Share This Author
An insertion/deletion polymorphism in the angiotensin I-converting enzyme gene accounting for half the variance of serum enzyme levels.
- B. Rigat, C. Hubert, F. Alhenc-Gelas, F. Cambien, P. Corvol, F. Soubrier
- BiologyThe Journal of clinical investigation
- 1 October 1990
The insertion/deletion polymorphism accounted for 47% of the total phenotypic variance of serum ACE, showing that the ACE gene locus is the major locus that determines serum ACE concentration.
Deletion polymorphism in the gene for angiotensin-converting enzyme is a potent risk factor for myocardial infarction
It is reported that the DD genotype, which is associated with higher levels of circulating ACE than the ID and II genotypes, is significantly more frequent in patients with myocardial infarction than in controls, especially among subjects with low body-mass index and low plasma levels of ApoB.
Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning.
- F. Soubrier, F. Alhenc-Gelas, P. Corvol
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 1 December 1988
The sequence of ACE reveals a high degree of internal homology between two large domains, suggesting that the molecule resulted from a gene duplication, and is consistent with the presence of a single gene for ACE in the haploid human genome.
The two homologous domains of human angiotensin I-converting enzyme are both catalytically active.
Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides.
The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors.
Angiotensin I-converting enzyme in human circulating mononuclear cells: genetic polymorphism of expression in T-lymphocytes.
- O. Costerousse, J. Allegrini, M. Lopez, F. Alhenc-Gelas
- BiologyThe Biochemical journal
- 15 February 1993
The results show that ACE is expressed in T-lymphocytes and indicate that the level of ACE expression in cells synthesizing the enzyme is genetically determined, which is highly reproducible and influenced by the polymorphism of the ACE gene.
Determination of Bradykinin B2 Receptor in Vivo Phosphorylation Sites and Their Role in Receptor Function*
Using metabolic32P labeling and phosphopeptide sequencing, a complete phosphorylation map of the human bradykinin B2receptor in its native cellular environment is provided and differential usage of clustered phosphoacceptor sites points to distinct roles of multiple kinases in controlling G protein-coupled receptor function.
Plasma Level and Gene Polymorphism of Angiotensin‐Converting Enzyme in Relation to Myocardial Infarction
It is indicated that plasma ACE level may be a risk factor for MI, independent of the ACE I/D polymorphism, as measured from frozen aliquots of plasma in a large subsample of the ECTIM study.
Contribution of genetic polymorphism in the renin-angiotensin system to the development of renal complications in insulin-dependent diabetes: Genetique de la Nephropathie Diabetique (GENEDIAB) study…
- M. Marre, X. Jeunemaître, F. Alhenc-Gelas
- Medicine, BiologyThe Journal of clinical investigation
- 1 April 1997
Genetic determinants that affect renal angiotensin II and kinin productions are risk factors for the progression of glomerular disease in uncontrolled insulin-dependent diabetic patients.