Plasma kininogen content of toads, fowl and reptiles

Rabito, Sara F.; Binia, A; Segovia, Raul

doi:10.1016/0300-9629(72)90057-6

Cited by 17 publications

(9 citation statements)

References 7 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%

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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%

“…The use of standard activation procedures in a range of species generated no detectable bradykinin activity [17,18]. The apparent absence of a circulatory kininogen in this group of tetrapods poses a fundamental question as to the nature of the protein(s) responsible for the generation of bradykinins in anuran skin.…”

mentioning

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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“…As Harris et al Some authors speculate that BK and BRP are present in the skin of these tree frogs as they lack the kallikrein-kinin system (34,35), and/or that these peptides may act on and/or potentiate the endogenous BK action on the cardiovascular and/or gastrointestinal system of their predators, thus acting as defensive peptides (13,11).…”

Section: Discussionmentioning

confidence: 99%

Identification of bradykinin: related peptides from Phyllomedusa nordestina skin secretion using electrospray ionization tandem mass spectrometry after a single-step liquid chromatography

Conceição¹,

Bruni²,

Sciani³

et al. 2009

J. Venom. Anim. Toxins incl. Trop. Dis

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ABSTRACT:Amphibian skin secretions are a source of potential new drugs with medical and biotechnological applications. Rich in peptides produced by holocrinetype serous glands in the integument, these secretions play different roles, either in the regulation of physiological skin functions or in the defense against predators or microorganisms. The aim of the present work was to identify novel peptides with bradykinin-like structure and/or activity present in the skin of Phyllomedusa nordestina. In order to achieve this goal, the crude skin secretion of this frog was prefractionated by solid phase extraction and separated by reversed-phase chromatography. The fractions were screened for low-molecular-mass peptides and sequenced by mass spectrometry. It was possible to identify three novel bradykininrelated peptides, namely: KPLWRL-NH 2 (Pnor 3), RPLSWLPK (Pnor 5) and VPPKGVSM (Pnor 7) presenting vascular activities as assessed by intravital microscopy. Pnor 3 and Pnor 7 were able to induce vasodilation. On the other hand, Pnor 5 was a potent vasoconstrictor. These effects were reproduced by their synthetic analogues.

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“…In a seemingly conflicting report (RABITO et al, 1972), kininogen was found in the pigeon and turtle as observed by others but not in the toad, chicken, or turkey. An explanation for this discrepancy may lie in the fact that trypsin was used to generate the kinin from kininogen and that the kinin was assayed only by estimating its vasodilator effect on perfused dog leg.…”

Section: Comparative Studies Of Plasma Kallikrein-kinin Systemsmentioning

confidence: 73%

Kinins in Nature

Pisano¹

1979

Bradykinin, Kallidin and Kallikrein

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Plasma kininogen content of toads, fowl and reptiles

Cited by 17 publications

References 7 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

Identification of bradykinin: related peptides from Phyllomedusa nordestina skin secretion using electrospray ionization tandem mass spectrometry after a single-step liquid chromatography

Kinins in Nature

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