ACE-like hydrolysis of gastrin analogs and CCK-8 by fundic mucosal cells of different species with release of the amidated C-terminal dipeptide
Dubreuil, P. ; Fulcrand, P. ; Rodriguez, M. ; Laur, J. ; Bali, J.-P. ; Martinez, J.
Amsterdam : Elsevier
Amsterdam : Elsevier
| ISSN: |
0167-4838
|
|---|---|
| Keywords: |
Angiotensin converting enzyme ; Gastric mucosal cell ; Gastrin ; Gastrin antagonist
|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
|
| Topics: |
Biology
Chemistry and Pharmacology
Medicine
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798291641242484736 |
|---|---|
| autor | Dubreuil, P. Fulcrand, P. Rodriguez, M. Laur, J. Bali, J.-P. Martinez, J. |
| autorsonst | Dubreuil, P. Fulcrand, P. Rodriguez, M. Laur, J. Bali, J.-P. Martinez, J. |
| book_url | http://linkinghub.elsevier.com/retrieve/pii/0167-4838(90)90182-F |
| datenlieferant | nat_lic_papers |
| fussnote | Various gastrin analogues and CCK-8 (Asp-Tyr(SO"3H)-Met-Gly-Trp-Met-Asp-Phe-NH"2) are hydrolyzed in vitro by angiotensin-converting enzyme (ACE), the main and initial cleavage occuring at the Met-Asp (or Leu-Asp) bond, releasing the C-terminal dipeptide amide Asp-Phe-NH"2. Tetragastrin analogues (e.g., Boc-Trp-Leu-Asp-Phe-NH"2) are degraded by a vesicular membrane fraction from rat gastric mucosa, yielding the C-terminal dipeptide Asp-Phe-NH"2. We report here on the degradation of gastrin analogues and CCK-8 by a gastric mucosal cell preparation containing specific gastrin receptors. We have shown that gastrin analogues were specifically degraded by gastric mucosal cells from different species (e.g., rabbit and dog) at 37^oC (pH 7.4), releasing the C-terminal dipeptide Asp-Phe-NH"2, similarly to ACE. This cleavage was found to be temperature and pH sensitive, and was inhibited by metalloproteinase inhibitors and by captopril, strongly suggesting that this enzymatic system closely resembles ACE. We have also demonstrated that a close correlation seems to exist between the apparent affinity of the gastrin analogues for gastrin receptors on gastric mucosal cells, and their ability of being hydrolyzed by this cell preparation. Moreover, all gastrin analogues which have been demonstrated to act as gastrin antagonists remained unaffected in the incubation conditions. |
| hauptsatz | hsatz_simple |
| identnr | NLZ186832141 |
| issn | 0167-4838 |
| journal_name | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 1039 (1990), S. 171-176 |
| schlagwort | Angiotensin converting enzyme Gastric mucosal cell Gastrin Gastrin antagonist |
| search_space | articles |
| shingle_author_1 | Dubreuil, P. Fulcrand, P. Rodriguez, M. Laur, J. Bali, J.-P. Martinez, J. |
| shingle_author_2 | Dubreuil, P. Fulcrand, P. Rodriguez, M. Laur, J. Bali, J.-P. Martinez, J. |
| shingle_author_3 | Dubreuil, P. Fulcrand, P. Rodriguez, M. Laur, J. Bali, J.-P. Martinez, J. |
| shingle_author_4 | Dubreuil, P. Fulcrand, P. Rodriguez, M. Laur, J. Bali, J.-P. Martinez, J. |
| shingle_catch_all_1 | Dubreuil, P. Fulcrand, P. Rodriguez, M. Laur, J. Bali, J.-P. Martinez, J. ACE-like hydrolysis of gastrin analogs and CCK-8 by fundic mucosal cells of different species with release of the amidated C-terminal dipeptide Angiotensin converting enzyme Gastric mucosal cell Gastrin Gastrin antagonist Angiotensin converting enzyme Gastric mucosal cell Gastrin Gastrin antagonist 0167-4838 01674838 Elsevier |
| shingle_catch_all_2 | Dubreuil, P. Fulcrand, P. Rodriguez, M. Laur, J. Bali, J.-P. Martinez, J. ACE-like hydrolysis of gastrin analogs and CCK-8 by fundic mucosal cells of different species with release of the amidated C-terminal dipeptide Angiotensin converting enzyme Gastric mucosal cell Gastrin Gastrin antagonist Angiotensin converting enzyme Gastric mucosal cell Gastrin Gastrin antagonist 0167-4838 01674838 Elsevier |
| shingle_catch_all_3 | Dubreuil, P. Fulcrand, P. Rodriguez, M. Laur, J. Bali, J.-P. Martinez, J. ACE-like hydrolysis of gastrin analogs and CCK-8 by fundic mucosal cells of different species with release of the amidated C-terminal dipeptide Angiotensin converting enzyme Gastric mucosal cell Gastrin Gastrin antagonist Angiotensin converting enzyme Gastric mucosal cell Gastrin Gastrin antagonist 0167-4838 01674838 Elsevier |
| shingle_catch_all_4 | Dubreuil, P. Fulcrand, P. Rodriguez, M. Laur, J. Bali, J.-P. Martinez, J. ACE-like hydrolysis of gastrin analogs and CCK-8 by fundic mucosal cells of different species with release of the amidated C-terminal dipeptide Angiotensin converting enzyme Gastric mucosal cell Gastrin Gastrin antagonist Angiotensin converting enzyme Gastric mucosal cell Gastrin Gastrin antagonist 0167-4838 01674838 Elsevier |
| shingle_title_1 | ACE-like hydrolysis of gastrin analogs and CCK-8 by fundic mucosal cells of different species with release of the amidated C-terminal dipeptide |
| shingle_title_2 | ACE-like hydrolysis of gastrin analogs and CCK-8 by fundic mucosal cells of different species with release of the amidated C-terminal dipeptide |
| shingle_title_3 | ACE-like hydrolysis of gastrin analogs and CCK-8 by fundic mucosal cells of different species with release of the amidated C-terminal dipeptide |
| shingle_title_4 | ACE-like hydrolysis of gastrin analogs and CCK-8 by fundic mucosal cells of different species with release of the amidated C-terminal dipeptide |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:35:51.489Z |
| titel | ACE-like hydrolysis of gastrin analogs and CCK-8 by fundic mucosal cells of different species with release of the amidated C-terminal dipeptide |
| titel_suche | ACE-like hydrolysis of gastrin analogs and CCK-8 by fundic mucosal cells of different species with release of the amidated C-terminal dipeptide Various gastrin analogues and CCK-8 (Asp-Tyr(SO"3H)-Met-Gly-Trp-Met-Asp-Phe-NH"2) are hydrolyzed in vitro by angiotensin-converting enzyme (ACE), the main and initial cleavage occuring at the Met-Asp (or Leu-Asp) bond, releasing the C-terminal dipeptide amide Asp-Phe-NH"2. Tetragastrin analogues (e.g., Boc-Trp-Leu-Asp-Phe-NH"2) are degraded by a vesicular membrane fraction from rat gastric mucosa, yielding the C-terminal dipeptide Asp-Phe-NH"2. We report here on the degradation of gastrin analogues and CCK-8 by a gastric mucosal cell preparation containing specific gastrin receptors. We have shown that gastrin analogues were specifically degraded by gastric mucosal cells from different species (e.g., rabbit and dog) at 37^oC (pH 7.4), releasing the C-terminal dipeptide Asp-Phe-NH"2, similarly to ACE. This cleavage was found to be temperature and pH sensitive, and was inhibited by metalloproteinase inhibitors and by captopril, strongly suggesting that this enzymatic system closely resembles ACE. We have also demonstrated that a close correlation seems to exist between the apparent affinity of the gastrin analogues for gastrin receptors on gastric mucosal cells, and their ability of being hydrolyzed by this cell preparation. Moreover, all gastrin analogues which have been demonstrated to act as gastrin antagonists remained unaffected in the incubation conditions. |
| topic | W V WW-YZ |
| uid | nat_lic_papers_NLZ186832141 |