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Results for “Complement C1 Inhibitor Protein”

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PubMed1980

C1 esterase inhibitor protein associated with human cancer: a tumour marker.

The concentration of a cancer-associated serum C1 esterase inhibitor protein was determined in 194 cases of human cancer, grouped according to their clinical activity. As control groups healthy blood donors and patients having non neoplastic chronic lung and liver diseases were included in the study. The results showed highly significant differences when the values obtained for "active" malignant tumors were compared with the two control groups and the quiescent tumours. The authors conclude that C1 esterase inhibitor protein measurement may be useful as a clinical tumour marker.

Complement C1 Inactivator Proteins↗
PubMed1997

Angioedema and swellings of the orofacial region.

OBJECTIVE: Patients may have various forms of angioedema and require dental treatment which can cause or contribute to the onset of an episode of angioedema. This paper seeks to highlight the causes and the management of this serious condition. DESIGN: An outline of the different types of angioedema is given here, along with three case reports which illustrate treatment and management. SUBJECTS AND METHODS: Three patients who presented to an Oral Medicine clinic with angioedema are presented to illustrate various types of angioedema and the different contributing factors that precipitated episodes of the condition. MAIN OUTCOME MEASURES: The three patients were all investigated for biochemical and allergic factors which may have caused their disease. RESULTS: Both drugs and dental materials were shown to be involved in the pathogenesis of angioedema in this short series of patients. CONCLUSIONS: Dental treatment or the use of some materials may promote or contribute to the disorder. Referral to hospital for specialist care is indicated for certain groups of patients who require invasive dental treatment. The multi-disciplinary team approach in the investigation and management of patients with angioedema is emphasised.

Aged↗
PubMed1983

Plasma protease inhibitors in premature infants: influence of gestational age, postnatal age, and health status.

In newborn infants, the influence of gestational age (GA), postnatal age (PA), and health status on the plasma protease inhibitors alpha 2-macroglobulin (alpha 2-M), alpha 1-antitrypsin (alpha 1-AT), C1 esterase inhibitor (C1E-INH), alpha 2-antiplasmin (alpha 2-AP), and antithrombin III (AT-III) was investigated. Inhibitor levels were measured by radial-immunodiffusion and expressed as a percentage of pooled plasma from adults (mean +/- SEM). In total, 54 premature infants (28-36 weeks gestation) were classified at birth as healthy (N = 22) (IV fluids, antibiotics only) or sick (N = 32) (all other support, but excluding infants with disseminated intravascular coagulation (DIC] and studied on Days 1 and/or 7 of life. Healthy term infants (N = 18) and infants with DIC (N = 10) were studied on Day 1 only. All inhibitors except C1E-INH increased with increasing gestational age (P less than 0.01). In healthy premature infants all inhibitor levels reached the normal adult range by 1 week of age. In contrast, at 1 week of age, sick infants had lower levels of alpha 2-M and alpha 2-AP, and higher levels of alpha 1-AT compared to healthy infants (P less than 0.01). The presence of DIC depressed all of the inhibitors on Day 1 except alpha 1-AT when compared to healthy controls (P less than 0.01). Thus, gestational age, postnatal age, and health status all significantly influenced the levels of these plasma protease inhibitors.

Antithrombin III↗
PubMed1982

Mouse plasma trypsin inhibitors: inhibitory spectrum of contrapsin and alpha-1-antitrypsin.

We have studied the effects of murine alpha-1-antitrypsin and contrapsin, a new trypsin inhibitor (Takahara, H. and Sinohara, H. (1982) J. Biol. Chem. 257, in press), on several serine proteases participating in blood clotting, fibrinolysis, kinin generation, and complement activation. Bovine plasmin and human plasma kallikrein were inactivated by contrapsin but not by alpha-1-antitrypsin, whereas bovine alpha-thrombin and porcine pancreas kallikrein were inhibited by alpha-1-antitrypsin but not by contrapsin. Heparin protected thrombin from inactivation by alpha-1-antitrypsin. Both inhibitors had virtually no effects on canine C1 esterase.

Animals↗
PubMed1975

Distinction between hereditary and acquired angioneurotic oedema according to the complement system.

It is often impossible to make a clinical distinction between acquired and hereditary acute angioneurotic oedema. Investigation of the complement system is indispensable for this diagnosis to be established. The value of total complement and C4 and C2 are lowered in the sera in the hereditary form (44 cases) and normal in the acquired type (68 cases). The use of tests for the activation of C1 esterase "in vitro" is useful to distinguish these two types of oedema as has been demonstrated by the formal measurement of C1 esterase inhibitor.

Angioedema↗
PubMed1985

Platelet C1- inhibitor. A secreted alpha-granule protein.

In order to characterize which proteins of the contact phase of coagulation interact with platelets, human platelets were studied immunochemically and functionally to determine if they contain C1- inhibitor. By means of monospecific antibody to C1- inhibitor, a competitive enzyme-linked immunosorbent assay (CELISA) was developed to measure directly platelet C1- inhibitor. With the CELISA, from 33 to 115 ng of C1- inhibitor antigen per 10(8) platelets from 15 normal donors was quantified in lysates of washed human platelets solubilized in nonionic detergent. The mean concentration in 10(8) platelets was 62 +/- 33 ng (SD). Plasma C1- inhibitor either in the platelet suspension medium or on the surface of the platelets could account for only from 6.5 to 16% of the total antigen measured in the solubilized platelets. Upon functional studies, platelets contained 84 +/- 36 ng (SD) of C1- inhibitor activity in 10(8) platelets. As assessed by the CELISA, platelet C1- inhibitor antigen was immunochemically identical to plasma and purified C1- inhibitor. In contrast, the mean concentration of platelet C1- inhibitor antigen in platelets from four patients with classical hereditary angioedema was 8.3 ng/10(8) platelets (range, 5.3 to 11.3 ng/10(8) platelets). 25 and 31% of the total platelet C1- inhibitor was secreted without cell lysis from normal platelets after exposure to collagen (20 micrograms/ml) and thrombin (1 U/ml), respectively, and this secretion was blocked by metabolic inhibitors. Platelet subcellular fractionation showed that platelet C1- inhibitor resided mostly in alpha-granules, similar to the location of platelet fibrinogen. Thus, human platelets contained C1- inhibitor, which became available by platelet secretion. The identification of platelet C1- inhibitor suggests that platelets may modulate the activation of the proteins of early blood coagulation and the classical complement pathways.

Blood Platelets↗
PubMed1987

The complement system in type 1 (insulin-dependent) diabetes.

The complement proteins C1q, r, s, C2, C4, C3, factor B, C5, C6, and the inhibitors, C1 inhibitors, factors I and H were measured in 35 patients with recently diagnosed Type 1 (insulin-dependent) diabetes, 76 patients with longer-duration disease (30 with complications) and 43 first-degree healthy relatives. We found that C1q, C4 and C3 were reduced significantly in all groups of patients (p less than 0.001 for each protein in recent onset and uncomplicated patients; p less than 0.01, p less than 0.01 and p less than 0.05 respectively, for patients with complications) compared to 60 control subjects and that C4 was also reduced in healthy relatives (p less than 0.001). C4 allotypes were examined in 63 subjects (selected from the patient groups) in order to clarify the role of null alleles in the production of the C4 abnormality. These showed serum C4 to be reduced significantly in 50 patients without null alleles (patient mean 0.24 g/l; control subject mean 0.34 g/l) (p less than 0.0001), although levels were lowest in the 13 patients with one or more null alleles (mean 0.19 g/l). Finally, to examine the metabolic basis for the low concentrations of C4 and C3, the turnover of highly-purified, radiolabelled C4 and C3 was measured in seven recently diagnosed patients; four of these had low levels of C4. The data showed that three out of four of these patients had reduced synthesis of C3 and C4 and normal values for fractional catabolic rate. Two patients showed features of C4 hypercatabolism. We conclude that several early complement proteins are reduced in Type 1 diabetes, irrespective of duration or complications.(ABSTRACT TRUNCATED AT 250 WORDS)

Adolescent↗
PubMedDate not supplied

[The immunological reactivity indices (the humoral component) in persons in contact with mycotoxin-contaminated food products].

Blood serum levels of immunoglobulins (IgG, IgA, IgM, IgD, IgE), concentration of complement components (C1-inhibitor, C3, C4, C5, C9) as well as the content of some protein fractions (transferrin, ceruloplasmin, haptoglobin, orosomucoid, alpha 1-antitrypsin, alpha 2-macroglobulin, albumin and prealbumin) in the plasma were assayed in subjects exposed (due to their occupational necessity) to food raw materials (wheat, corn, barley, combined fodder) contaminated with mycotoxins. A total of 50 subjects, who have been working from 1 to 15 years at grain-treating factories, were investigated. It has been shown that a long-term exposure to food and fodder products containing mycotoxins induces a growth of IgE level attended by a drop in IgG content, and a decrease in the concentration of the complement components C3 and C9, transferrin and orosomucoid.

Antibody Formation↗
PubMed1975

Protease inhibitors in plasma of patients with chronic urticaria.

The hypothesis that deficiencies of plasma protease inhibitors might play a role in the pathogenesis of chronic urticaria was evaluated. Plasma levels were measured in patients with urticaria and a matched control group for alpha1-antitrypsin, alpha2-macroglobulin, total trypsin-inhibiting capacity, kallikrein-inhibiting capacity, and the complement factors C1 esterase inhibitor, C3, and C4. A total of 92 patients with chronic urticaria or more than three months' duration was studied. Patients with acquired cold urticaria had significantly decreased levels of alpha1-antitrypsin and total antitrypsin activity. In patients with acquired angioneurotic edema, alpha1-antitrypsin levels and antichymotrypsin activities were lowered, with less significant decreases in anti-trypsin and antikallikrein activities. Levels of C1 esterase inhibitor , C3, and C4 were normal in all groups. There was no correlation between the increased sensitivity to intracutaneously administered kallikrein injection and deficiencies of of protease inhibitors.

Adolescent↗
PubMedDate not supplied

Mechanism of complement activation during extracorporeal blood-biomaterial interaction: effects of heparin coated and uncoated surfaces.

In vitro studies with miniaturized rotating circuits and heparinized human blood, as well as long-term extracorporeal membrane oxygenation with either heparin coated (HBS) or uncoated surfaces connected to adult sheep, were performed comparing the impact on complement activation in blood and on surfaces. Analysis of surface bound complement proteins revealed significantly reduced binding of activated C3 and C5b-9 to HBS in vitro, compared with uncoated surfaces, which was probably due to more HBS bound complement inhibitors (C1-Inhibitor, factor H) being present. This was reflected by significantly reduced activation of the alternative pathway (C3bBbP) and terminal complex (SC5b-9) by HBS but slightly increased levels of classic pathway complex (C1rs-C1-inhibitor). These results were confirmed during in vivo study by analysis of hemolytic complement function, activation specific C3 derived split products, and surface bound complement proteins. Increased binding of complement regulators to HBS appears to effectively reduce complement activation by biomaterials, leading to improved long-term biocompatibility.

Animals↗
PubMed1983

Blood levels of proteinase inhibitors in pre-eclampsia.

The blood levels of alpha 2-macroglobulin, alpha 1-antitrypsin, CT inactivator, antithrombin III and alpha 2-antiplasmin were measured in 18 primigravidae with moderate or severe pre-eclampsia and in 18 gestation-matched primigravidae with uncomplicated pregnancy. The mean levels of the proteinase inhibitors did not differ between the pre-eclampsia and uncomplicated pregnancy groups.

Adolescent↗