Angiotensin I-converting enzyme and metabolism of the haematological peptide N-acetyl-seryl-aspartyl-lysyl-proline

Clinical and Experimental Pharmacology and Physiology

Volumn 28, Issue 12, 2001, Pages 1066-1069

  Azizi, Michel ^a,c   Junot, Christophe ^b   Ezan, Eric ^b   Ménard, Joël ^a  

^a HÔPITAL EUROPÉEN GEORGES POMPIDOU   (France)

^b Institut National de la Recherche Agronomique   (France)

^c Centre d'Investigations Cliniques   (France)

Author keywords

Angiotensin converting enzyme inhibitor; Haematopoiesis; Metabolism; N acetyl seryl aspartyl lysyl proline; Oligo peptides; Peptidyl dipeptidase A

Indexed keywords

ANGIOTENSIN I; CAPTOPRIL; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; LISINOPRIL; RXP 407; SERASPENIDE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; CARBOXY TERMINAL SEQUENCE; CELL CYCLE S PHASE; CONFERENCE PAPER; CONTROLLED STUDY; DOSE RESPONSE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SUBSTRATE; GLOMERULUS FILTRATION; HEMATOPOIETIC STEM CELL; HUMAN; HYPERTENSION; MOUSE; NONHUMAN; ORGAN DISTRIBUTION; PROTEIN BLOOD LEVEL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN METABOLISM; PROTEIN URINE LEVEL; RAT; REGULATORY MECHANISM; STEM CELL;

ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANIMALS; HUMANS; HYDROLYSIS; HYPERTENSION; MICE; OLIGOPEPTIDES; PEPTIDYL-DIPEPTIDASE A; PROTEIN STRUCTURE, TERTIARY; RATS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 0035684284     PISSN: 03051870     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1440-1681.2001.03560.x     Document Type: Conference Paper

References (39)

1. Inhibitor of hematopoietic pluripotent stem cell proliferation: Purification and determination of its structure
2. + subpopulations in response to growth factors
3. The mechanism of action of the tetrapeptide acetyl-N-Ser-Asp-Lys-Pro (AcSDKP) in the control of haematopoietic stem cell proliferation
4. Involvement of thymosin beta 4 and endoproteinase Asp-N in the biosynthesis of the tetrapeptide AcSerAspLysPro a regulator of the hematopoietic system
5. AcSDKP, an inhibitor of CFU-S proliferation, is synthesized in mice under steady-state conditions and secreted by bone marrow in long-term culture
6. Negative regulator of pluripotent hematopoietic stem cell proliferation in human white blood cells and plasma as analysed by enzyme immunoassay
7. Distribution of a negative regulator of haematopoietic stem cell proliferation (AcSDKP) and thymosin β4 in mouse tissues
8. Amelioration of chemotherapy-induced toxicity by cotreatment with AcSDKP, a tetrapeptide inhibitor of hematopoietic stem cell proliferation
9. In vivo effect of the tetrapeptide, N-acetyl-Ser-Asp-Lys-Pro on the G1-S transition of rat hepatocytes
10. Acetyl-seryl-aspartyl-lysyl-proline is a novel natural cell cycle regulator of renal cells
11. Effect of N-acetyl-seryl-aspartyl-lysyl-proline on DNA and collagen synthesis in rat cardiac fibroblasts
12. Antifibrotic effects of N-acetyl-seryl-aspartyl-lysyl-proline on the heart and kidney in aldosterone-salt hypertensive rats
13. The tetrapeptide acetyl-N-Ser-Asp-Lys-Pro (goralatide) protects from doxorubicin-induced toxicity: Improvement in mice survival and protection of bone marrow stem cells and progenitors
14. In vivo protective effects of tetrapeptide AcSDKP, with or without granulocyte colony-stimulation factor, on murine progenitor cells after sublethal irradiation
15. Séraspénide (acétyl SDKP): Étude en phase I-II d'un inhibiteur de l'hématopoièse la protégeant de la toxicité de monochimiothérapies aracytine et ifosfamide
16. The two homologous domains of human angiotensin I-converting enzyme are both catalytically active
17. The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme
18. Involvement of human plasma angiotensin I-converting enzyme in the degradation of the haemoregulatory peptide N-acetyl seryl aspartyl lysyl proline
19. 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
20. The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors
21. Substrate dependence of angiotensin I-converting enzyme inhibition: Captopril displays a partial selectivity for inhibition of N-acetyl-seryl-aspartyl-lysyl-proline hydrolysis compared with that of angiotensin I
22. N-Domain-specific substrate and C-domain inhibitors of angiotensin-converting enzyme: Angiotensin-(1-7) and keto-ACE
23. Differences in the hydrolysis of enkephalin congeners by the two domains of angiotensin converting enzyme
24. Acute angiotensin-converting enzyme inhibition increases the plasma level of the natural stem cell regulator N-acetyl-seryl-aspartyl-lysyl-proline
25. High plasma level of acetyl-seryl-aspartyl-lysyl-proline: A new marker of chronic angiotensin-converting enzyme inhibition
26. Renal and metabolic clearance of AcSDKP during angiotensin converting enzyme inhibition in humans
27. Pharmacokinetics in healthy volunteers and patients of NAc-SDKP (seraspenide), a negative regulator of hematopoiesis
28. Angiotensin I converting enzyme and the changes in our concepts through the years
29. Effect of angiotensin-converting enzyme inhibition on plasma, urine, and tissue concentrations of hemoregulatory peptide acetyl-Ser-Asp-Lys-Pro in rats
30. Captopril reduces collagen and mast cell accumulation in irradiated rat lung
31. Captopril inhibits proliferation of human lung fibroblasts in culture: A potential antifibrotic mechanism
32. Value of different clinical and biochemical correlates to assess angiotensin converting enzyme inhibition
33. Measurement of converting enzyme activity by antibody-trapping of generated angiotensin II. Comparison with two other methods
34. Nonadherence with angiotensin-converting enzyme inhibitor therapy: A comparison of different ways of measuring it in patients with chronic heart failure
35. In vitro and in vivo inhibition of the 2 active sites of ACE by omapatrilat, a vasopeptidase inhibitor
36. In vivo assessment of captopril selectivity of angiotensin I-converting enzyme inhibition: Differential inhibition of acetyl-ser-asp-lys-pro and angiotensin I hydrolysis
37. RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites
38. RXP 407, a selective inhibitor of the N-domain of angiotensin I-converting enzyme, blocks in vivo the degradation of hemoregulatory peptide acetyl-Ser-Asp-Lys-Pro with no effect on angiotensin I hydrolysis
39. Lisinopril, an angiotensin I-converting enzyme inhbitor, prevents in vivo the entry into cell cycle of murine hematopoietic stem cells following irradiation