| Angiotensin converting enzyme-like activity in tissues from the river lamprey or lampern, Lampetra fluviatilis, acclimated to freshwater and seawater. | |
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MedLine Citation:
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PMID: 12161196 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Angiotensin converting enzyme (ACE) or kininase II is a dipeptidyl-carboxypeptidase that converts angiotensin I (Ang I) to angiotensin II (Ang II) in the renin-angiotensin system (RAS) and inactivates bradykinin in the kallikrein-kinin system (KKS). Angiotensin converting enzyme-like activity (ACELA) has been demonstrated in a wide range of vertebrates, and only in lampreys is a lack of ACELA still suggested. Though long controversial, a lamprey RAS has recently been identified by isolation and sequencing of lamprey Ang I and the measurement of circulating plasma angiotensins. We therefore re-investigated the presence of ACE in tissues from the river lamprey or lampern, Lampetra fluviatilis, using a highly sensitive fluorimetric assay. Significant detection of ACELA was found in a wide range of lamprey tissues (brain, gill, gonad, gut, heart, liver, skeletal muscle, skin, kidney, and plasma). The mammalian ACE inhibitor captopril at 10(-5)M was an effective, but variable inhibitor of the ACELA found in most lamprey tissues. The brain contained the highest ACELA, while kidney (including urinary duct), skin, gonads, and heart only contained very low ACELA. In most tissues, ACELA was similar in lampreys acclimated to freshwater (FW) and seawater (SW). However, gut ACELA was significantly higher in lampreys acclimated to SW than in FW-acclimated lampreys. Liver, skin, and gonad ACELA was significantly lower in lampreys acclimated to SW than in FW lampreys. Male and female lampreys acclimated to FW showed similar ACELA in all tissues except the kidney (including the urinary duct), where ACELA was significantly higher in male than in female lampreys. These results indicate that ACELA, a component of the RAS and KKS, is present in tissues from one of the earliest evolved groups of vertebrates. |
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Authors:
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Christopher S Cobb; Sue C Frankling; J Clifford Rankin; J Anne Brown |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: General and comparative endocrinology Volume: 127 ISSN: 0016-6480 ISO Abbreviation: Gen. Comp. Endocrinol. Publication Date: 2002 Jun |
Date Detail:
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Created Date: 2002-08-05 Completed Date: 2003-02-13 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0370735 Medline TA: Gen Comp Endocrinol Country: United States |
Other Details:
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Languages: eng Pagination: 8-15 Citation Subset: IM |
Affiliation:
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School of Biological Sciences, Hatherly Laboratories, University of Exeter, UK. c.s.cobb@exeter.ac.uk |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adaptation, Physiological* Animals Brain / enzymology Captopril / pharmacology Enzyme Inhibitors / pharmacology Female Fresh Water* Gills / enzymology Intestines / enzymology Lampreys / metabolism* Liver / enzymology Male Muscle, Skeletal / enzymology Myocardium / enzymology Peptidyl-Dipeptidase A / metabolism* Seawater* Skin / enzymology |
| Chemical | |
Reg. No./Substance:
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0/Enzyme Inhibitors; 62571-86-2/Captopril; EC 3.4.15.1/Peptidyl-Dipeptidase A |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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