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

Colman, Robert W.; Bagdasarian, Andranik; Talamo, Richard C.; Scott, Cheryl F.; Seavey, Molly; Guimarães, Jorge A.; Pierce, Jack V.; Kaplan, Allen P.

doi:10.1172/jci108247

Cited by 321 publications

(207 citation statements)

References 39 publications

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“…The deficiency of HK leads to in vitro coagulation impairment but not an in vivo hemostatic disorder (Colman et al, 1975). However, a large body of evidence supports the important role of HK and thus the contact system in body defenses (Colman, 1984).…”

Section: Discussionmentioning

confidence: 99%

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The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc‐dependent binding to an anionic surface

Dela

Colman

1992

Protein Science

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The histidine-glycine-rich region of the light chain of cleaved high molecular weight kininogen (HK) is thought to be responsible for binding to negatively charged surfaces and initiation of the intrinsic coagulation, fibrinolytic, and kinin-forming systems. However, the specifically required amino acid sequences have not been delineated. An IgG fraction of a monoclonal antibody (MAb) CllCl to the HK light chain was shown to inhibit by 66% the coagulant activity and by 57% the binding of HK to the anionic surface of kaolin at a concentration of 1.5 pM and 27 pM, respectively. Proteolytic fragments of HK were produced by successive digestion with human plasma kallikrein and factor XIa (FXIa). Those polypeptides that bound tightly (Kd = 0.77 nM) to a C11C1 affinity column were eluted at pH 3.0 and purified by membrane filtration. On 15% SDS polyacrylamide electrophoresis, the approximate M, was 7.3 kDa (range 6.2-8.1 kDa). Based on N-terminal sequencing, this polypeptide (I2), which extends from the histidine residue 459 to a lysine at position 505, 509, 51 1, 512, 515, or 520, inhibits by 50% the coagulant activity expressed by HK at a concentration of 22 pM. The synthetic peptide HGLGHGH representing the N-terminal of the l2 fragment was synthesized, tested, and found at 4 mM to inhibit the procoagulant activity of HK 50%. A synthetic heptadecapeptide, HGLGHGHEQQHGLGHGH (residues 459-475) included within the l2 fragment, and with the ability to bind zinc, inhibited 50% of the HK coagulant activity at a concentration of 325 pM in the absence and presence of added Zn2+ (30 pM). The specific binding of 12'I-HK to a negatively charged surface (kaolin) was inhibited 50% by unlabeled HK (5 pM). HGLGHGH, at a concentration of 7.0 mM, inhibited the binding to kaolin by 50%. The heptadecapeptide inhibited the specific binding of I2'I-HK to kaolin by 50%, at a concentration of 2.3 mM, in the absence of Zn2+.In contrast, when Zn2+ was added, the concentration to achieve 50% inhibition decreased to 630 pM, indicating that Zn2+ was required to attain a favorable conformation for binding. Moreover, the I, fragment was found to inhibit 50% of the I2'I-HK binding to kaolin at a concentration of 380 pM. These results suggest that residues contained within the 1, fragment, notably HGLGHGHEQQHGLGHGH, serves as a primary structural feature for binding to a negatively charged surface.

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Section: Discussionmentioning

confidence: 99%

“…Normal pooled plasma (PNP), used as a reference standard, was purchased from George King Biomedicals, Inc. (Overland Park, Kansas). Plasmas deficient in FXI and HK were donated directly to us by a know FXI-deficient patient and M. Williams (Colman et al, 1975), respectively. Ninety-six-well tissue culture plates (no.…”

Section: Methodsmentioning

confidence: 99%

The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc‐dependent binding to an anionic surface

Dela

Colman

1992

Protein Science

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“…Proteins that are known to be involved in contact activation of human plasma include Hageman factor (HF, blood coagulation Factor XII) (6), plasma prekallikrein (Fletcher factor) (7,8), coagulation Factor XI (plasma thromboplastin antecedent) (9), and high molecular weight (Mr) kininogen, which was recognized in studies.of Flaujeac trait (10), Fitzgerald trait (11,12), Williams trait (13), and "contact activation cofactor" (14).…”

mentioning

confidence: 99%

Role of surface in surface-dependent activation of Hageman factor (blood coagulation Factor XII)

Griffin

1978

Proc. Natl. Acad. Sci. U.S.A.

243

143

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The mechanism by which negatively charged substances such as celite, kaolin, or ellagic acid contribute to the surface-dependent activation of Hageman factor (Factor XII) was studied. Kinetic studies of the proteolytic activation of '514-labeled human Hageman factor by human plasma kallikrein, plasmin, activated Factor XI, and trypsin were performed in the presence and absence of hig molecular, weight kininogen and surface materials such as celite, kaolin, or ellagic acid. The results showed that surface-bound Hageman factor was 500 times more susceptible than soluble Hageman factor to proteolytic activation by kallikrein in the presence of high molecular weight kininogen. Surface binding of Hageman factor enhanced its cleavage by plasmin, activated Factor XI, and trypsin by 100-fold, 30-fold, and 5-fold, respectively. On a molar basis, trypsin was twice as potent as kallikrein in the cleavage of the surface-bound Hageman factor, while plasmin and activated Factor XI were an order of magnitude less potent than kallikrein. Kallikrein even at concentrations as low as 0.5 nM (i.e., 1/1000th of the concentration of prekallikrein' in plasma) was very potent in the limited proteolysis of the surface-boulid Hageman factor. These results suggest that substances classically known as "activating surfaces" promote the activation of Hageman factor indirectly by alerng its structure such that it is much more susceptible to proteolytic activation by otherplasma or cellular proteases.

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“…2). Kinin generation in human plasma is dependent upon the interaction of certain negatively charged surfaces with factor XII (Hageman factor -HF) and the circulating prekallikrein-HMWK complex (16,73,87). Activated HF (HFA) initiates the conversion of prekallikrein to kallikrein, which, in a positive feedback mechanism, rapidly activates the further conversion of HF in its activated form.…”

Section: Biochemical Pharmacology Of Kininsmentioning

confidence: 99%

Role of the kinin‐kallikrein pathway in allergic diseases

Polosa¹

1993

Allergy

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

Cited by 321 publications

References 39 publications

The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc‐dependent binding to an anionic surface

The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc‐dependent binding to an anionic surface

Role of surface in surface-dependent activation of Hageman factor (blood coagulation Factor XII)

Role of the kinin‐kallikrein pathway in allergic diseases

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