scholarly journals Interactions of C1(-)-inhibitors from normal persons and patients with type II hereditary angioneurotic edema with purified activated Hageman factor (factor XIIa)

Blood ◽  
1990 ◽  
Vol 75 (4) ◽  
pp. 911-921 ◽  
Author(s):  
VH Donaldson ◽  
BH Mitchell ◽  
B Everson ◽  
OD Ratnoff
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Type Ii ◽  
C1 Inhibitor ◽  
Angioneurotic Edema ◽  
Hageman Factor ◽  
Hereditary Angioneurotic Edema ◽  
Coagulant Activity ◽  
Inhibitor Type ◽  
Carboxy Terminal

Abstract Activated high molecular weight Hageman factor (75 Kd) and Hageman factor carboxy-terminal fragments both formed complexes with purified C1(-)-inhibitor, but the Hageman factor fragments appeared to have a higher affinity for the C1(-)-inhibitor than activated Hageman factor. Therefore, the clot-promoting activity of activated Hageman factor might be relatively unimpaired if Hageman factor fragments are also present. Normal C1(-)-inhibitor was cleaved by Hageman factor fragments. Clot-promoting activity was not generated in Hageman factor by exposure to Hageman factor fragments, nor was Hageman factor cleaved by Hageman factor fragments. When Hageman factor was cleaved by streptokinase-activated plasminogen, a 40 Kd fragment was released. In contrast to their interactions with other proteinases, which are blocked by normal C1(-)-inhibitor, Type II C1(-)-inhibitors from plasmas of affected members of eight different kindred with this form of hereditary angioneurotic edema all inhibited the specific coagulant activity of activated Hageman factor to some degree. They did not all form complexes with activated Hageman factor that were stable during sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

scholarly journals Interactions of C1(-)-inhibitors from normal persons and patients with type II hereditary angioneurotic edema with purified activated Hageman factor (factor XIIa)

Blood ◽  
1990 ◽  
Vol 75 (4) ◽  
pp. 911-921
Author(s):  
VH Donaldson ◽  
BH Mitchell ◽  
B Everson ◽  
OD Ratnoff
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Type Ii ◽  
C1 Inhibitor ◽  
Angioneurotic Edema ◽  
Hageman Factor ◽  
Hereditary Angioneurotic Edema ◽  
Coagulant Activity ◽  
Inhibitor Type ◽  
Carboxy Terminal

Activated high molecular weight Hageman factor (75 Kd) and Hageman factor carboxy-terminal fragments both formed complexes with purified C1(-)-inhibitor, but the Hageman factor fragments appeared to have a higher affinity for the C1(-)-inhibitor than activated Hageman factor. Therefore, the clot-promoting activity of activated Hageman factor might be relatively unimpaired if Hageman factor fragments are also present. Normal C1(-)-inhibitor was cleaved by Hageman factor fragments. Clot-promoting activity was not generated in Hageman factor by exposure to Hageman factor fragments, nor was Hageman factor cleaved by Hageman factor fragments. When Hageman factor was cleaved by streptokinase-activated plasminogen, a 40 Kd fragment was released. In contrast to their interactions with other proteinases, which are blocked by normal C1(-)-inhibitor, Type II C1(-)-inhibitors from plasmas of affected members of eight different kindred with this form of hereditary angioneurotic edema all inhibited the specific coagulant activity of activated Hageman factor to some degree. They did not all form complexes with activated Hageman factor that were stable during sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

scholarly journals Interactions of plasma kallikrein and C1-s with normal and dysfunctional C1(-)-inhibitor proteins from patients with hereditary angioneurotic edema: analytic gel studies

Blood ◽  
1987 ◽  
Vol 69 (4) ◽  
pp. 1096-1101 ◽  
Author(s):  
VH Donaldson ◽  
CJ Wagner ◽  
B Tsuei ◽  
G Kindness ◽  
DH Bing ◽  
...  
Keyword(s):  
Complex Formation ◽  
Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Original Position ◽  
Stable Complex ◽  
Plasma Kallikrein ◽  
Type Ii ◽  
C1 Inhibitor ◽  
Angioneurotic Edema ◽  
Hereditary Angioneurotic Edema

Abstract Purified preparations of normal C1(-)-inhibitor (C1(-)-INH) formed high mol wt complexes with plasma kallikrein that were stable during sodium dodecyl sulfate (SDS)-gel electrophoresis, but most of the dysfunctional C1(-)-INH proteins isolated from plasma of patients with type II hereditary angioneurotic edema (HANE) did not. Two of eight dysfunctional C1(-)-INH proteins were cleaved to lower mol wt forms that were not seen following the reaction of normal C1(-)-INH with equimolar amounts, or less, of plasma kallikrein. Only the higher mol wt component of normal C1(-)-INH (106,000 mol wt) appeared to form a stable complex with the plasma kallikrein, whereas both the 106,000 and 96,000 mol wt forms made stable complexes with C1-s. When a preparation of normal C1(-)-INH containing a homogeneous single band of C1(-)-INH was exposed to C1-s or kallikrein, a “doublet” form evolved in which the heaviest band was in the original position of native C1(-)-INH; C1- s cleavage provided a second band of 96,000; and cleavage by kallikrein, a second band of 94,000 mol wt. We conclude that dysfunctional C1(-)-INH proteins from plasma of persons with type II hereditary angioneurotic edema have impaired interactions with plasma kallikrein and are heterogeneous with respect to these interactions. Moreover, the requirements for the formation of stable complexes between normal C1(-)-INH and plasma kallikrein differed from those for stable complex formation with C1-s. The doublet form of C1(-)-INH, which purified preparations frequently demonstrate, may be due to prior cleavage by C1-s or kallikrein.

scholarly journals Interactions of plasma kallikrein and C1-s with normal and dysfunctional C1(-)-inhibitor proteins from patients with hereditary angioneurotic edema: analytic gel studies

Blood ◽  
1987 ◽  
Vol 69 (4) ◽  
pp. 1096-1101
Author(s):  
VH Donaldson ◽  
CJ Wagner ◽  
B Tsuei ◽  
G Kindness ◽  
DH Bing ◽  
...  
Keyword(s):  
Complex Formation ◽  
Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Original Position ◽  
Stable Complex ◽  
Plasma Kallikrein ◽  
Type Ii ◽  
C1 Inhibitor ◽  
Angioneurotic Edema ◽  
Hereditary Angioneurotic Edema

Purified preparations of normal C1(-)-inhibitor (C1(-)-INH) formed high mol wt complexes with plasma kallikrein that were stable during sodium dodecyl sulfate (SDS)-gel electrophoresis, but most of the dysfunctional C1(-)-INH proteins isolated from plasma of patients with type II hereditary angioneurotic edema (HANE) did not. Two of eight dysfunctional C1(-)-INH proteins were cleaved to lower mol wt forms that were not seen following the reaction of normal C1(-)-INH with equimolar amounts, or less, of plasma kallikrein. Only the higher mol wt component of normal C1(-)-INH (106,000 mol wt) appeared to form a stable complex with the plasma kallikrein, whereas both the 106,000 and 96,000 mol wt forms made stable complexes with C1-s. When a preparation of normal C1(-)-INH containing a homogeneous single band of C1(-)-INH was exposed to C1-s or kallikrein, a “doublet” form evolved in which the heaviest band was in the original position of native C1(-)-INH; C1- s cleavage provided a second band of 96,000; and cleavage by kallikrein, a second band of 94,000 mol wt. We conclude that dysfunctional C1(-)-INH proteins from plasma of persons with type II hereditary angioneurotic edema have impaired interactions with plasma kallikrein and are heterogeneous with respect to these interactions. Moreover, the requirements for the formation of stable complexes between normal C1(-)-INH and plasma kallikrein differed from those for stable complex formation with C1-s. The doublet form of C1(-)-INH, which purified preparations frequently demonstrate, may be due to prior cleavage by C1-s or kallikrein.

INTERACTIONS OF DYSFUNCTIONAL Cl-INHIBITORS FROM PATIENTS WITH TYPE II HEREDITARY ANGIONEUROTIC EDEMA (HANE) WITH ACTIVATED HAGEMAN FACTOR (FACTOR XIIa).

1987 ◽  
Author(s):  
V H Donaldson ◽  
M D B H Mitchell
Keyword(s):  
Normal Serum ◽  
Type Ii ◽  
Inhibitor Protein ◽  
Amidolytic Activity ◽  
Hageman Factor ◽  
Hereditary Angioneurotic Edema ◽  
Coagulant Activity ◽  
Antigenic Properties ◽  
Factor Xiia

Type II HANE is characterized by a deficiency of Cl-inhibitor (Cl-INH) activity in serum which is associated with a dysfunctional inhibitor protein having a normal or increased quantity o|_the antigenic properties of normal serum Cl-inhibitor. Dysfunctional Cl-INH proteins were purified from members_of eight different kindred with Type II HANE and compared to normal Cl-inhibitor with respect to their inhibitory activity directed against the amidolytic and clot-promoting properties of purified activated Hageman factor. All but one dysfunctional Cl-inhibitor blocked the amidolytic activity of ellagic acid-activated Hageman factor; all eight blocked the clot-promoting activity of Hageman factor activated in solutions of sulfatides and BSA. The inhibition _of amidolytic activity was equal to or greater than that of normal Cl-INH (Donaldson, et al., 3. Clin. Invest. 75:124,1985). The impairment of the specific Hageman factor coagulant activity of activated Hageman factor by six^f the eight dysfunctional inhibitors was less than that of the normal Cl-inhibitor, although readily measured. Dysfunctional Cl-inhibitor proteins were also heterogeneous with respect to their formation of stable complexes and their susceptibility to cleavage by Hageman factor activated with BSA-sulfatides when analyzed in SDS-gel electrophoresis. Although these observatons cannot be directly applied to in vivo pathophysiologic changes in plasma, dysfunctional Cl-inhibitors do have the potential of regulating activated Hageman factor.

scholarly journals Synthesis of C1 inhibitor in fibroblasts from patients with type I and type II hereditary angioneurotic edema.

1991 ◽  
Vol 87 (5) ◽  
pp. 1614-1620 ◽  
Author(s):  
J Kramer ◽  
Y Katz ◽  
F S Rosen ◽  
A E Davis ◽  
R C Strunk
Keyword(s):  
Type I ◽  
Type Ii ◽  
C1 Inhibitor ◽  
Angioneurotic Edema ◽  
Hereditary Angioneurotic Edema

Radioimmunoassay for the pyridinoline cross-linked carboxy-terminal telopeptide of type I collagen: a new serum marker of bone collagen degradation

1993 ◽  
Vol 39 (4) ◽  
pp. 635-640 ◽  
Author(s):  
J Risteli ◽  
I Elomaa ◽  
S Niemi ◽  
A Novamo ◽  
L Risteli
Keyword(s):  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Bone Collagen ◽  
Collagen Molecule ◽  
Type I ◽  
Serum Samples ◽  
Amino Terminal ◽  
Wide Range ◽  
Carboxy Terminal

Abstract We developed a radioimmunoassay (RIA) for the carboxy-terminal telopeptides of type I collagen (ICTP), cross-linked with the helical domain of another type I collagen molecule, after isolation from human femoral bone. The cross-linked peptide was liberated by digesting insoluble, denatured bone collagen either with bacterial collagenase or with trypsin, and purified by two successive reversed-phase separations on HPLC, with monitoring of pyridinoline-specific fluorescence. The purity of the peptide was verified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its origin in the type I collagen fibers was determined by amino-terminal amino acid sequencing. Polyclonal antibodies and a separation reagent containing second antibody and polyethylene glycol are used in the RIA. An immunologically identical, somewhat larger antigen is present in human serum; its concentration increases in multiple myeloma and in rheumatoid arthritis. The ICTP antigen seems to be cleared from the circulation by the kidneys, because glomerular filtration rates that are two-thirds of normal or less are associated with increased circulating ICTP concentrations. The CVs of the method are between 3% and 8% for a wide range of concentrations. The analysis of 40 serum samples can be completed in 4 h.

The basophil activation marker defined by antibody 97A6 is identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3

Blood ◽  
2001 ◽  
Vol 97 (10) ◽  
pp. 3303-3305 ◽  
Author(s):  
Hans-Jörg Bühring ◽  
Martina Seiffert ◽  
Christina Giesert ◽  
Anke Marxer ◽  
Lothar Kanz ◽  
...  
Keyword(s):  
Peripheral Blood ◽  
Messenger Rna ◽  
High Performance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Type Ii ◽  
Partial Amino Acid Sequence ◽  
Phosphodiesterase 3 ◽  
293 Cells ◽  
Basophil Cell

Abstract It has recently been shown that monoclonal antibody (MoAb) 97A6 detects a surface antigen expressed on basophils and their CD34+ precursor cells, as well as the basophil cell line KU-812. In this report the partial amino acid sequence of affinity chromatography– and sodium dodecyl sulfate–polyacrylamide gel electrophoresis–separated 97A6 antigen(s) from KU-812 lysates was determined. Sequence alignment of high-performance liquid chromatography–selected tryptic peptides from the resulting 130- and 150-kd bands revealed a 100% identity with amino acids 393 to 405 of ectonucleotide pyrophosphatase/phosphodiesterase-3 (E-NPP3; CD203c) but not of the related ectoenzyme PC-1 (E-NPP1). Moreover, MoAb 97A6 selectively recognized 293 cells transfected with human E-NPP3, but did not react with cells transfected with PC-1 or parental 293 cells. In addition, E-NPP3 messenger RNA expression was detected in basophils but not other peripheral blood cells. Finally, MoAb 97A6 immunoprecipitated phosphodiesterase activity from KU-812 cells and peripheral blood basophils, but not from other cell populations. These data demonstrate that MoAb 97A6 recognizes the functionally active type II transmembrane ectoenzyme E-NPP3.

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