Plasma prokallikrein and kininogens in burned patients

Adam, Albert; Damas, Jacques; Albert, Adelin; Ers, P.; Marichi, Jacques; Calay, G; Laurent, Philippe

doi:10.1016/0049-3848(86)91699-3

Cited by 7 publications

(2 citation statements)

References 8 publications

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“…Using larger amounts of trypsin, further hydrolysis of the larger fragments has been observed before a significant amount of immunoreactive kinin is released. This result is in close agreement with that of Adam et al [20], who observed a decrease of the immunoreactivity of human low-M, kininogen upon trypsin treatment most probably resulting from the partial proteolysis of the kininogen heavy chain. Such a change of the immunoreactivity was not observed when tissue kallikrein was used as a kininogenase since this enzyme selectively cleaves human low- Whether or not the liberation of an inhibitory peptide from T kininogen as well as of a vasoactive peptide is of biological relevance remains questionable.…”

Section: Discussionsupporting

confidence: 82%

Relationship between the cysteine-proteinase-inhibitory function of rat T kininogen and the release of immunoreactive kinin upon trypsin treatment

et al. 1986

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The potential kininogenic function of rat T kininogen has been studied in parallel with the cysteine-proteinaseinhibitory function also carried by this molecule. Proteolytic cleavage of the molecule was observed upon incubation with catalytic amounts of trypsin. These conditions do not permit any significant release of immunoreactive kinin and do not modify the total papain-inhibiting capacity of T kininogen. As trypsin concentration increases in the reaction mixture, immunoreactive kinin is liberated and the total papain-inhibiting capacity decreases accordingly, as indicated by titration studies. This decrease, however, does not exceed 50% of the initial value even at a trypsin concentration as high as 75 pM, indicating that only one of the two inhibitory sites has been inactivated. The remaining inhibitory fragment corresponds to a peptide of apparent M , 24000, which binds papain at least as well as native T kininogen.T kininogen, therefore, appears as a potent proteinase inhibitor and/or a proteinase inhibitor precursor, whereas its kininogenic function remains questionable since no specific kininogenase able to release T kinin or another kinin under physiologically compatible conditions has been found so far. In addition to its potential function as kinin precursor, T kininogen as well as other kininogens is a potent cysteine proteinase inhibitor identical with the previously reported u1 cysteine proteinase inhibitor [lo]. At variance with other kininogens, however, T kininogen also behaves as a typical acute-phase reactant since its concentration may be increased by 5-10 during an inflammatory state [lo].

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Section: Discussionsupporting

confidence: 82%

Relationship between the cysteine-proteinase-inhibitory function of rat T kininogen and the release of immunoreactive kinin upon trypsin treatment

et al. 1986

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“…The N-terminal heavy chain of 371 amino acids contains four apple domains whose homologues are also found in factor XI (FXI); whereas, the C-terminal light chain forms the catalytic domain[27]. Plasma prekallikrein associates with high molecular weight kininogen (HK), an α-globulin which circulates in plasma as an 88- to 120-kDa single-chain glycoprotein at a concentration of 70 to 90 μg/mL[28]. …”

Section: Synthesis and Stucture Of The Kksmentioning

confidence: 99%

Human Plasma Kallikrein-Kinin System: Physiological and Biochemical Parameters

Bryant

Shariat‐Madar²

2009

CHAMC

116

100

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The plasma kallikrein-kinin system (KKS) plays a critical role in human physiology. The KKS encompasses coagulation factor XII (FXII), the complex of prekallikrein (PK) and high molecular weight kininogen (HK). The conversion of plasma to kallikrein by the activated FXII and in response to numerous different stimuli leads to the generation of bradykinin (BK) and activated HK (HKa, an antiangiogenic peptide). BK is a proinflammatory peptide, a pain mediator and potent vasodilator, leading to robust accumulation of fluid in the interstitium. Systemic production of BK, HKa with the interplay between BK bound-BK receptors and the soluble form of HKa are key to angiogenesis and hemodynamics. KKS has been implicated in the pathogenesis of inflammation, hypertension, endotoxemia, and coagulopathy. In all these cases increased BK levels is the hallmark. In some cases, the persistent production of BK due to the deficiency of the blood protein C1-inhibitor, which controls FXII, is detrimental to the survival of the patients with hereditary angioedema (HAE). In others, the inability of angiotensin converting enzyme (ACE) to degrade BK leads to elevated BK levels and edema in patients on ACE inhibitors. Thus, the mechanisms that interfere with BK liberation or degradation would lead to blood pressure dysfunction. In contrast, anti-kallikrein treatment could have adverse effects in hemodynamic changes induced by vasoconstrictor agents. Genetic models of kallikrein deficiency are needed to evaluate the quantitative role of kallikrein and to validate whether strategies designed to activate or inhibit kallikrein may be important for regulating whole-body BK sensitivity.

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