Flaujeac trait plasma resembled Hageman trait or Fletcher trait, in that the intrinsic coagulation pathway, plasma fibinolytic pathway, kinin-forming system, permeability factor of dilution (PF/dil) phenomenon were abnormal. The defect in each assay was reconstituted by afactor separable from Hageman factor or Fletcher factor. This substance was an alpha-globulin with an approximate mol wt of 170,000. Flaujeac plasma did not release a kinin upon incubation with kallikrein and was deficient in total kininogen antigen. Antiserum to kininogen inhibited the activity of the factor in solution. Flaufeac factor was identified as a kininogen of high molecular weight (HMW-kininogen). The mean total kininogen antigen in four children of the proposita was 51% (range 34-62%) of normal. A functional coagulation assay of HMW-kininogen in the children was 34% (range 23-55%). The results were consistent with autosomal recessive inheritance. The plasma pathways of intrinsic coagulation, fibrinolysis, kinin formation, and PF/dil generation are dependent upon HMW-kininogen. We believe this is the first demonstration of biological function for a kininogen apart from its role as a substrate for kallikreins.

/pdf/flaujeac-trait-deficiency-of-human-plasma-kininogen-3lxviessss.pdf

Flaujeac trait. Deficiency of human plasma kininogen.

Pathophysiology in Specific Pathologic States In the initial report describing bradykinin activity,2 it was proposed that this substance might have a pathogenic function in shock because of its hyp...

Kinins--possible physiologic and pathologic roles in man.

Publisher Summary In the early stages of inflammation, the main vascular events include vasodilatation and augmented blood flow, increased vascular permeability, and the emigration of neutrophil leukocytes. These events are evoked relatively quickly, even by moderate injury. Furthermore, the pattern of response is remarkably similar in various types of injuries and the rapidity and constancy of the vascular reactions appear to have prompted the notion that all the principal vascular phenomena in inflammation might be mediated by a common substance, even in different species. The inflammatory process, however, is complex; even individual vascular events may be complicated. Thus, the permeability response, for example, in thermal injury, includes both early and late responses, each of which is probably evoked by a different substance. The permeability changes also vary in both pattern and time course with different kinds of injuries, and it is likely that vasodilatation and tissue leukocytosis are similarly variable. The study of the chemical mediation of inflammation has been directed particularly at the increase in vascular permeability. Not only is increased permeability a key response in the inflammatory reaction, but also its experimental demonstration has made it an important indicator reaction in the search for mediators of the entire inflammatory process.

Chemical Mediators. I

Evidence is presented in this paper that the kaolin-activated arginine esterase of plasma is related to plasma kallikrein activity Such a relationship is based on studies that (1) establish a constant ratio of esterase activity on various synthetic substrates for the kaolin-activated arginine esterase, purified kallikrein(s), and preparations obtained during the fractionation procedure; (2) exclude other known plasma and tissue arginine esterases; (3) confirm the requirement for factor XII in the activation of the enzyme precursor; and (4) show similarities in behavior between the plasma esterase and purified kallikrein(s) toward a variety of inhibitors

Based on this probable identification, evidence is provided that the concentration of active factor XII determines the rate of activation of plasma kallikreinogen, and that the activation may be blocked by polybrene Once activated, plasma kallikrein is rapidly inactivated by the naturally occurring plasma inhibitor, but the inhibition is incomplete Acid or chloroform treatment of plasma rapidly inactivates the plasma inhibitor without affecting the concentration of plasma kallikreinogen

Another plasma arginine esterase with properties suggestive of permeability factor is activated by factor XII in the presence of synthetic substrates, but only at low ionic strength The data suggest that this enzyme is closely related to plasma kallikrein and that it arises from a common precursor

/pdf/studies-on-the-prekallikrein-kallikreinogen-kallikrein-5fpr5zwgnu.pdf

Studies on the prekallikrein (kallikreinogen)—kallikrein enzyme system of human plasma: II. Evidence relating the kaolin-activated arginine esterase to plasma kallikrein

A B S T R A C T Evidence is presented in this paper that the kaolin-activated arginine esterase of plasma is related to plasma kallikrein activity. Such a relationship is based on studies that (1) establish a constant ratio of esterase activity on various synthetic substrates for the kaolin-activated arginine esterase, purified kallikrein(s), and preparations obtained during the fractionation procedure; (2) exclude other known plasma and tissue arginine esterases; (3) confirm the requirement for factor XII in the activation of the enzyme precursor; and (4) show similarities in behavior between the plasma esterase and purified kallikrein (s) toward a variety of inhibitors. Based on this probable identification, evidence is provided that the concentration of active factor XII determines the rate of activation of plasma kallikreinogen, and that the activation may be blocked by polybrene. Once activated, plasma kallikrein is rapidly inactivated

/pdf/ii-evidence-relating-the-kaolin-activated-arginine-esterase-3rkxngotb5.pdf

Ii. evidence relating the kaolin-activated arginine esterase to plasma kallikrein

Susceptibility of the Guinea Pig to Pharmacological Factors from its Own Serum

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Susceptibility of the Guinea Pig to Pharmacological Factors from its Own Serum