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At least 1,549 records · Page 86Linked to original sources
PubMed1977

[Study by means of enzymatic and immunochemical determination of Cl esterase inhibitor in 59 patients with hereditary angioneurotic edema].

Serum C1 esterase inhibitor was determined in 138 members of 18 italian families with hereditary angioedema by immunochemical and enzymatic assays. On the basis of quantitative and functional findings, the type A of hereditary angioedema was diagnosed in 44 subjects, and the type B in 15. Some technical devices concerning serum sample handling were identified. The influence of heparin, EDTA, and citrate on C1 esterase inhibitor activity of normal plasma was also investigated.

Adult↗
PubMed1993

A modification of an affinity procedure for purification of human C1- inhibitor that provides a homogeneous stable preparation.

Human C1- inhibitor can be rapidly purified by the affinity chromatography procedure described by Pilatte and his associates (1989), but the inhibitor so purified breaks down during storage or is in a cleaved form when initially purified. By adding an ion-exchange chromatography procedure after the affinity chromatography, a stable, single species of C1- inhibitor molecules is obtained. It is likely that serine proteinases in trace amounts, which may be complexed with some of the C1- inhibitor, are removed during the ion-exchange procedure. This procedure provides a highly purified and useful preparation of C1- inhibitor.

Chromatography, Affinity↗
PubMed1997

[Efficient expression of human C1-inhibitor in CHO cells by using a dicistronic expression vector].

The full-length cDNA fragment encoding human C1-INH was obtained by gene recombination techniques and a stable expression plasmid was constructed by inserting the human C1-INH cDNA into an efficient dicistronic expression vector pED. This plasmid was transfected into DHFR-deficient Chinese Hamster Ovary cells (CHO-dhfr-) by Lipofectin method, and the positive CHO-dhfr+ cell clones which stably express C1-INH was generated. Expression of C1-INH mRNA was detected by Northern blot. Expression of C1-INH protein was confirmed by immunoprecipitation and Western blot analysis. The level of expressed C1-INH was estimated at 0.4 microgram/ml by specific ELISA techniques. The biological activity of recombinant C1-INH was assayed by using the inhibition of C1 estrolytic activity.

Animals↗
PubMedDate not supplied

[Effect of Yersinia pseudotuberculosis pVM82 on the activity of components of complement and phagocytosis by human blood neutrophils].

Three isogenic Y. pseudotuberculosis strains were studied. One of them contained pVM82 plasmid which was found in foci of pseudotuberculosis outbreaks and increased Yersinia resistance to blood serum. Cells with pVM82 plasmid did not inhibit the activation of complement components C1, C2, C3, C4, and C5 in human serum and increased the consumption of these complement components in comparison with control strains. Y. pseudotuberculosis cells with pVM82 were better resistant to human neutrophil phagocytosis than bacterial cells without this plasmid. For the strain with pVM82 plasmid, a lower level of phagocytosis within the first 30 min of Y. pseudotuberculosis incubation with neutrophils and a reduced percentage of killed bacteria among all those phagocytosed over the entire period of incubation of bacteria with neutrophils were observed.

Complement System Proteins↗
PubMed1991

[Hereditary angioedema, a rare cause of recurrent abdominal pains. A report of 2 clinical cases and comments of a general nature].

Two clinical cases of recurrent abdominal pain are reported. These led to the unusual diagnosis of hereditary angioedema due to deficiency of C1 esterase inhibitor (C1-INH). The difficulties of identifying this genetic disease were caused by the variability of its clinical expression: the alteration of an autosomal dominant gene triggers angioedema attacks that may strike the cutaneous, gastroenteric and respiratory apparatus with differing intensity. Various subjects suffering from hereditary angioedema were found in the genealogical trees of the two patients, but all had extraintestinal symptoms of very variable intensity. Measurement of C4 and C1-INH made it is possible to identify in the first family a functional defect of C1 esterase inhibitor and in the second a quantitative defect in the same inhibitor.

Abdominal Pain↗
PubMed1984

[Hereditary angioneurotic edema: a molecular disease caused by a defect in the O-glycosylation of C1 esterase inhibitor (C1-INH)].

A quantitative and qualitative study of neutral and aminosaccharides in C 1-esterase inhibitor (C 1-INH), protein of the complement system, was performed. We observe a mixed glycosylation of the molecule with an N-glycosylated: O-glycosylated chain ratio of 1: 4. The loss of the inhibitory activity of the molecule in hereditary angioedema (O ANH) is associated with an O-glycosylation deficiency which differs according to the two molecular variants: C 1-INH (1 A) and C 1-INH (II) previously described.

Angioedema↗
PubMed1997

Regulation of C1-inhibitor function by binding to type IV collagen and heparin.

Serpins inhibit proteinases by a branched pathway, in which an intermediate serpin-proteinase complex can either form a stable covalent serpin-proteinase complex or produce reactive center cleaved serpin in a substrate reaction. It was tested whether these competing reactions could be regulated for the serpin C1-inhibitor by ligand binding. C1-inhibitor bound to type IV collagen, laminin, and entactin. Type IV collagen (10 microg/ml) caused an increase in the stoichiometry of inhibition for C1s inhibition by C1-inhibitor to 1.48 from 1.09 in the absence of ligand. A dose-dependent increase in the stoichiometry up to 1.27 in the presence of 100 microg/ml heparin was also observed. At low ionic strength the stoichiometry increased to 2.55. These data provide the first report that C1-inhibitor can bind to type IV collagen and also show that C 1-inhibitor can be regulated by ligand binding.

Binding, Competitive↗
PubMed1987

Serum activity of C1 inactivator in Duchenne-type progressive muscular dystrophy.

We previously found that the level of the immunoreactive activity of C1 inactivator in the plasma Duchenne-type patients with progressive muscular dystrophy was lower than that in normal boys. Therefore, we investigated the level of the C1 inactivator inhibiting activity against C1 esterase in the serum from PMD patients. The mean level of anti-esterase activity of C1 inactivator against C1 esterase in the serum from PMD was 50% lower than that of the control group (P less than 0.05).

Adolescent↗