Disease relevance of ACE

• Acute hypoxia decreased the angiotensin I-converting enzyme activity in guinea pig lung and carp gill arch, but the changes in chicken lung and kidney were considered nonsignificant [1].
• The evaluation of anti-hypertensive activities of whole hydrolysates and fractions were also tested, monitoring the ability of the fraction to inhibit the activity of angiotensin I-converting enzyme involved in hypertension regulation [2].
• We found that angiotensin I-converting enzyme (ACE), ataxia-telangiectasia mutated protein (ATM), calpain 1, and stearoyl coenzyme A desaturase 1 (SCD1) were highly expressed in adipocytes compared with preadipocytes (P < 0.05) [3].

High impact information on ACE

• Inhibition of the angiotensin I-converting enzyme by captopril (10 nmol/mL) suppressed angiotensin II by 85% and increased angiotensin I by 352% (n = 5, P < .05) [4].
• Peptidyl dipeptidase A (angiotensin-I-converting enzyme) was of less importance, even in respect of angiotensin I and bradykinin [5].
• Angiotensin I-converting enzyme inhibition but not angiotensin II suppression alters angiotensin I-converting enzyme gene expression in vessels and epithelia [6].
• Structural and biological roles of glycosylations in pulmonary angiotensin I-converting enzyme [7].
• Angiotensin I-converting enzyme (ACE/kininase II) inhibitors potentiated guinea pig ileum's isotonic contractions to bradykinin (BK) and its analogues, shifting the BK dose-response curve to the left [8].

Biological context of ACE

• These peptides inhibited angiotensin I-converting enzyme activity with an IC50 of 5.8, 7.4, 2.1 and 1.9 microM, respectively [9].
• T-kinin is resistant to hydrolysis by angiotensin I-converting enzyme [10].
• The angiotensin I-converting enzyme (ACE; EC.3.4.15.1) is a dipeptidyl carboxypeptidase that plays a central role in blood pressure regulation [11].
• 1. Somatic angiotensin I-converting enzyme (ACE) is a protein that contains two similar domains (N- and C-terminal), each possessing an active site [12].

Anatomical context of ACE

• Vascular origin determines angiotensin I-converting enzyme expression in endothelial cells [13].
• Angiotensin I-converting enzyme [EC 3.4.15.1] was rapidly and highly purified from a particulate fraction of hog kidney cortex with 13% yield [14].
• Previous observations on the heterogeneous distribution of von Willebrand factor in the vascular endothelium led us to examine the expression of angiotensin I-converting enzyme (ACE) in function of the vascular origin of endothelial cells (EC) [13].

Associations of ACE with chemical compounds

• Ramiprilat is an angiotensin I-converting enzyme (ACE) inhibitor whose particular lipophilicity may modify its inhibitory activity on the cellular form of this enzyme in comparison to ACE inhibitors that are more hydrophilic [15].
• Angiotensin i-converting enzyme in the nephron [16].
• Peptidyldipeptide hydrolase [angiotensin I-converting enzyme, EC 3.4.15.1] was inhibited by inorganic and organic phosphorus compounds tested, except for beta-glycerophosphate, 5'-AMP, and 5'-ADP, at the reagent concentrations used [17].

Analytical, diagnostic and therapeutic context of ACE

• Purification and analysis of lung and plasma angiotensin I-converting enzyme by high-performance liquid chromatography [18].

References