Isolation of two functionally different kininogens from human plasma—separation from proteinase inhibitors and interaction with plasma kallikrein

Habal, Flavio; Movat, Henry Z.; Burrowes, Clement E.

doi:10.1016/0006-2952(74)90558-9

Cited by 90 publications

(42 citation statements)

References 14 publications

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“…However, the importance of HMW kininogen in the coagulation process has been well documented (26)(27)(28)(29), although the specific in vivo functions of the various kininogens are otherwise unknown. In addition, Pierce and Guimaraes (10) as well as Habal et al (30) have corroborated earlier observations by Jacobsen and Kriz (31) that HMW kininogen is the preferred substrate for plasma kallikrein. These two observations are consistent with the predominant intravascular distribution of HMW kininogen, but do not shed further light on the relationship between distribution and function of the kininogens.…”

Section: Discussionsupporting

confidence: 84%

Turnover of human and monkey plasma kininogens in rhesus monkeys.

Yamada¹,

Wing²,

Pierce³

et al. 1979

J. Clin. Invest.

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A B S T R A C T The normal metabolic turnover of plasma kininogens was studied by measuring the disappearance of intravenously administered radiolabeled human and monkey plasma kininogens from the circulation of healthy adult rhesus monkeys. Curves obtained by plotting log radioactivity against time could be expressed as double exponential equations, with the first term representing diffusion, and the second, catabolism. No significant difference between the turnovers of human and monkey kininogens was observed. The difference between the t112 of high molecular weight kininogen (25.95±1.60 h) (mean +SEM) and that of low molecular weight kininogen (18.94±1.93 h) was only marginally significant (P < 0.05). In contrast, a highly significant (P < 0.001) difference in their mean catabolic rates (1.12±0.08 d-l for high molecular weight kininogen vs. 2.07±0.09 d-l for low molecular weight kininogen) was observed. These differences between the two kininogens were attributed to differences in their distribution between the intra-and extravascular pools. Studies of kininogen turnover will be useful in elucidating the in vivo func-

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Section: Discussionsupporting

confidence: 84%

Turnover of human and monkey plasma kininogens in rhesus monkeys.

Yamada¹,

Wing²,

Pierce³

et al. 1979

J. Clin. Invest.

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“…Although it is clear from the studies of Spragg and Austen that the majority of plasma kininogen is of low molecular weight (49), this does not appear to be the sole form of native human kininogen. Previous authors have described a human high molecular weight kininogen that possesses different kinetic properties when activated by kallikrein (15,20,50,51). It is clear from our studies that such a high molecular weight kininogen can be separated from low molecular weight kininogen and this kininogen has a special function in the early steps of the Hageman factor-dependent pathways.…”

mentioning

confidence: 53%

Williams trait. Human kininogen deficiency with diminished levels of plasminogen proactivator and prekallikrein associated with abnormalities of the Hageman factor-dependent pathways.

Colman¹,

Bagdasarian²,

Talamo³

et al. 1975

J. Clin. Invest.

321

194

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A B S T R A C T An asymptomatic woman (Ms. \Vil-liams) was found to have a severe abnormality in the surface-activated intrinsic coagulation, fibrinolvtic, and kinin-generating pathways. Assays for known coagulation factors were normal while Fletcher factor (prekallikrein) was 45%, insufficient to account for the observed markedly prolonged partial thromboplastin time. Plasminogen proactivator was present at 20% of normal levels and addition of highly purified plasminogen proactivator containing 10% plasminogen activator partially corrected the coagulation and fibrinolytic abnormalities but not the kinin-generating defect. This effect was due to its plasminogen activator content. In addition, Williams trait plasma failed to convert prekallikrein to kallikrein or release kiniin upon incubation with kaolin. Kininogen

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“…HMW-kininogen was prepared from normal human plasma by a modification of published methods (15,16). During purification, Fitzgerald factor activity was identified by a clotpromoting assay (12), 1 U being arbitrarily defined as that amount present in 1 ml of normal pooled plasma.…”

Section: Michmentioning

confidence: 99%