Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.15.1 (ACE)
18,300 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Peptide inhibitors of angiotensin I-converting enzyme (peptidyldipeptide hydrolase, EC 3.4.15.1) were produced by digesting gelatin with bacterial collagenase. The inhibitors were isolated from the digests with a combination of alcohol fractionation, treatment with Amberlite CG-50 column, gel filtration through Sephadex G-25, and Dowex 50 column and paper chromatography. Nine peptide fractions were purified to apparent homogeneity judging by thin-layer and ion-exchange column chromatography, and amino acid composition. Amino acid sequences of the peptides were determined: 2 were found to be mixtures of peptides and the sequence of another was only partially determined. Six of the peptides were potent inhibitors of the converting enzyme, while the other three were less active. 6 peptides were substrates for the enzyme. The enzyme released a dipeptide, Ala-Hyp from one peptide and was strongly inhibited by this dipeptide. The remainder of the parent peptides was a less effective inhibitor.
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PMID:Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase. 21 31

Converting enzyme activity was studied in endothelial cells, isolated from pig pulmonary arteries and aorta by exposure to collagenase. The measure was based on the release of His-Leu from Z-Phe-His-Leu was related to the DNA content of the cellular suspension. The same activity was found in the two types of endothelium: 1 nmol His-Leu/mug DNA per 30 min. Subendothelial cells showed a very low activity, amounting to 10% of the value found for the endothelium. The enzyme activity was 2inhibited by the nonapeptide SQ 20881, EDTA, and the lack of Cl- in the same fashion for the two types of endothelium. The presence of another enzyme hydrolyzing His-Leu was detected in both endothelial populations. Isolated fragments of plasma membrane, however, exhibited only converting enzyme activity. It can be concluded that endothelial cells isolated from large vessels of the pulmonary and the systemic circulations have similar properties when dipeptidyl carboxypeptidase activity is measured.
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PMID:Converting enzyme activity in endothelial cells isolated from pig pulmonary artery and aorta. 40 22

Whereas mesangial and epithelial cells from glomeruli are commonly grown in vitro, there has been a failure to isolate and propagate human glomerular capillary endothelial cells. This study defines the conditions for the reproducible isolation and growth of homogeneous monolayers of primate (baboon and human) glomerular capillary endothelial cells. Using selective media and growth factors, the following criteria were identified to optimize the isolation and proliferation of glomerular endothelial cells: (1) collagenase treatment of isolated glomeruli; (2) requirement for 20% serum, endothelial cell growth factor and heparin; (3) requirement of fibronectin as surface matrix; and (4) isolation from donors less than 60 years old, as premature senescence was directly proportional to the age of the human kidney donor. Under these conditions, primary cultures with an endothelial cell composition greater than 70% were reproducibly obtained. Homogeneous endothelial monolayers were developed from 20 of 23 human kidneys, and maintained for 5 to 10 passages, depending on the age of the kidney donor. Purification to homogeneity was achieved by patch cloning or by fluorescence-activated cell sorting. Glomerular capillary endothelial cells exhibited a cobblestone morphology at confluence, expressed factor VIII-related antigen, angiotensin converting enzyme activity, and endocytosed acetylated low-density lipoproteins. Electron microscopy revealed the presence of intracellular Weibel-Palade bodies and caveolae and microvillous projections on the luminal surface. Glomerular cells also stained positive for Ulex europaeus, a lectin characteristic of human endothelial cells. In addition, preliminary results indicate that human glomerular endothelial cells increase intracellular cyGMP in response to alpha-human 5 to 28 atrial natriuretic peptide and intracellular free calcium in response to thrombin.
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PMID:Culture of endothelial cells from baboon and human glomeruli. 150 7

Dog, monkey and human aortic tissues contained two distinct types of angiotensin II-generating enzymes; angiotensin converting enzyme (ACE) and chymostatin-sensitive angiotensin II-generating enzyme (CAGE). Endothelium, media and adventitia of canine thoracic aortae were separated using collagenase digestion, and determined for their ACE and CAGE activity. ACE activity was assayed by hippuryl-His-Leu cleavage. CAGE activity was estimated with ANG I as substrate in the presence of inhibitors of ACE and angiotensinases. His-Leu, the common product of both enzyme reactions, was fluorimetrically quantified after o-phthalaldehyde condensation. ACE localized mainly in endothelium, while CAGE distributed predominantly in adventitia. Similar results were obtained with human and monkey aortae. Such a contrasting distribution may indicate the distinct functional role of these two enzymes.
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PMID:Different distribution of two types of angiotensin II-generating enzymes in the aortic wall. 282 56

Bronchoalveolar lavage fluid from 43 patients with biopsy proved sarcoidosis and 10 control subjects were assayed for fibronectin and collagenase activity. Fibronectin was significantly increased in the group with sarcoidosis and was found to be positively correlated with angiotensin converting enzyme activity, protein concentration, percentage of T cells and helper:suppressor ratios in the lavage fluid. Increased fibronectin in the bronchoalveolar lavage fluid was not related to functional or radiographic indices of interstitial disease and did not identify patients subsequently requiring treatment. Latent collagenase was present in bronchoalveolar lavage fluid from 16 patients with sarcoidosis but not in any control sample. There was no association between the collagenase activity and the cell profiles of the lavage fluid. Yet carbon monoxide transfer factor was decreased in patients with bronchoalveolar lavage fluid collagenase. Ten of 16 patients with bronchoalveolar lavage fluid collagenase had radiographic class III or IV disease and a disease duration of more than two years. On follow up 62% of patients with bronchoalveolar lavage fluid collagenase required subsequent treatment, compared with only 23% of patients without collagenase. These results indicate an association between bronchoalveolar lavage fluid collagenase and progressive, prolonged disease in sarcoidosis, whereas increased bronchoalveolar lavage fluid fibronectin is associated with indices of disease activity.
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PMID:Collagenase and fibronectin in bronchoalveolar lavage fluid in patients with sarcoidosis. 284 27

The amino-terminal amino acid sequence and several internal peptide sequences of angiotensin I-converting enzyme (ACE; peptidyl-dipeptidase A, kininase II; EC 3.4.15.1) purified from human kidney were used to design oligonucleotide probes. The nucleotide sequence of ACE mRNA was determined by molecular cloning of the DNA complementary to the human vascular endothelial cell ACE mRNA. The complete amino acid sequence deduced from the cDNA contains 1306 residues, beginning with a signal peptide of 29 amino acids. A highly hydrophobic sequence located near the carboxyl-terminal extremity of the molecule most likely constitutes the anchor to the plasma membrane. The sequence of ACE reveals a high degree of internal homology between two large domains, suggesting that the molecule resulted from a gene duplication. Each of these two domains contains short amino acid sequences identical to those located around critical residues of the active site of other metallopeptidases (thermolysin, neutral endopeptidase, and collagenase) and therefore bears a putative active site. Since earlier experiments suggested that a single Zn atom was bound per molecule of ACE, only one of the two domains should be catalytically active. The results of genomic DNA analysis with the cDNA probe are consistent with the presence of a single gene for ACE in the haploid human genome. Whereas the ACE gene is transcribed as a 4.3-kilobase mRNA in vascular endothelial cells, a 3.0-kilobase transcript was detected in the testis, where a shorter form of ACE is synthesized.
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PMID:Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. 284

N-[[[(5-chloro-2-benzothiazolyl)thiolphenyllacetyll-L-cysteine (WY-45,368) is a potent inhibitor of human skin fibroblast collagenase. Kinetic data show that the inhibition is competitive, with a Ki of 3.5 microM. WY-45,368 inhibits neither of two other metalloproteinases, thermolysin and angiotensin converting enzyme, nor does it inhibit clostridial collagenase--thus indicating specificity for mammalian collagenase.
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PMID:A novel inhibitor of mammalian collagenase. 299 88

A versatile, convenient assay for vertebrate collagenases has been developed using the fluorescent peptide substrate dansyl-Pro-Gln-Gly-Ile-Ala-Gly-D-Arg. This sequence resembles that of collagen at the site of cleavage but includes modifications designed to eliminate nonspecific hydrolysis by contaminating peptidases. Both human skin fibroblast and bovine corneal cell collagenases cleave the substrate specifically at the Gly-Ile bond. Plasmin, thrombin, trypsin, alpha-chymotrypsin, carboxypeptidase B, and bacterial collagenase do not cleave the substrate. Elastase and angiotensin converting enzyme display 20- and 400-fold less activity than the vertebrate collagenases, respectively, and cleave the peptide at different positions. The assay is performed by incubating a 5- to 25-microliters aliquot of trypsin-activated sample with an equal volume of 2 mM substrate overnight at 33 degrees C and pH 7.5. Thin-layer chromatography then separates the fluorescent product from the substrate in less than 20 min and allows the detection of subnanogram levels of collagenase. The assay is applicable to the screening of large numbers of samples under different conditions of pH and ionic strength and is readily adaptable for use in a variety of collagenase-dependent systems, such as assays for collagenase activating and/or inducing factors.
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PMID:A convenient fluorescent assay for vertebrate collagenases. 301 20

The clinical course of sarcoidosis is varying and unpredictable. Once the diagnosis has been made, the clinician needs simple tests to detect and predict remission or progression, to determine whether treatment is effective or not, and to assess the clinical activity of the disease. Sarcoidosis is a multisystem disease, but the lungs are almost always involved. Traditionally, the clinical management has therefore included chest X-rays and lung function studies. Extrapulmonary lesions have been followed in different ways. Sensitive and reproducible biochemical tests would be helpful in evaluating the clinical course of patients with sarcoidosis, if they measure functions related to the granulomatous inflammation. This review will deal with measurements of serum and urinary calcium, and 1,25-dihydroxyvitamin D. The usefulness of single and serial determinations of lysozyme, angiotensin converting enzyme, beta 2-microglobulin, collagenase, carboxypeptidase and glucuronidase in serum, bronchoalveolar lavage fluid, and other biological fluids will be discussed.
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PMID:Biochemical markers in sarcoidosis. 302 7

The distribution of kininases along microdissected nephron segments was studied. Single nephrons from collagenase treated rabbit kidney were microdissected and divided into following 9 segments: glomerulus; early proximal tubule; middle proximal tubule; late proximal tubule; cortical thick ascending limb; distal convoluted tubule; connecting tubule; cortical collecting tubule; medullary collecting tubule. Kininase activities in these nephron segments were measured with or without kininase II inhibitor. Kininase II and other peptidases were mainly localized in glomeruli and whole part of the proximal tubules.
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PMID:Distribution of kininase activity along the rabbit nephron. 303 11


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