The central role of angiotensin I-converting enzyme in vertebrate pathophysiology.
Identifieur interne : 000222 ( Psycho/Analysis ); précédent : 000221; suivant : 000223The central role of angiotensin I-converting enzyme in vertebrate pathophysiology.
Auteurs : David W. Moskowitz [États-Unis] ; Frank E. JohnsonSource :
- Current topics in medicinal chemistry [ 1568-0266 ] ; 2004.
Descripteurs français
- KwdFr :
- Adulte, Adulte d'âge moyen, Animaux, Antagonistes du récepteur de type 1 de l'angiotensine-II, Conformation des protéines, Génotype, Humains, Inhibiteurs de l'enzyme de conversion de l'angiotensine (), Inhibiteurs de l'enzyme de conversion de l'angiotensine (pharmacologie), Modèles moléculaires, Mâle, Peptidyl-Dipeptidase A (), Peptidyl-Dipeptidase A (génétique), Peptidyl-Dipeptidase A (physiologie), Spermatozoïdes (enzymologie), Testicule (enzymologie), Vertébrés (physiologie).
- MESH :
- enzymologie : Spermatozoïdes, Testicule.
- génétique : Peptidyl-Dipeptidase A.
- pharmacologie : Inhibiteurs de l'enzyme de conversion de l'angiotensine.
- physiologie : Peptidyl-Dipeptidase A, Vertébrés.
- Adulte, Adulte d'âge moyen, Animaux, Antagonistes du récepteur de type 1 de l'angiotensine-II, Conformation des protéines, Génotype, Humains, Inhibiteurs de l'enzyme de conversion de l'angiotensine, Modèles moléculaires, Mâle, Peptidyl-Dipeptidase A.
English descriptors
- KwdEn :
- Adult, Angiotensin II Type 1 Receptor Blockers, Angiotensin-Converting Enzyme Inhibitors (chemistry), Angiotensin-Converting Enzyme Inhibitors (pharmacology), Animals, Genotype, Humans, Male, Middle Aged, Models, Molecular, Peptidyl-Dipeptidase A (chemistry), Peptidyl-Dipeptidase A (genetics), Peptidyl-Dipeptidase A (physiology), Protein Conformation, Spermatozoa (enzymology), Testis (enzymology), Vertebrates (physiology).
- MESH :
- chemical , chemistry : Angiotensin-Converting Enzyme Inhibitors, Peptidyl-Dipeptidase A.
- chemical , genetics : Peptidyl-Dipeptidase A.
- chemical , pharmacology : Angiotensin-Converting Enzyme Inhibitors.
- chemical , physiology : Peptidyl-Dipeptidase A.
- chemical : Angiotensin II Type 1 Receptor Blockers.
- enzymology : Spermatozoa, Testis.
- physiology : Vertebrates.
- Adult, Animals, Genotype, Humans, Male, Middle Aged, Models, Molecular, Protein Conformation.
Abstract
Genomic epidemiologic data, increasingly supported by clinical outcomes results, strongly suggest that overactivity of angiotensin I-converting enzyme (ACE) may underlie most age-related diseases. Angiotensin II, the main product of ACE, is a pleiotropic hormone, capable of serving as a neurotransmitter, growth factor, angiogenesis factor, vasoconstrictor, pro-thrombotic agent, and cytokine. So it is perhaps not surprising that the ACE D/D genotype is associated with several major psychiatric diseases, most cancers except prostate cancer (where the D/D genotype is actually protective), most cardiovascular diseases, most autoimmune diseases, and even infectious diseases like tuberculosis and HIV. In a preliminary study, angiotensin II blockade appeared to hasten recovery from West Nile virus encephalitis; it may be equally useful in SARS. The ACE gene underwent duplication at the origin of Chordata, just before the "Cambrian Explosion" in the number of species. The ancestral, unduplicated form of ACE is still expressed during the terminal differentiation of human spermatocytes, suggesting a critical role in reproduction. The crystal structure of testicular ACE (tACE) was recently published. Computer modeling suggests that tACE may be activated by both mechanical forces and reducing agents. The duplicated form of ACE (somatic ACE, sACE) is expressed in areas of high fluid flow. sACE may auto-dimerize via a novel protein motif, the "disulfide zipper." The sACE dimer is predicted to have higher catalytic efficiency and redox resistance than tACE.
DOI: 10.2174/1568026043387818
PubMed: 15379656
Affiliations:
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pubmed:15379656Le document en format XML
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Angiotensin II, the main product of ACE, is a pleiotropic hormone, capable of serving as a neurotransmitter, growth factor, angiogenesis factor, vasoconstrictor, pro-thrombotic agent, and cytokine. So it is perhaps not surprising that the ACE D/D genotype is associated with several major psychiatric diseases, most cancers except prostate cancer (where the D/D genotype is actually protective), most cardiovascular diseases, most autoimmune diseases, and even infectious diseases like tuberculosis and HIV. In a preliminary study, angiotensin II blockade appeared to hasten recovery from West Nile virus encephalitis; it may be equally useful in SARS. The ACE gene underwent duplication at the origin of Chordata, just before the "Cambrian Explosion" in the number of species. The ancestral, unduplicated form of ACE is still expressed during the terminal differentiation of human spermatocytes, suggesting a critical role in reproduction. The crystal structure of testicular ACE (tACE) was recently published. Computer modeling suggests that tACE may be activated by both mechanical forces and reducing agents. The duplicated form of ACE (somatic ACE, sACE) is expressed in areas of high fluid flow. sACE may auto-dimerize via a novel protein motif, the "disulfide zipper." The sACE dimer is predicted to have higher catalytic efficiency and redox resistance than tACE.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Missouri (État)</li></region></list><tree><noCountry><name sortKey="Johnson, Frank E" sort="Johnson, Frank E" uniqKey="Johnson F" first="Frank E" last="Johnson">Frank E. Johnson</name></noCountry><country name="États-Unis"><region name="Missouri (État)"><name sortKey="Moskowitz, David W" sort="Moskowitz, David W" uniqKey="Moskowitz D" first="David W" last="Moskowitz">David W. 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