Angiotensin-converting enzyme in organs of air-breathing fish

Olson, Kenneth R.; Lipke, David W.; Munshi, J. S. Datta; Moitra, A.; Ghosh, T. K.; Kunwar, Gopal K.; Ahmad, Monir; Roy, P. K.; Singh, O.N.; Nasar, Sri S; Pandey, A.; Oduleye, S. O.; Kullman, D.

doi:10.1016/0016-6480(87)90088-8

Cited by 21 publications

(4 citation statements)

References 13 publications

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“…The inhibition of this activity by the kininase II inhibitor, captopril, indicates that this enzymatic activity resembles kininase II or an enzyme with similar properties. The kininase II-like activity was very similar to that observed in other teleosts ) and in some lungfish (Olson et al 1987;Masini et al 1996), and confirms the data observed in Antarctic teleosts (Uva et al 1991). In the present study, kininase II was measured at different temperatures.…”

Section: Discussionsupporting

confidence: 77%

Key enzymes of the kallikrein-kinin system in Antarctic teleosts

1997

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In this study, some of the mammalian kallikrein-kinin system (KKS)-like components were identified in two species of Antarctic notothenioid [Chionodraco hamatus (Channichthydae) and ¹remato-mus bernacchii (Nothothenidae)]. The kidney and heart were assayed for kallikrein-like activity using the synthetic substrate D-Val-Leu-Arg-paranitroanilide. Values expressed as nmol p-nitroanilide/mg proteins, were in C. hamatus 15.5$1.5 and 15.2$1.4 in kidney and heart, respectively, and 15.8$2.2 and 15.9$1 in kidney and heart of ¹. bernacchii. Kallikrein-like activity was inhibited by aprotinin and phenylmethylsulfonyl fluoride (PMSF). The assay was stable at 20°C. Kininase II-like activity was performed on kidney, gills and heart using the substrate hippuryl-L-histidyl-Lleucine. The activity was inhibited by captopril, and in kidney and gills by high temperatures (20°C and 37°C); in the heart the enzymatic activity was measurable also at 20°C. Bradykinin-like immunoreactive cells were localized by immunohistochemistry in the nephron, in the gills, and in the arterial walls of the heart. These results show that Antarctic teleosts possess elements comparable to those of the KKS, including kallikreinlike, and kininase II-like activities, and the end product of the enzymatic cascade, bradykinin. The enzymatic cascade appears to be fully active only at low temperatures.

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Section: Discussionsupporting

confidence: 77%

Key enzymes of the kallikrein-kinin system in Antarctic teleosts

1997

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“…The gill vasculature is situated in series with the entire systemic circulation and therefore is in an ideal position to affect the concentration of any biologically active molecule to which the systemic tissues might be exposed. It is becoming increasingly evident that, in addition to a large vascular surface area, gills possess enzymes capable of synthesizing or metabolizing a variety of hormones including angiotensin (Galardy et al, 1984;Olson et al, 1986Olson et al, , 1987, adenosine (Colin and Leray, 1979), eicosanoids (Piomelli, 1985;Van Pragg et al, 1987), and catecholamines (Nekvasil and Olson, 1986b). The ability of the gill to influence plasma catecholamines is especially important, as adrenergic activity is required by fish in their response to a variety of stressful stimuli.…”

Section: Discussionmentioning

confidence: 99%

Catecholamine metabolism by the perfused rainbow trout gill

Colletti

Olson

1988

J. Exp. Zool.

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The trout gill has the capacity to influence general adrenergic activity through extraction and metabolism of circulating catecholamines (CAI; (Nekvasil and Olson, Am. J. Physiol., 1986,250:R526-R531). To further examine the metabolic process, isolated gills were perfused with M and lo-" M norepinephrine (NEPI) or epinephrine (EPI) and effluent from the arterioarterial (AA) and arteriovenous (AV) pathways analyzed by high pressure liquid chromatography with electrochemical detection (HPLC-EC). After 20 minutes of continuous lo-' M NEPI perfusion, metabolites accounted for 70% and 96% of the total amines recovered in the AA and AV effluents, respectively. After 20 minutes of M EPI perfusion, 60% and 94% of the amines in the AA and AV effluents, respectively, were metabolites. Similar results were seen during perfusion with 10" M CAs. Dihydroxymandelic acid (DHMA) and vanillylmandelic acid (VMA) were the major metabolites identified in gill effluent. Gills perfused with a bolus of 3H-NEPI extracted 47% of the radiolabel. Continuous perfusion with 10" M cocaine or M tyramine 30 minutes after the 3H-NEPI pulse released 3H-labeled and -unlabeled NEPI and metabolites into the AA effluent. Cocaine released more unmetabolized 3H-NEPI than tyramine, whereas tyramine released more 3H-labeled metabolites than cocaine. These studies indicate that the gill efficiently inactivates CAs through metabolism and that the major products formed are deaminated (DHMA) and deaminated:O-methylated (VMA) metabolites. The gill is also able to remove NEPI from the perfusate and store it intact for up to 50 minutes. Branchial uptake of CAs in fish and pulmonary uptake of CAs in mammals appear to have basic similarities.

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“…With the possible exception of cyclostomes, renin or renin-like activities have been described in representatives of all vertebrate groups in addition to the eutherian mammals (fishes: 67,560,568,597,647; amphibians: 102, 340, 653; birds: 117, 912; marsupials: 746,802). The second enzyme of the cascade, angiotensin 1converting enzyme (kininase II), also has a widespread phylogenetic distribution from fish through representative amniotes (145,292,317,532,674,720,876). Several angiotensins have been sequenced, and there is significant homology among them (Table 10.34).…”

Section: The Kidneymentioning

confidence: 99%

Endocrinology of the Vertebrates

Henderson

1997

Comprehensive Physiology

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Angiotensin-converting enzyme in organs of air-breathing fish

Cited by 21 publications

References 13 publications

Key enzymes of the kallikrein-kinin system in Antarctic teleosts

Key enzymes of the kallikrein-kinin system in Antarctic teleosts

Catecholamine metabolism by the perfused rainbow trout gill

Endocrinology of the Vertebrates

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