Male reproductive function and semen.

Acute inflammation. A review.

https://mmbr.asm.org/content/mmbr/27/2/117.full.pdf

The inflammatory response

Hereditary angioneurotic edema. I. Case reports and review of the literature.

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.

THE increase of vascular permeability in response to a number of types of mild injury—including thermal injury—is biphasic, consisting of a transient immediate phase, usually lasting 20–30 min, and a delayed phase which comes to a maximum several hours later1–3. The alteration of a vessel wall is demonstrable in animals with carbon particles or a vital dye in the circulating blood: in one case the carbon is deposited between the vascular endothelium and the basement membrane under it; in the other, dye-stained plasma exudes into the surrounding tissues. Majno et al.4,5, applying these methods to the rat cremaster muscle, showed therein that venules and fine capillary vessels were readily distinguishable by their characteristic distribution and size, and that, according to the type of injury, venules alone or both venules and capillaries might be affected. We used Majno's technique to locate the site of vascular change during the response to mild thermal injury. A heated copper disk 9 mm in diameter, as used by Wilhelm and Mason3 in their investigation of thermal injury to the dorsal skin of the rat trunk, was applied to the scrotal skin.

Site of the Vascular Reponse to Thermal Injury

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

Enzyme-like globulins from serum reproducing the vascular phenomena of inflammation. IV. Activable permeability factor and its inhibitor in the serum of the rat and the rabbit.

Globulin Permeability Factors without Kininogenase Activity

THE globulin permeability factors obtainable from the serum of man1, guinea pig2,3, rat4 and rabbit4 appear to be proteases because they are highly active on vascular endothelium—on a molar basis, they are 60–2,000 times as active as histamine, itself a potent permeability factor5; and because they are readily inhibited by prior treatment in vitro with the trypsin inhibitors from soya bean, lima bean and bovine pancreas. The action of these inhibitors, however, is apparently very rapid, a mixture of factor and inhibitor only 1 min. old being inactive when injected into the skin of animals with circulating pontamine blue4,7. Consequently, it is impossible to distinguish inactivation of a protease permeability factor in vitro from inactivation of a protease newly activated in vivo. Moreover, even the best preparations of permeability factors also contain known serum proteases, and so far no enzyme substrate has been found which is hydrolysed by serum fractions in strict proportion to their content of permeability factor.

Enzymic Nature of the Serum Globulin Permeability Factor

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