Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “AFIBRINOGENEMIA”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,153 records · Page 64Linked to original sources
PubMed1976

[Resolution of Bbeta and gamma chains from normal human fibrinogen Zürich II into 2 variants with each differing sialic acid content].

The gamma- and Bbeta-polypeptide chains of purified human fibrinogen (both pooled and single donor) have each been resolved into 2 major components: gammaL and gammaR, and BbetaL and BbetaR. They are similar in molecular weight (SDS-PAGE), but differ in sialic acid content, which approximates 2 and 1 residues per molecular of polypeptide in the L- and R-components respectively. Tryptic peptide maps of the L-and R- forms of the gamma chain showed differences within the small group of peptides containing the sialic acid residues. No differences between the peptide maps of BbetaL- and BbetaR-chains were found . A larger ratio of L:R in the gamma- and Bbeta-chains of dysfibrinogenemia fibrinogen "Zürich II" explains the higher content of sialic acid measured in the unmodified Zürich II fibrinogen molecule.

Afibrinogenemia↗
PubMed1999

Fibrinogen St. Gallen I (gamma 292 Gly--> Val): evidence for structural alterations causing defective polymerization and fibrinogenolysis.

Fibrinogen St. Gallen I was detected in an asymptomatic Swiss woman. Routine coagulation tests revealed a prolonged thrombin and reptilase time. Functionally measured fibrinogen levels were considerably lower than those determined immunologically. Polymerization of fibrin monomers derived from purified fibrinogen was delayed in the presence of either calcium or EDTA. Normal fibrinopeptide A and B release by thrombin was established. An abnormal degradation of fibrinogen St. Gallen I by plasmin was observed. Fragment D1 of normal fibrinogen was fully protected against further proteolysis in the presence of 10 mM calcium, whereas fibrinogen St. Gallen I was partially further degraded to fragments D2 and D3. In the presence of 10 mM EDTA, the conversion of variant fragment D1 to D2 was accelerated whereas the degradation of fragment D2 to D3 was delayed in comparison to degradation of fragments D1 and D2 of normal fibrinogen. Three high-affinity calcium binding sites were found in both normal and variant fibrinogen. Mutation screening with SSCP analysis suggested a mutation in exon VIII of the gamma-chain gene. Cycle sequencing of this gene portion revealed a single base substitution from G to T of the base 7527, leading to replacement of gamma 292 glycine by valine. The same mutation has already been described for the fibrinogen variant Baltimore I. Molecular modeling was performed of a part of the gamma-chain containing the mutation site, based on recently published X-ray crystal structures of human fibrinogen fragment D and of a 30 kD C-terminal part of the gamma-chain. Significant structural alterations due to the substitution of glycine by valine at gamma 292 were observed, e.g. spreading of the protein backbone, probably leading to a modified accessibility of the plasmic cleavage sites in the gamma-chain at 356 Lys and 302 Lys. A shift of gamma 297 Asp that is involved in interactions of fragment D with the Gly-Pro-Arg-Pro-peptide was noted by molecular modeling. The latter observation is compatible with delayed polymerization of fibrin monomers.

Abortion, Spontaneous↗
PubMed1976

[Concentrated antihemophilic globulin in the treatment of hemorrhagic syndromes].

The author presented the general informations on the preparation of the Factor VIII and Factor IX concentrates, on their use and side effects. Special attention was paid to the resolutions of the Scientific group on the Inherited Blood Clotting Disorders, in the meeting of the World Health Organization, which was held in Geneva, 1972.

Afibrinogenemia↗
PubMedDate not supplied

[Effect of antithrombin III on anticoagulating system function in animals intravenously injected with tissue thromboplastin].

In experiments with rats, antithrombin III (a natural inhibitor of fibrinolysis) was shown to decrease the activation of the anticoagulation system either in prophylactic administration or during the development of thrombogenesis, caused by intravenous administration of tissue thromboplastin. The phenomenon led to the maintaining of the more high content of fibrinogen in blood of experimental animals, to the shortening of the thrombin time and to the increase in content of alpha2-macroglobulin and alpha1-antitrypsin (in-hibitors of fibrinolysis) as compard with control animals, administered with the only thrombolastin. Effect of antithrombin III depended on periods of administration of the prearation and on injection of tissue thromboplastin.

Afibrinogenemia↗
PubMed1999

Hypofibrinogenemia associated with a heterozygous missense mutation gamma153Cys to arg (Matsumoto IV): in vitro expression demonstrates defective secretion of the variant fibrinogen.

We genetically analyzed a case of hypofibrinogenemia that showed no bleeding or thrombotic tendency. Direct sequencing of a polymerase chain reaction-amplified gamma-chain gene segment showed a novel nucleotide substitution. This heterozygous mutation encodes both Cys (TGT) and Arg (CGT) at residue 153. To examine the basis for the fibrinogen deficiency, we prepared expression vectors containing mutant gamma-chain DNAs encoding gamma153R and gamma153A for in vitro expression in Chinese hamster ovary (CHO) cells. Enzyme-linked immunosorbent assay and immunoblot analysis of the culture media and cell lysates showed that CHO cells transfected with gamma153R or gamma153A synthesized the variant gamma-chain, but did not secrete variant fibrinogen into the culture medium. Metabolic pulse-chase experiments showed that fibrinogen assembly was impaired when either variant gamma-chain was expressed. In cells expressing normal fibrinogen, assem- bly intermediates and intact fibrinogen were seen in cell lysates prepared after short (3 minutes) or long (1 hour) incubation with (35)S-methionine. Neither intermediates nor intact fibrinogen was seen with the variant gamma-chains. These data suggest that gamma-chains have an important early role in fibrinogen assembly. Thus, our results support the model for fibrinogen assembly proposed by Huang et al (J Biol Chem 268:8919, 1993), in which the first step in assembly is the formation of alphagamma or betagamma dimers, or both. This model implies that gammaCys153 has a critical role in the formation of these early assembly intermediates. We concluded that the gamma153Cys-->Arg substitution does not allow fibrinogen assembly and secretion, and this is manifest in vivo as a fibrinogen deficiency. We designated this variant as fibrinogen Matsumoto IV.

Adult↗