C1 Inhibitor and Hereditary Angioneurotic Edema

1988 ◽  
Vol 6 (1) ◽  
pp. 595-628 ◽  
Author(s):  
A E Davis
Keyword(s):  
C1 Inhibitor ◽  
Angioneurotic Edema ◽  
Hereditary Angioneurotic Edema

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 Transinhibition of C1 inhibitor synthesis in type I hereditary angioneurotic edema.

1993 ◽  
Vol 91 (3) ◽  
pp. 1258-1262 ◽  
Author(s):  
J Kramer ◽  
F S Rosen ◽  
H R Colten ◽  
K Rajczy ◽  
R C Strunk
Keyword(s):  
Type I ◽  
C1 Inhibitor ◽  
Angioneurotic Edema ◽  
Hereditary Angioneurotic Edema

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 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.

scholarly journals Plasma levels of C1- inhibitor complexes and cleaved C1- inhibitor in patients with hereditary angioneurotic edema.

1990 ◽  
Vol 85 (4) ◽  
pp. 1215-1220 ◽  
Author(s):  
M Cugno ◽  
J Nuijens ◽  
E Hack ◽  
A Eerenberg ◽  
D Frangi ◽  
...  
Keyword(s):  
Plasma Levels ◽  
C1 Inhibitor ◽  
Angioneurotic Edema ◽  
Hereditary Angioneurotic Edema

scholarly journals Nonsense mutations affect C1 inhibitor messenger RNA levels in patients with type I hereditary angioneurotic edema.

1991 ◽  
Vol 88 (3) ◽  
pp. 755-759 ◽  
Author(s):  
D Frangi ◽  
M Cicardi ◽  
A Sica ◽  
F Colotta ◽  
A Agostoni ◽  
...  
Keyword(s):  
Messenger Rna ◽  
Type I ◽  
C1 Inhibitor ◽  
Angioneurotic Edema ◽  
Nonsense Mutations ◽  
Hereditary Angioneurotic Edema ◽  
Rna Levels

DECRIPTION OF A HEREDITARY ANGIONEUROTIC EDEMA FORM IN A CHILD

2020 ◽  
pp. 46-54
Author(s):  
Tatyana S. Lutkova ◽  
Luiza M. Karzakova ◽  
Nadezhda D. Ukhterova ◽  
Nadezhda V. Zhuravleva ◽  
Nataliya P. Andreeva ◽  
...  
Keyword(s):  
Differential Diagnostics ◽  
C1 Inhibitor ◽  
C1 Inhibitor Deficiency ◽  
Angioneurotic Edema ◽  
Congenital Deficiency ◽  
Treatment And Prevention ◽  
Hereditary Angioneurotic Edema ◽  
Dominant Disease ◽  
Genetic Examination

Congenital deficiency of the C1-component inhibitor of the complement cascade, or hereditary angioneurotic edema, is a rare autosomal dominant disease due to a mutation in the human C1-esterase inhibitor. Caused by C1 deficiency unregulated cleavage of high molecular weight plasma kininogen results in excess production of a mediator with vasodilating action – bradykinin. Hereditary type 1 angioedema develops as a result of C1 inhibitor deficiency, while type 2 is caused by decreased C1 inhibitor activity. The disease manifests itself in childhood or adolescence as recurrent episodes of edema in the skin, subcutaneous fiber and mucous membranes. Localization of edemas in the submucous layer of the larynx represents a threat to life, which can lead to the development of laryngostenosis and acute respiratory failure. The article describes a case of hereditary angioneurotic edema in a girl, which manifested in early childhood. There were no great difficulties in diagnosing the disease, as patients with this pathology were already identified earlier in the family. A significant reduction in C1-inhibitor content was found in the patient, which made it possible to clarify the type of hereditary angioneurotic edema and to categorize it to type 1. A synthetic antifibrinolytic agent with the ability to block kinins and angioneurotic edemas was successfully used in the treatment and prevention of swelling attacks in the patient. The analysis of the case shows that hereditary angioneurotic edema remains a problem difficult enough for a practical doctor requiring careful history taking, assessment of disease development dynamics and performing a laboratory – genetic examination. In most cases, only differential diagnostics can give the opportunity to suspect the dangerous pathology in the patient in a timely manner which requires immediate hospitalization and providing aid adequate to the disease.

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