Linked Life Data

2266130

Source:http://linkedlifedata.com/resource/pubmed/id/2266130

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
1991-2-14
pubmed:abstractText
Although angiotensin II (Ang II)-forming enzymatic activity in the human left cardiac ventricle is minimally inhibited by angiotensin I (Ang I) converting enzyme inhibitors, over 75% of this activity is inhibited by serine proteinase inhibitors (Urata, H., Healy, B., Stewart, R. W., Bumpus, F. M., and Husain, A. (1990) Circ. Res. 66, 883-890). We now report the identification and characterization of the major Ang II-forming, neutral serine proteinase, from left ventricular tissues of the human heart. A 115,150-fold purification from human cardiac membranes yielded a purified protein with an Mr of 30,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Based upon its amino-terminal sequence, the major human cardiac Ang II-forming proteinase appears to be a novel member of the chymase subfamily of chymotrypsin-like serine proteinases. Human heart chymase was completely inhibited by the serine proteinase inhibitors, soybean trypsin inhibitor, phenylmethylsulfonyl fluoride, and chymostatin. It was partially inhibited by p-tosyl-L-phenylalanine chloromethyl ketone, but was not inhibited by p-tosyl-L-lysine chloromethyl ketone, and aprotinin. Also, human heart chymase was not inhibited by inhibitors of the other three classes of proteinases. Human heart chymase has a high specificity for the conversion of Ang I to Ang II and the Ang I-carboxyl-terminal dipeptide His-Leu (Km = 60 microM; Kcat = 11,900 min-1; Kcat/Km = 198 min-1 microM-1). Human heart chymase did not degrade several peptide hormones, including Ang II, bradykinin, and vasoactive intestinal peptide, nor did it form Ang II from angiotensinogen. The high substrate specificity of human heart chymase for Ang I distinguishes it from other Ang II-forming enzymes including Ang I converting enzyme, tonin, kallikrein, cathepsin G, and other known chymases.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22348-57
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:2266130-Amino Acid Sequence, pubmed-meshheading:2266130-Angiotensin I, pubmed-meshheading:2266130-Angiotensin II, pubmed-meshheading:2266130-Animals, pubmed-meshheading:2266130-Chromatography, Affinity, pubmed-meshheading:2266130-Chromatography, Gel, pubmed-meshheading:2266130-Chromatography, High Pressure Liquid, pubmed-meshheading:2266130-Chymases, pubmed-meshheading:2266130-Endopeptidases, pubmed-meshheading:2266130-Heart Ventricles, pubmed-meshheading:2266130-Humans, pubmed-meshheading:2266130-Kinetics, pubmed-meshheading:2266130-Molecular Sequence Data, pubmed-meshheading:2266130-Molecular Weight, pubmed-meshheading:2266130-Myocardium, pubmed-meshheading:2266130-Neuropeptides, pubmed-meshheading:2266130-Peptides, pubmed-meshheading:2266130-Protease Inhibitors, pubmed-meshheading:2266130-Sequence Homology, Nucleic Acid, pubmed-meshheading:2266130-Serine Endopeptidases, pubmed-meshheading:2266130-Substrate Specificity
pubmed:year
1990
pubmed:articleTitle
Identification of a highly specific chymase as the major angiotensin II-forming enzyme in the human heart.
pubmed:affiliation
Department of Heart and Hypertension Research, Cleveland Clinic Foundation, Ohio 44195-5069.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't