Interaction of human plasma kallikrein and its light chain with C.hivin.1 inhibitor

Biochemistry ◽  
1983 ◽  
Vol 22 (20) ◽  
pp. 4860-4866 ◽  
Author(s):  
Fedde Van der Graaf ◽  
Johannes A. Koedam ◽  
John H. Griffin ◽  
Bonno N. Bouma
Keyword(s):  
Human Plasma ◽  
Light Chain ◽  
Plasma Kallikrein

Corrections - High Molecular Weight Kininogen or its Light Chain Protects Human Plasma Kallikrein from Inactivation by Plasma Protease Inhibitors

Biochemistry ◽  
1982 ◽  
Vol 21 (12) ◽  
pp. 3036-3036
Author(s):  
Marc Schapira ◽  
Cheryl Scott ◽  
Ann James ◽  
Lee Silver ◽  
Frederich Kueppers ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Human Plasma ◽  
High Molecular Weight ◽  
Protease Inhibitors ◽  
Light Chain ◽  
Plasma Kallikrein ◽  
High Molecular Weight Kininogen

High molecular weight kininogen or its light chain protects human plasma kallikrein from inactivation by plasma protease inhibitors

Biochemistry ◽  
1982 ◽  
Vol 21 (3) ◽  
pp. 567-572 ◽  
Author(s):  
Marc Schapira ◽  
Cheryl F. Scott ◽  
Ann James ◽  
Lee D. Silver ◽  
Friedrich Kueppers ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Human Plasma ◽  
High Molecular Weight ◽  
Protease Inhibitors ◽  
Light Chain ◽  
Plasma Kallikrein ◽  
High Molecular Weight Kininogen

scholarly journals Effect of cleavage of the heavy chain of human plasma kallikrein on its functional properties

Blood ◽  
1985 ◽  
Vol 65 (2) ◽  
pp. 311-318 ◽  
Author(s):  
RW Colman ◽  
YT Wachtfogel ◽  
U Kucich ◽  
G Weinbaum ◽  
S Hahn ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Human Plasma ◽  
Heavy Chain ◽  
Light Chain ◽  
Human Neutrophils ◽  
Plasma Kallikrein ◽  
Factor Xii ◽  
C1 Inhibitor ◽  
Amidolytic Activity ◽  
Coagulant Activity

Abstract Human plasma kallikrein consists of an N-terminal heavy chain of molecular weight (mol wt) 52,000, linked by disulfide bonds to two light chain variants (mol wt 36,000 or 33,000). Although the active catalytic site of kallikrein resides on the C-terminal light chain, the role of the N-terminal heavy chain is less clear. We therefore studied an enzyme designated beta-kallikrein, containing a single cleavage in the heavy chain (mol wt 28,000 + 18,000) and compared it to the enzyme, alpha-kallikrein, with an intact heavy chain. The rates of inactivation by C1 inhibitor of plasma alpha- and beta-kallikreins were kinetically identical, as measured by residual amidolytic activity, after various times of incubation with the inhibitor. Both enzymes reacted completely with C1 inhibitor after 18 hours and formed identical C1 inhibitor- kallikrein complexes of mol wt 195,000. The rate of activation of factor XII by alpha-kallikrein and beta-kallikrein was similar. In contrast, the rate of cleavage of high molecular weight kininogen (HMWK) by alpha-kallikrein was at least fivefold faster and the ratio of coagulant activity to amidolytic activity was fourfold greater than for beta-kallikrein. Plasma alpha-kallikrein, at concentrations potentially achievable in plasma, induced aggregation of neutrophils, but beta-kallikrein failed to elicit this response. In addition, human neutrophils pretreated with cytochalasin B released 2.46 +/- 0.10 microgram/10(7) cells of elastase antigen, but beta-kallikrein released only 0.25 +/- 0.10 micrograms/10(7) cells. These observations suggest that cleavage of the heavy chain influences the rate of cleavage of HMWK and decreases its coagulant activity. Moreover, an intact heavy chain appears to be requisite to support the ability of kallikrein to aggregate neutrophils and release elastase.

Interaction of human plasma kallikrein and its light chain with .alpha.2-macroglobulin

Biochemistry ◽  
1984 ◽  
Vol 23 (8) ◽  
pp. 1760-1766 ◽  
Author(s):  
Fedde Van der Graaf ◽  
Annie Rietveld ◽  
Freke J. A. Keus ◽  
Bonno N. Bouma
Keyword(s):  
Human Plasma ◽  
Light Chain ◽  
Plasma Kallikrein

Structure - Function Relationships of Human High MW Kininogen(HMWK), A Cofactor in Contact Activation of Human Plasma

1979 ◽  
Author(s):  
D. M. Kerbiriou ◽  
J.H. Griffin
Keyword(s):  
Human Plasma ◽  
Light Chain ◽  
Procoagulant Activity ◽  
Free Form ◽  
Plasma Kallikrein ◽  
Factor Xii ◽  
Free Molecule ◽  
Contact Activation ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

HMWK has been isolated from human plasma as a single polypeptide chain of apparent 110,000 MW on SDS gels. Purified plasma kallikrein cleaved HMWK to produce kinin and a kinin-free molecule made up of two disulfide-linked polypeptide chains with apparent MW of 65,000 and 44,000. Following reduction and carboxymethylation of the two-chain, kinin-free molecule, a histidine-rich light chain was isolated that quantitatively retained the full procoagulant activity of the native molecule. HMWK was digested with a bacterial protease to produce kinin and polypeptides that have no procoagulant activity. From this digest, cationic fragments were isolated which possess a high histidine (36%) and glycine (36%) content that is similar to the composition of Fragment 1.2 cleaved from bovine HMWK by bovine plasma kallikrein. When kaolin was added to normal human plasma containing 125I-HMWK and 131I-Factor XII , the HMWK was rapidly cleaved with a half-time of cleavage of 40 ± 10 sec which was similar to the kinetics of cleavage of Factor XII. This surface-initiated cleavage of 125I-HMWK in plasma did not occur in plasmas deficient in either prekallikrein or Factor XII, but occurred when purified kallikrein was added. These observations suggest that when kaolin is added to plasma, kallikrein cleaved HMWK to release kinin and to give rise to a two-chain, kinin-free form of HMWK whose ability to correct the clotting deficiency of HMWK-deficient plasma resides totally in the histidine-rich light chain of the molecule.

scholarly journals Effect of cleavage of the heavy chain of human plasma kallikrein on its functional properties

Blood ◽  
1985 ◽  
Vol 65 (2) ◽  
pp. 311-318 ◽  
Author(s):  
RW Colman ◽  
YT Wachtfogel ◽  
U Kucich ◽  
G Weinbaum ◽  
S Hahn ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Human Plasma ◽  
Heavy Chain ◽  
Light Chain ◽  
Human Neutrophils ◽  
Plasma Kallikrein ◽  
Factor Xii ◽  
C1 Inhibitor ◽  
Amidolytic Activity ◽  
Coagulant Activity

Human plasma kallikrein consists of an N-terminal heavy chain of molecular weight (mol wt) 52,000, linked by disulfide bonds to two light chain variants (mol wt 36,000 or 33,000). Although the active catalytic site of kallikrein resides on the C-terminal light chain, the role of the N-terminal heavy chain is less clear. We therefore studied an enzyme designated beta-kallikrein, containing a single cleavage in the heavy chain (mol wt 28,000 + 18,000) and compared it to the enzyme, alpha-kallikrein, with an intact heavy chain. The rates of inactivation by C1 inhibitor of plasma alpha- and beta-kallikreins were kinetically identical, as measured by residual amidolytic activity, after various times of incubation with the inhibitor. Both enzymes reacted completely with C1 inhibitor after 18 hours and formed identical C1 inhibitor- kallikrein complexes of mol wt 195,000. The rate of activation of factor XII by alpha-kallikrein and beta-kallikrein was similar. In contrast, the rate of cleavage of high molecular weight kininogen (HMWK) by alpha-kallikrein was at least fivefold faster and the ratio of coagulant activity to amidolytic activity was fourfold greater than for beta-kallikrein. Plasma alpha-kallikrein, at concentrations potentially achievable in plasma, induced aggregation of neutrophils, but beta-kallikrein failed to elicit this response. In addition, human neutrophils pretreated with cytochalasin B released 2.46 +/- 0.10 microgram/10(7) cells of elastase antigen, but beta-kallikrein released only 0.25 +/- 0.10 micrograms/10(7) cells. These observations suggest that cleavage of the heavy chain influences the rate of cleavage of HMWK and decreases its coagulant activity. Moreover, an intact heavy chain appears to be requisite to support the ability of kallikrein to aggregate neutrophils and release elastase.

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