title: Angiotensin converting enzyme-like activity in tissues from the river lamprey or lampern, Lampetra fluviatilis, acclimated to freshwater and seawater.
abstract: 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.
authors.affiliation: School of Biological Sciences, Hatherly Laboratories, University of Exeter, UK. c.s.cobb@exeter.ac.uk
authors.forename: Christopher S
authors.initials: CS
authors.lastname: Cobb
authors.forename: Sue C
authors.initials: SC
authors.lastname: Frankling
authors.forename: J Clifford
authors.initials: JC
authors.lastname: Rankin
authors.forename: J Anne
authors.initials: JA
authors.lastname: Brown
mesh_terms: D000222:Adaptation, Physiological; D000818:Animals; D001921:Brain / Q000201:enzymology; D002216:Captopril / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005260:Female; D005618:Fresh Water; D005880:Gills / Q000201:enzymology; D007422:Intestines / Q000201:enzymology; D007798:Lampreys / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008297:Male; D018482:Muscle, Skeletal / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D012623:Seawater; D012867:Skin / Q000201:enzymology
chemical_list: D004791:Enzyme Inhibitors; D002216:Captopril; D007703:Peptidyl-Dipeptidase A