Threshold-stimulated kallikrein activity distinguishes bradykinin- from histamine-mediated angioedema

SummaryThe behaviour of the contact system was studied in 40 patients with total hip arthroplasty, by measuring plasma prekallikrein, spontaneous kallikrein activity and factor XII. In the literature it had been shown that patients with complications from this operation had decreased prekallikrein and increased kallikrein activity (M. Nakahara. Acta orthop scand 1982; 53: 591-6). In the present study, comprising patients with and without pain and proven loosening of the hip prosthesis, these findings could only partially be confirmed. Patients with a loosened prosthesis had significantly lower prekallikrein (mean 0.78 ± 0.28 U/ml; p <0.01) than patients without problems, but no detectable kallikrein activity in plasma. Patients with pain but no loosening had normal prekallikrein (1.04 ±0 0.26 U/ml) and also no demonstrable kallikrein activity. Factor XII was normal in all patient groups. It is concluded that decreased prekallikrein is limited to patients with a loosened hip prosthesis, with or without pain.

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Cold Promoted Activation of Factor VII VI. Effect of Inhibitors

Thrombosis and Haemostasis ◽

10.1055/s-0038-1648105 ◽

1973 ◽

Vol 29 (03) ◽

pp. 633-643

Author(s):

H Gjønnæss

Keyword(s):

Soya Bean ◽

Factor Vii ◽

Plasma Kallikrein ◽

Contact Activation ◽

Activation Reaction ◽

Hexadimethrine Bromide ◽

Bean Trypsin Inhibitor ◽

Plasma Arginine ◽

Kallikrein Activity ◽

Effect Of Inhibitors

SummaryThe cold promoted activation of factor VII occurs in parallel with an activation of a plasma arginine esterase, and, on inhibition of the cold activation of factor VII, the esterase activation also decreased. The inhibitor pattern supported our theory that the arginine esterase that is activated in the cold activation of factor VII is plasma kallikrein.The cold activation of factor VII was completely inhibited with soya bean trypsin inhibitor in doses that did not interfere with the contact activation. On the other hand, inhibition of the contact activation with hexadimethrine bromide did not interfere with the cold activation of factor VII except when this was kaolin induced. Contact and cold activation therefore appear to represent two different pathways for the activation of factor VII. The cold activation reaction is probably mediated by the activation of plasma prekallikrein, and inhibition of the plasma kallikrein activity correlates with the inhibition of the cold promoted activation of factor VII.

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The Relationship of Urinary Kallikrein Activity to Renal Salt and Water Excretion

Clinical Science ◽

10.1042/cs0540039 ◽

1978 ◽

Vol 54 (1) ◽

pp. 39-45 ◽

Cited By ~ 1

Author(s):

S. B. Levy ◽

R. P. Frigon ◽

R. A. Stone

Keyword(s):

Racial Differences ◽

Sodium Intake ◽

Dietary Sodium ◽

Racial Groups ◽

Urinary Kallikrein ◽

Experimental Conditions ◽

Water Excretion ◽

Water Load ◽

Black And White ◽

Kallikrein Activity

1. We measured urinary kallikrein (kininogenin) excretion in black and white normotensive subjects during a variety of manipulations of salt and water balance. 2. A large intravenous saline load administered while the subjects were on an unrestricted sodium diet did not significantly change urinary kallikrein activity in either racial group. 3. After several days of dietary sodium restriction both racial groups increased their urinary kallikrein activity. An intravenous water load given then further increased urinary kallikrein activity. White subjects were studied for an additional 24 h period, and urinary kallikrein activity returned to pre-water load values, indicating that the excretion of a water load in sodium-depleted subjects is associated with an increase in kallikrein excretion. 4. Black subjects excreted less kallikrein in the urine than white subjects during the initial 24 h periods of unrestricted dietary sodium intake, but there were no other significant racial differences during the other experimental conditions.

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Plasma Total Prekallikrein/Kallikrein Activity in Rheumatoid Arthritis with and without Amyloidosis

Acta Medica Scandinavica ◽

10.1111/j.0954-6820.1985.tb02714.x ◽

2009 ◽

Vol 217 (4) ◽

pp. 397-402 ◽

Cited By ~ 2

Author(s):

ANNA-MAIJA TEPPO ◽

RAIMO PAKKANEN ◽

C.P. J. MAURY

Keyword(s):

Rheumatoid Arthritis ◽

Kallikrein Activity

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P1-93 Prenatal hyperglycemia alters kallikrein activity response to high sodium diet in adult rats

Early Human Development ◽

10.1016/s0378-3782(07)70263-3 ◽

2007 ◽

Vol 83 ◽

pp. S108

Author(s):

S.P. Salas ◽

A. Giacaman ◽

F.J. Guarda ◽

J. Acosta ◽

C.P. Vío

Keyword(s):

Adult Rats ◽

High Sodium ◽

Sodium Diet ◽

Activity Response ◽

Kallikrein Activity ◽

High Sodium Diet

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Plasma Prekallikrein, Functional Kallikrein Inhibition, Antithrombin III, Plasminogen, Kallikrein Activity and Proenzyme Functional Inhibition Index in 172 Acute ILL Surgical Patients on Admission

Kinins IV - Advances in Experimental Medicine and Biology ◽

10.1007/978-1-4757-0154-8_58 ◽

1986 ◽

pp. 451-461

Author(s):

L. Viksmoen ◽

O. P. N. Grüner ◽

P. Bjoernstad ◽

A. O. Aasen

Keyword(s):

Antithrombin Iii ◽

Surgical Patients ◽

Functional Inhibition ◽

Kallikrein Activity ◽

Inhibition Index

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Pathophysiology of genetic deficiency in tissue kallikrein activity in mouse and man

Thrombosis and Haemostasis ◽

10.1160/th12-12-0937 ◽

2013 ◽

Vol 110 (09) ◽

pp. 476-483 ◽

Cited By ~ 18

Author(s):

Ludovic Waecke ◽

Louis Potier ◽

Christine Richer ◽

Ronan Roussel ◽

Nadine Bouby ◽

...

Keyword(s):

Human Subjects ◽

Physiological Role ◽

Tissue Kallikrein ◽

Site Mutation ◽

Cardiac Ischaemia ◽

Kinin Receptors ◽

At1 Receptor Antagonists ◽

Kallikrein Activity ◽

Deficient Mice

SummaryStudy of mice rendered deficient in tissue kallikrein (TK) by gene inactivation and human subjects partially deficient in TK activity as consequence of an active site mutation has allowed recognising the physiological role of TK and its peptide products kinins in arterial function and in vasodilatation, in both species. TK appears as the major kinin forming enzyme in arteries, heart and kidney. Non-kinin mediated actions of TK may occur in epithelial cells in the renal tubule. In basal condition, TK deficiency induces mild defective phenotypes in the cardiovascular system and the kidney. However, in pathological situations where TK synthesis is typically increased and kinins are produced, TK deficiency has major, deleterious consequences. This has been well documented experimentally for cardiac ischaemia, diabetes renal disease, peripheral ischaemia and aldosterone-salt induced hypertension. These conditions are all aggravated by TK deficiency. The beneficial effect of ACE/kininase II inhibitors or angiotensin II AT1 receptor antagonists in cardiac ischaemia is abolished in TK-deficient mice, suggesting a prominent role for TK and kinins in the cardioprotective action of these drugs. Based on findings made in TK-deficient mice and additional evidence obtained by pharmacological or genetic inactivation of kinin receptors, development of novel therapeutic approaches relying on kinin receptor agonism may be warranted.

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Application of bradykinin radioimmunoassay for the measurement of urinary kallikrein activity in rats

Klinische Wochenschrift ◽

10.1007/bf01477463 ◽

1978 ◽

Vol 56 (S1) ◽

pp. 127-129 ◽

Cited By ~ 12

Author(s):

M. Stocker ◽

J. Hornung

Keyword(s):

Urinary Kallikrein ◽

Kallikrein Activity

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A monoclonal anti-human plasma prekallikrein antibody that inhibits activation of prekallikrein by factor XIIa on a surface

Blood ◽

10.1182/blood.v70.4.1053.bloodjournal7041053 ◽

1987 ◽

Vol 70 (4) ◽

pp. 1053-1062

Author(s):

D Veloso ◽

LD Silver ◽

S Hahn ◽

RW Colman

Keyword(s):

Heavy Chain ◽

Sodium Dodecyl ◽

Factor Xii ◽

Contact Activation ◽

Fab Fragments ◽

Microtiter Plates ◽

Normal Plasma ◽

Reducing Conditions ◽

Factor Xiia ◽

Kallikrein Activity

Of five IgGI/k murine monoclonal anti-human prekallikrein antibodies produced (MAbs), MAb 13G11 was selected for studying interaction of prekallikrein with factor XII and high-mol-wt kininogen (HMWK) during activation on a surface. Immunoblots from sodium dodecyl sulfate (SDS) gels showed that this MAb recognizes two variants (88 kd and 85 kd) of prekallikrein and kallikrein both in purified proteins and normal plasma. Under reducing conditions, kallikrein exhibits the epitope on the heavy chain but not on the light chains. Preincubation of MAb 13G11 with prekallikrein (added to prekallikrein-deficient plasma) or with normal plasma inhibited surface activation of prekallikrein 60% to 80%, as judged by amidolytic and coagulant assays. In normal plasma, inhibition by the Fab fragments was 87% of that with the entire MAb. Inhibition was not by competition between the MAb and HMWK, since neither binding of 13G11 to prekallikrein (coated on microtiter plates) was inhibited by an excess of HMWK, nor was hydrolysis of HMWK by kallikrein inhibited by 13G11. Using purified proteins in a system mimicking contact activation, inhibition by 13G11 of prekallikrein activation by factor XIIa, HMWK, and kaolin present was approximately 80%. Decreased inhibition (55% to 25%) occurred without HMWK or when kallikrein was used instead of prekallikrein. Kallikrein activity was not inhibited by 13G11 Fab fragments. These results indicate that the effect of 13G11 in plasma was neither dissociation of prekallikrein- HMWK complex nor a direct effect on kallikrein activity. Similar to the results in plasma, activation of prekallikrein, HMWK present, by factor XIIa bound to kaolin, was inhibited approximately 70% by 13G11. The results suggest a previously unrecognized site on the prekallikrein (heavy chain) required for its interaction with factor XIIa, either shared with the 13G11 epitope or located in very close proximity. The inhibition of kallikrein by intact 13G11 indicates that its binding site on the heavy chain is sterically related to the active site (light chain).

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