Hageman factor substrates. Human plasma prekallikrein: mechanism of activation by Hageman factor and participation in hageman factor-dependent fibrinolysis.

Mandle, Robert J.; Kaplan, Allen P.

doi:10.1016/s0021-9258(17)40034-2

Cited by 192 publications

(19 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Preparation of Plasma Kallikrein. Prekallikrein was isolated by the procedure of Mandle and Kaplan (17). SDS gel electrophoresis of reduced prekallikrein yielded two bands of 88,000 and 85,000 daltons, respectively, as previously reported (17) and the preparation contained no detectable Hageman factor or factor XI.…”

Section: Methodsmentioning

confidence: 67%

“…Prekallikrein was isolated by the procedure of Mandle and Kaplan (17). SDS gel electrophoresis of reduced prekallikrein yielded two bands of 88,000 and 85,000 daltons, respectively, as previously reported (17) and the preparation contained no detectable Hageman factor or factor XI. Active kallikrein was obtained by incubating 100/~g of prekallikrein with 2 /~g of Hageman factor fragments (18) overnight at 4°C.…”

Section: Methodsmentioning

confidence: 67%

See 1 more Smart Citation

Characterization of human high molecular weight kininogen. Procoagulant activity associated with the light chain of kinin-free high molecular weight kininogen.

Thompson¹,

Mandle²,

Kaplan³

1978

The Journal of Experimental Medicine

Self Cite

132

View full text Add to dashboard Cite

High molecular weight (HMW) 1 kininogen has been shown to be a critical factor which functions at the initial step of the Hageman factor-dependent pathways. Thus, plasmas deficient in HMW kininogen have a markedly prolonged partial thromboplastin time and diminished kaolin-activatable fibrinolysis (1-4). The Hageman factor substrates, prekallikrein and factor XI, circulate bound to HMW kininogen (5, 6) and are adsorbed to negatively charged surfaces where they interact with surface-bound Hageman factor. HMW kininogen augments the ability of activated Hageman factor or Hageman factor fragments to activate prekallikrein (7-10) and factor XI (7-11), and it also augments the rate of Hageman factor activation (8) and cleavage (7, 12) by kallikrein. Kallikrein also cleaves the HMW kininogen to liberate the vasoacrive peptide bradykinin.We have previously reported that kinin-free HMW kininogen could still function as a coagulation factor (2) and this observation was confirmed by Schiffman et al. (13). However, Chan et al. (14) reported that kallikrein digestion of human HMW kininogen progressively diminished its coagulant activity, while Matheson et al. (15) assessed bovine HMW kininogen in human HMW kininogen-deficient plasma and found that the kinin-free protein possessed <1% of the coagulant activity of the native molecule. In this report we investigate the structural changes that occur in purified human HMW kininogen as a consequence of kallikrein digestion. The critical portion of the molecule that is responsible for its coagulant activity has been isolated, as reported in preliminary form (6), and is shown to possess an antigenic determinant that distinguishes HMW kininogen from low molecular weight (LMW) kininogen.

show abstract

Section: Methodsmentioning

confidence: 67%

Section: Methodsmentioning

confidence: 67%

Characterization of human high molecular weight kininogen. Procoagulant activity associated with the light chain of kinin-free high molecular weight kininogen.

Thompson¹,

Mandle²,

Kaplan³

1978

The Journal of Experimental Medicine

Self Cite

132

View full text Add to dashboard Cite

show abstract

“…These morphologic changes are associated with, and presumably the result of, activation of factor XII-dependent pathways and generation of kinin activity because it could be demonstrated that coagulation and fibrinolytic pathways had been activated in the dog and monkey. Activated factor XII converts prekallikrein to kallikrein, and several laboratories have presented evidence indicating that kallikrein converts plasminogen to plasmin (9,10). Ellagic acid and E. coli endotoxin are known to activate factor XII-dependent pathways in vitro and in vivo, and it has been demonstrated in this laboratory that rutin can activate factor XII-dependent pathways in human plasma in vitro (11)(12)(13)(14).…”

Section: Discussionmentioning

confidence: 97%

Induction of acute cholecystitis by activation of factor XII.

Becker¹,

Dubin²,

Glenn³

1980

The Journal of Experimental Medicine

View full text Add to dashboard Cite

Acute, acalculous cholecystitis is a serious, often fatal disease that is seen among patients suffering with bacterial sepsis, burns, or trauma, including surgical trauma, and cancer (1). In 1921, F. C. Mann (2) of the Mayo Clinic induced acute inflammation and hemorrhage in the gall bladder of dogs by intravenous injection of solutions of sodium hypochloride. Mann's experiments (2) indicated that the gall bladder could be injured by intravenous injection of a known chemical substance and/or a chain of events set in motion by such an injection.Factor XII (Hageman factor) can be activated by bacterial endotoxin and by exposure of plasma to collagen (3, 4). It is possible in the clinical settings mentioned above that induction of acute cholecystitis results from the activation of the intrinsic pathway of coagulation leading to generation of mediators of inflammation.To test this hypothesis we injected dogs and monkeys intravenously with chemically defined polyphenol activators of factor XII, with Escherichia coli endotoxin, or with buffered saline and observed the effects of systemic activation of factor XII-dependent pathways on the gall bladder and other tissues. The results of these experiments are described below. Materials and MethodsExperimental Protocol. 12 mongrel male dogs that weighed between 8 and 15 kg, and 3 male African Green Monkeys (Cercopithecus aethiops) that weighed between 4 and 6 kg, were used. The animals were anesthetized by intravenous injection of pentobarbital, and under surgical conditions the abdomen was opened and the gall bladder visualized. Besides the gall bladder, the stomach, duodenum, small bowel, colon, mesentery, liver, and spleen were clearly visible in the operative field.Animals were injected in the femoral vein with 10 -4 M solutions of ellagic acid (K and K Laboratories, Inc., Plainview, N. Y.), rutin (Sigma Chemical Co., St. Louis, Mo.), or with lipopolysaccharide W E. coli O128:B12 (Difco Laboratories, Detroit, Mich.), all dissolved in phosphate-buffered physiologic saline (PBS), 1 or with PBS in comparable volume as control according to the plan in Table I.Blood samples were obtained before injection of solutions of ellagic acid, rutin, E. coli endotoxin, or PBS, at intervals thereafter either by venopuncture with plastic syringes or through a polyethylene catheter implanted in the femoral vein, and anticoagulated with Na citrate in chilled plastic tubes for studies described below.The gall bladder and other viscera were observed for 1 h after injection of activator substance or control PBS, and photographs taken at different intervals during this period. At the end of

show abstract

“…Platelets themselves are readily activated at negatively charged surfaces [39] or by shear stress [43] from the HLM or wringing of the swabs. Tissue-factor expressing cells, such as activated monocytes [44], or neutrophil extracellular traps (NET) from activated neutrophils [45], can trigger the coagulation cascade [46], but also contact phase activation (by hydrolysis of FXII [47]) through the artificial surfaces of the HLM or swabs can occur and promote coagulation and inflammation [48][49][50][51]. A significant coagulation activation (measured by TAT complex formation) was observed in blood taken from the HLM despite the high anticoagulation regime used to prevent this [52,53].…”

Section: Discussionmentioning

confidence: 99%

Synthetic Material Abdominal Swabs Reduce Activation of Platelets and Leukocytes Compared to Cotton Materials

et al. 2021

View full text Add to dashboard Cite

During surgical procedures, cotton abdominal swabs with their high absorptive capacity and malleability are used to retain organs and absorb blood or other body fluids. Such properties of the natural material cotton are advantageous for most operations, but in cardiopulmonary bypass (CPB) surgery, a high blood volume can accumulate in the thoracic cavity that is quickly retransfused via the heart–lung machine (HLM). This common practice is supposed to be safe due to the high anticoagulation. However, in vitro analyses showed that blood cells and plasma proteins were activated despite a high anticoagulation, which can propagate especially an inflammatory response in the patient. Thus, we investigated patients’ blood during CPB surgery for inflammatory and coagulation-associated activation after contact to the HLM and either cotton or synthetic abdominal swabs. Contact with cotton significantly increased thrombocyte and neutrophil activation measured as β-thromboglobulin and PMN-elastase secretion, respectively, compared to synthetic abdominal swabs. Both inflammatory cytokines, interleukin (IL) 1β and IL6, were also significantly increased in the cotton over the synthetic patient group, while SDF-1α was significantly lower in the synthetic group. Our data show for the first time that cotton materials can activate platelets and leukocytes despite a high anticoagulation and that this activation is lower with synthetic materials. This additional activation due to the material on top of the activation exerted by the tissue contact that blood is exposed to during CPB surgery can propagate further reactions in patients after surgery, which poses a risk for this already vulnerable patient group.

show abstract

Hageman factor substrates. Human plasma prekallikrein: mechanism of activation by Hageman factor and participation in hageman factor-dependent fibrinolysis.

Cited by 192 publications

References 26 publications

Characterization of human high molecular weight kininogen. Procoagulant activity associated with the light chain of kinin-free high molecular weight kininogen.

Characterization of human high molecular weight kininogen. Procoagulant activity associated with the light chain of kinin-free high molecular weight kininogen.

Induction of acute cholecystitis by activation of factor XII.

Synthetic Material Abdominal Swabs Reduce Activation of Platelets and Leukocytes Compared to Cotton Materials

Contact Info

Product

Resources

About