05 a.u.; 9B9-CAT, 0.14 ± 0.04 a.u.; P < 0.001]. These results validate immunotargeting by anti-ACE conjugates as a prospective and specific strategy to augment antioxidative defenses of the pulmonary endothelium in vivo.

Dual inhibition of angiotensin converting enzyme and neutral endopeptidase by omapatrilat in rat in vivo

2001 ◽  
Vol 44 (5) ◽  
pp. 411-418 ◽  
Author(s):  
Tom Bäcklund ◽  
Eeva Palojoki ◽  
Tina Grönholm ◽  
Anders Eriksson ◽  
Olli Vuolteenaho ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Neutral Endopeptidase ◽  
Converting Enzyme ◽  
Dual Inhibition

scholarly journals Novel activity of angiotensin-converting enzyme. Hydrolysis of cholecystokinin and gastrin analogues with release of the amidated C-terminal dipeptide

1989 ◽  
Vol 262 (1) ◽  
pp. 125-130 ◽  
Author(s):  
P Dubreuil ◽  
P Fulcrand ◽  
M Rodriguez ◽  
H Fulcrand ◽  
J Laur ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Chloride Ion ◽  
Peptide Bond ◽  
Major Product ◽  
Enzyme Hydrolysis ◽  
Ion Concentration ◽  
Converting Enzyme ◽  
Rabbit Lung ◽  
Hydrolysis Of

ACE (angiotensin-converting enzyme; peptidyl dipeptidase A; EC 3.4.15.1), cleaves C-terminal dipeptides from active peptides containing a free C-terminus. We investigated the hydrolysis of cholecystokinin-8 [CCK-8; Asp-Tyr(SO3H)-Met-Gly-Trp-Met-Asp-Phe-NH2] and of various gastrin analogues by purified rabbit lung ACE. Although these peptides are amidated at their C-terminal end, they were metabolized by ACE to several peptide fragments. These fragments were analysed by h.p.l.c., isolated and identified by comparison with synthetic fragments, and by amino acid analysis. The initial and major site of hydrolysis was the penultimate peptide bond, which generated a major product, the C-terminal amidated dipeptide Asp-Phe-NH2. As a secondary cleavage, ACE subsequently released di- or tri-peptides from the C-terminal end of the remaining N-terminal fragments. The cleavage of CCK-8 and gastrin analogues was inhibited by ACE inhibitors (Captopril and EDTA), but not by other enzyme inhibitors (phosphoramidon, thiorphan, bestatin etc.). Hydrolysis of [Leu15]gastrin-(14-17)-peptide [Boc (t-butoxycarbonyl)-Trp-Leu-Asp-Phe-NH2] in the presence of ACE was found to be dependent on the chloride-ion concentration. Km values for the hydrolysis of CCK-8, [Leu15]gastrin-(11-17)-peptide and Boc-[Leu15]gastrin-(14-17)-peptide at an NaCl concentration of 300 mM were respectively 115, 420 and 3280 microM, and the catalytic constants were about 33, 115 and 885 min-1. The kcat/Km for the reactions at 37 degrees C was approx. 0.28 microM-1.min-1, which is approx. 35 times less than that reported for the cleavage of angiotensin I. These results suggest that ACE might be involved in the metabolism in vivo of CCK and gastrin short fragments.

Assay of Pulmonary Microvascular Endothelial Angiotensin Converting Enzyme, in Vivo: Comparison of Three Methods

1993 ◽  
pp. 192-193
Author(s):  
S. E. Orfanos ◽  
X-L Chen ◽  
J. W. Ryan ◽  
A. Y. K. Chung ◽  
S. E. Burch ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Converting Enzyme ◽  
Microvascular Endothelial

Interaction of mAb to angiotensin-converting enzyme (ACE) with antigen in vitro and in vivo: antibody targeting to the lung induces ACE antigenic modulation

1994 ◽  
Vol 6 (8) ◽  
pp. 1153-1160 ◽  
Author(s):  
Sergei Danilov ◽  
Elena Atochina ◽  
Holger Hiemisch ◽  
Tatiana Churak-ova ◽  
Aygul Moldobayeva ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Converting Enzyme ◽  
Antigenic Modulation ◽  
Antibody Targeting

scholarly journals Angiotensin-Converting Enzyme C-Terminal Catalytic Domain Is the Main Site of Angiotensin I Cleavage In Vivo

Hypertension ◽  
2008 ◽  
Vol 51 (2) ◽  
pp. 267-274 ◽  
Author(s):  
Sebastien Fuchs ◽  
Hong D. Xiao ◽  
Christine Hubert ◽  
Annie Michaud ◽  
Duncan J. Campbell ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Catalytic Domain ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
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