scholarly journals Inhibition of Angiotensin - Converting Enzyme by a Synthetic Peptide Fragment of Glyceraldehyde-3-phosphate Dehydrogenase

2000 ◽  
Vol 55 (7-8) ◽  
pp. 657-660
Author(s):  
Ewa Seweryn ◽  
Artur Pędyczak ◽  
Teresa Banaś
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Angiotensin Converting Enzyme ◽  
Synthetic Peptide ◽  
Human Muscle ◽  
Converting Enzyme ◽  
Peptide Fragment ◽  
Rabbit Lung ◽  
Synthetic Peptide Fragment

Abstract A novel inhibitor of angiotensin - converting enzyme (ACE) identical to a sequence part of human muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was chemically synthesized. Amino acid sequence was as follows Pro - Glu - Asn - Ile - Lys - Trp - Gly - Asp. This peptide inhibited rabbit lung ACE with a K1 value of 1.6 μм. The inhibitor of ACE acts in a non-competitive manner. The amino acid sequence of the new inhibitor was com- pared of GAPDH from other sources.

scholarly journals Novel activity of angiotensin-converting enzyme. Hydrolysis of cholecystokinin and gastrin analogues with release of the amidated C-terminal dipeptide

1989 ◽  
Vol 262 (1) ◽  
pp. 125-130 ◽  
Author(s):  
P Dubreuil ◽  
P Fulcrand ◽  
M Rodriguez ◽  
H Fulcrand ◽  
J Laur ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Chloride Ion ◽  
Peptide Bond ◽  
Major Product ◽  
Enzyme Hydrolysis ◽  
Ion Concentration ◽  
Converting Enzyme ◽  
Rabbit Lung ◽  
Hydrolysis Of

ACE (angiotensin-converting enzyme; peptidyl dipeptidase A; EC 3.4.15.1), cleaves C-terminal dipeptides from active peptides containing a free C-terminus. We investigated the hydrolysis of cholecystokinin-8 [CCK-8; Asp-Tyr(SO3H)-Met-Gly-Trp-Met-Asp-Phe-NH2] and of various gastrin analogues by purified rabbit lung ACE. Although these peptides are amidated at their C-terminal end, they were metabolized by ACE to several peptide fragments. These fragments were analysed by h.p.l.c., isolated and identified by comparison with synthetic fragments, and by amino acid analysis. The initial and major site of hydrolysis was the penultimate peptide bond, which generated a major product, the C-terminal amidated dipeptide Asp-Phe-NH2. As a secondary cleavage, ACE subsequently released di- or tri-peptides from the C-terminal end of the remaining N-terminal fragments. The cleavage of CCK-8 and gastrin analogues was inhibited by ACE inhibitors (Captopril and EDTA), but not by other enzyme inhibitors (phosphoramidon, thiorphan, bestatin etc.). Hydrolysis of [Leu15]gastrin-(14-17)-peptide [Boc (t-butoxycarbonyl)-Trp-Leu-Asp-Phe-NH2] in the presence of ACE was found to be dependent on the chloride-ion concentration. Km values for the hydrolysis of CCK-8, [Leu15]gastrin-(11-17)-peptide and Boc-[Leu15]gastrin-(14-17)-peptide at an NaCl concentration of 300 mM were respectively 115, 420 and 3280 microM, and the catalytic constants were about 33, 115 and 885 min-1. The kcat/Km for the reactions at 37 degrees C was approx. 0.28 microM-1.min-1, which is approx. 35 times less than that reported for the cleavage of angiotensin I. These results suggest that ACE might be involved in the metabolism in vivo of CCK and gastrin short fragments.

The NH2-and COOH-terminal sequences of the angiotensin-converting enzyme isozymes from rabbit lung and testis

1982 ◽  
Vol 107 (3) ◽  
pp. 1097-1103 ◽  
Author(s):  
Kazushi Iwata ◽  
Chun-Yen Lai ◽  
Hamza A. El-Dorry ◽  
Richard L. Soffer
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Converting Enzyme ◽  
Rabbit Lung

Expression of the proto-oncogene fos (c-fos) by preimplantation blastocysts of the pig

Development ◽  
1989 ◽  
Vol 105 (3) ◽  
pp. 651-656
Author(s):  
A. Whyte ◽  
H.J. Stewart
Keyword(s):  
Synthetic Peptide ◽  
Expression Vector ◽  
Monolayer Culture ◽  
Peptide Fragment ◽  
Blastocyst Development ◽  
Thin Sections ◽  
Fos Protein ◽  
Rna Probes ◽  
Synthetic Peptide Fragment

Blastocyst material was obtained from 25 pigs during the period 10 to 33 days post coitum, and fixed thin sections of tissue were hybridized in situ to sense and antisense fos RNA probes synthesized using the expression vector Bluescribe M13. Indirect immunofluorescence using antisera to a synthetic peptide fragment of c-fos was used to confirm the tissue distribution of oncogene-encoded proteins, which were shown by immunoprecipitation to have Mrs of 55,000 and 40,000, which are the known Mrs of the fos gene product and an associated nucleoprotein, respectively. Northern and slot blots were used to assess the distribution of c-fos mRNA and the size of the fos transcript was found to be 2.3 kbases. C-fos was expressed in trophectoderm from blastocysts early in pregnancy but declined with increasing blastocyst development so that it was virtually absent by day 19 of gestation. High levels of fos proto-oncogene expression were, however, retained in the allantoic membranes up to at least day 19 of pregnancy. The expression of the fos protein could be prolonged in trophectodermal cells in monolayer culture by addition of conditioned medium from blastocysts cultured for 2 h, suggesting the presence of a growth-factor-like substance.

Plasmin-platelet interaction involves cleavage of functional thrombin receptor

1996 ◽  
Vol 271 (1) ◽  
pp. C54-C60 ◽  
Author(s):  
M. Kimura ◽  
T. T. Andersen ◽  
J. W. Fenton ◽  
W. F. Bahou ◽  
A. Aviv
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Platelet Activation ◽  
Synthetic Peptide ◽  
Time Dependent ◽  
Thrombin Receptor ◽  
Amino Acid Residues ◽  
Enzymatic Action ◽  
High Concentrations ◽  
Inhibition Of Thrombin

We tested the hypothesis that the inhibition of thrombin-induced platelet activation by plasmin is mediated via the enzymatic action of plasmin on the functional thrombin receptor. We monitored the binding of the anti-thrombin receptor antibody [anti-TR-(34-46)] to platelets; this binding is sensitive to the cleavage of the thrombin receptor at amino acid residues Arg-41 to Ser-42. Plasmin inhibited anti-TR-(34-46) binding in dose- and time-dependent manners. The inactive synthetic peptide with the amino acid sequence 40-55 of the thrombin receptor (D-FPRSFLLRNPNDKYEPF) was similarly cleaved by thrombin and plasmin to an active peptide (SFLLRNPNDKYEPF) that produced robust cytosolic Ca2+ responses. At high concentrations, plasmin itself can activate platelets. We explored this effect with the use of anti-TR-(1-160). This antibody abolished the cytosolic Ca2+ responses to thrombin and to the thrombin receptor-activating peptide SFLLRN but did not attenuate the plasmin-induced cytosolic Ca2+ response. Thus plasmin inhibits thrombin-evoked platelet activation by cleaving the thrombin receptor, but the plasmin-induced cytosolic Ca2+ response is not due to the generation of the tethered peptide of the thrombin receptor.

Angiotensin converting enzyme inhibitors: N-Substituted monocyclic and bicyclic amino acid derivatives

1983 ◽  
Vol 26 (9) ◽  
pp. 1267-1277 ◽  
Author(s):  
James L. Stanton ◽  
Norbert Gruenfeld ◽  
Joseph E. Babiarz ◽  
Michael H. Ackerman ◽  
Robert C. Friedmann ◽  
...  
Keyword(s):  
Amino Acid ◽  
Angiotensin Converting Enzyme ◽  
Enzyme Inhibitors ◽  
Angiotensin Converting Enzyme Inhibitors ◽  
Amino Acid Derivatives ◽  
Converting Enzyme ◽  
Converting Enzyme Inhibitors

scholarly journals A 193-Amino Acid Fragment of the SARS Coronavirus S Protein Efficiently Binds Angiotensin-converting Enzyme 2

2003 ◽  
Vol 279 (5) ◽  
pp. 3197-3201 ◽  
Author(s):  
Swee Kee Wong ◽  
Wenhui Li ◽  
Michael J. Moore ◽  
Hyeryun Choe ◽  
Michael Farzan
Keyword(s):  
Amino Acid ◽  
Angiotensin Converting Enzyme ◽  
Converting Enzyme ◽  
Sars Coronavirus ◽  
S Protein ◽  
Angiotensin Converting Enzyme 2 ◽  
Amino Acid Fragment ◽  
Acid Fragment
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