Comparative studies of plasma kinins: The kallikrein-kinin system in poikilotherm and other vertebrates

Dunn, Katrina; Perks, A. M.

doi:10.1016/0016-6480(75)90132-x

Cited by 21 publications

(10 citation statements)

References 17 publications

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“…While it may be true that canonical bradykinin is not present, the data presented here unequivocally demonstrate the presence of two, novel bradykinin-related peptides in a European bombinid toad. In addition, these data may provide an insight into the apparent absence of a circulating kallikrein-kinin system in anuran amphibians [17,18,23]. The high degree of primary structural variability of bradykinins in amphibian skin secretions, their differing spectra of bioactivity and the lack of information on bradykinin receptor subtypes and pharmacology in amphibians, may mean that, in the past, inappropriate bio-and/or immuno-assays have been employed to detect the endogenous circulatory kinins.…”

Section: Discussionmentioning

confidence: 99%

Novel bradykinins and their precursor cDNAs from European yellow‐bellied toad (Bombina variegata) skin

Chen

Orr

Bjourson

et al. 2002

European Journal of Biochemistry

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Two novel bradykinin-related peptides (Ala3,Thr6)-bradykinin and (Val1,Thr3,Thr6)-bradykinin, were identified by a systematic sequencing study of peptides in the defensive skin secretion of the yellow-bellied toad, Bombina variegata. These peptides are the first amphibian skin bradykinins to exhibit amino acid substitutions at the Pro3 position of the bradykinin nonapeptide. Previously reported bradykinins from other Bombina species were not detected. Respective precursor cDNAs, designated BVK-1 and BVK-2, respectively, were cloned from a skin library by 3¢-and 5¢-RACE reactions. BVK-1 contained an open-reading frame of 97 amino acids encoding a single copy of (Ala3,Thr6)-bradykinin and similarly, the open-reading frame of BVK-2 consisted of 96 amino acids encoding a single copy of (Val1,Thr3,Thr6)-bradykinin. Synthetic replicates of each novel bradykinin were found to be active on mammalian arterial and small intestinal smooth muscle preparations. The structural diversity of bradykinins in amphibian defensive skin secretions may be related to defence against specific predators.Keywords: amphibian; bradykinin; skin; precursor; cloning.The skins of anuran amphibians, in addition to mucous glands, contain highly specialized poison glands, which, in reaction to stress or attack, exude a complex noxious cocktail of biologically active molecules [1]. These secretions often contain a plethora of peptides among which bradykinin or structural variants have been identified [2][3][4][5].The kallikrein-kininogen system appears to be a common target for certain venom components of many invertebrates and vertebrates. Among snakes, venoms from members of the Crotalinae (pit vipers) contain low molecular mass peptides that inhibit angiotensin-converting enzyme -a major bradykinin inactivating protease -thus potentiating the activity of endogenous bradykinin [6]. These bradykinin-potentiating peptides were the leads in developing angiotensin-converting enzyme inhibitor drugs that are frontline pharmaceuticals in the treatment of hypertension.Peptides with angiotensin-converting enzyme inhibitory activity have also been isolated from scorpion venom [7,8]. Wasp venoms contain bradykinin-related peptides that are responsible for the reddening, oedema and intense pain associated with envenomation by these insects [9,10]. These molecular strategies appear to be related to either potentiation of the effects of endogenous bradykinin by inhibition of catabolic proteases (snakes and scorpions) or by local delivery of supraphysiological quantities of bradykinins (wasps and amphibians).Although canonical bradykinin (RPPGFSPFR) has been isolated from the European common frog (Rana temporaria), with a range of minor N-and C-terminally extended forms [11,12], other species of ranid frog have been found to contain structural variants. These include (Thr6)-bradykinin and (Thr6)-bradykinyl-IAPEIV in R. rugosa and (Val1, Thr6)-bradykinin and (Val1,Thr6)-bradykinyl-VAPAS in R. nigromaculata [13,14]. Additional structural variants such as phylloki...

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Section: Discussionmentioning

confidence: 99%

Novel bradykinins and their precursor cDNAs from European yellow‐bellied toad (Bombina variegata) skin

Chen

Orr

Bjourson

et al. 2002

European Journal of Biochemistry

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“…Birds lack the activator but snake, frog, and fish appear to lack prekallikrein and kininogen as well (SEKI et al, 1973). However, in another study, hog pancreatic kallikrein generated an oxytocic substance after addition to all of the above plasmas as well as in plasmas from the amphibians Arnphiurna tridaetylurn and Rana eatesbeiana and the teleost Salrno gairdnerii (DUNN and PERKS, 1975).…”

Section: Comparative Studies Of Plasma Kallikrein-kinin Systemsmentioning

confidence: 96%

Kinins in Nature

Pisano¹

1979

Bradykinin, Kallidin and Kallikrein

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“…Because ACE phylogenetically predates the evolution of the classic RAS, it has been hypothesized that other biomolecules, e.g., kinins, may have been the original substrates for ACE (Lipke and Olson 1988), a suggestion which is further evidenced by the fact that the Km of ACE for bradykinin is lower than for angiotensin (ANG) I (Ryan 1982). Recently, we (Lipke and Olson 1990;Lipke et al 1990a,b) provided the first evidence that all components of a KKS are present in trout, including: kallikrein-like enzymatic activity localized to gill and kidney tissue, a kallikrein substrate in trout plasma, an endogenous vasopressor substance (T60K, Lipke et al 1990a;Dunn and Perks 1975) formed by the action of glandular kallikrein on trout plasma, kinin receptors and kininase II activity.…”

Section: Introductionmentioning

confidence: 99%

“…Evidence indicating that fish possess a complete kallikrein-kinin system (KKS) was first suggested by Dunn and Perks (1975) who observed that mammalian pancreatic kallikrein generated a substance from heat-inactivated fish plasma which contracted uterine smooth muscle in a manner similar to bradykinin. Prior to this study, it was thought that elements of the KKS (except kininase activity) were not present in vertebrates more primitive than reptiles (Rabito et al 1972;Seki et al 1973).…”

Section: Introductionmentioning

confidence: 99%

A specific inhibitor of mammalian kallikrein, Phe-Phe-Arg-chloromethyl ketone, inhibits the production of vasoactive substances from trout plasma by kallikrein and blocks endogenous kallikrein-like activity in trout gills

Lipke

Olson

1992

Fish Physiol Biochem

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The cardiovascular effects of the kallikrein-kinin system (KKS) have not been completely characterized in lower vertebrates. In the present study, a specific, irreversible kallikrein inhibitor, Phe-Phe-Arg-chloromethyl ketone (PPACMK) was used to examine: 1. the role of the KKS in blood pressure regulation in vivo; 2. the nature of the pressor substance formed by the action of kallikrein on trout plasma in vivo and in vitro; and 3. the presence of kallikrein in trout gills and kidney. Dorsal aortic cannulated rainbow trout were used for in vivo blood pressure assays and two colorimetric serine-protease assays were used to examine tissue kallikrein activity. PPACMK alone had no effect on blood pressure in vivo. Pretreatment of porcine kallikrein with PPACMK inhibited the enzyme's pressor effect in trout by 80% and significantly attenuated the synthesis of vasopressor substance(s) from heat-treated trout plasma in vitro. Approximately 30% of gill serine protease activity was inhibited by pretreatment with PPACMK; no PPACMK-sensitive kallikrein activity was observed in the kidney. Salt water adaptation did not affect kallikrein-specific activity in the gill. These results show that the salmonid KKS does not appear to be involved in the regulation of systemic blood pressure. Further, the formation of pressor substances from trout plasma in vivo and in vitro is due to kallikrein activity and the peptides generated are similar. A kallikrein, similar to the mammalian enzyme, is found in trout gills, suggesting that the salmonid KKS may be a local mediator of gill function.

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Comparative studies of plasma kinins: The kallikrein-kinin system in poikilotherm and other vertebrates

Cited by 21 publications

References 17 publications

Novel bradykinins and their precursor cDNAs from European yellow‐bellied toad (Bombina variegata) skin

Novel bradykinins and their precursor cDNAs from European yellow‐bellied toad (Bombina variegata) skin

Kinins in Nature

A specific inhibitor of mammalian kallikrein, Phe-Phe-Arg-chloromethyl ketone, inhibits the production of vasoactive substances from trout plasma by kallikrein and blocks endogenous kallikrein-like activity in trout gills

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