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Biomedical subjects

D Ménaché

Publications and source records attributed to D Ménaché.

At least 19 recordsLinked to original sources
PubMed1985

[PPSB].

PPSB, the plasma derivative which contains the vitamin K-dependent clotting factors, was first produced in 1959 at the Centre National de Transfusion Sanguine in Paris under the leadership of Jean-Pierre Soulier. Today over 20 such products are manufactured around the world. All production methods take advantage of the common adsorption and elution properties of all the vitamin K-dependent clotting factors due to the presence of gamma carboxy residues. Although the clinical use of PPSB has been extended to all congenital and acquired deficiencies of the vitamin K-dependent clotting factors and more recently to treat hemorrhagic episodes of hemophilia A patients with antibody to Factor VIII, the major clinical indication remains hemophilia B. The major complication associated with the use of PPSB is the occurrence of viral diseases, particularly non-A, non-B hepatitis of unknown etiology and specifically associated with the use of PPSB is the occurrence in some patients of thromboembolic complications. Current research is oriented toward the production of a safer product.

Blood Coagulation Factors↗
PubMed1981

Congenital abnormal fibrinogens.

Congenital and hereditary abnormal fibrinogen is the most common of the inherited disorders of fibrinogen. There is no uniform clinical pattern which characterizes the disease and the diagnosis is evoked on the results of laboratory tests which show an abnormal conversion of fibrinogen to fibrin. This abnormality should be confirmed on the purified defective fibrinogen. Characterization of the abnormality includes physical, immunological, functional and structural analyses. Studies related to fibrinogen behavior upon plasmin digestion and those related to polymerization also provide useful information. Recognition of the specific nature of the molecular defect is dependent on molecular analysis. A single distinctive amino acid substitution is currently recognized for Fibrinogen Detroit, Lille and München.

Blood Coagulation Disorders↗
PubMed1980

A survey of the effectiveness of prothrombin complex concentrates in controlling hemorrhage in patients with hemophilia and anti-Factor VIII antibodies.

The treatment of patients with hemophilia A and anti-Factor VIII antibodies is difficult. Between July 1977 and June 1978, a survey was carried out by an ad hoc working party of the subcommittee on Factor IX concentrates of the International Committee on Thrombosis and Hemostasis to assess the effectiveness of Prothrombin Complex Concentrates in controlling hemorrhage in these patients. The results are presented in this paper and, although subjective, support the view that these concentrates are not as effective in patients with inhibitors as Factor VIII concentrates are in patients without inhibitors.

Antibodies↗
PubMed1980

Electron microscopy of fibrin Paris I.

Fibrinogen Paris I, a congenital fibrinogen abnormality, is characterized by delayed fibrin aggregation and poor clot retraction owing to the replacement of normal gamma-chains by mutant gamma-chains, which are termed gamma-Paris I. Available evidence indicates that the structural abnormality involves the amino acid sequence near the COOH-terminus of the mutant chain and probably includes the region containing the normal gamma-chain crosslinking site. Electron microscopy was carried out on Paris I fibrin. In place of the normally interwoven network of branching cross-striated fibers, negatively or positively contrasted Paris I fibrin was characterized by nonfibrous clumps of material connected by distince fibrous strands tending to be thinner and more irregular in width than normal fibrin. Most Paris I fibrin fibers tended to the aperiodic, although cross-striations were observed occasionally in negatively contrasted specimens and rarely in positively contrasted specimens. In addition, Paris I fibrin frequently showed relatively short, abruptly terminating fibers. The gross ultrastructural differences between normal and Paris I fibrin suggest that for fibrin assembly to take place normally, a region(s) in the fibrin molecule near to or possibly overlapping the COOH-terminal gamma-chain crosslinking site must be preserved or at least not sterically hindered.

Amino Acid Sequence↗
PubMed1979

Congenital deficiency of blood clotting factors II, VII, IX, and X.

A patient congenitally deficient in factors II, VII, IX, and X has been further investigated after a follow-up of 15 yr. At birth, these factors, when determined by clotting assays, were undetectable. Following therapy with vitamin K1, the clotting activity of these factors rose but never exceeded 18% of normal. Immunologic assays revealed much higher levels of these factors than did clotting assays, thus suggesting that the vitamin-K-dependent factors were present in abnormal forms. Two-dimensional crossed immunoelectrophoresis showed that at least two forms of prothrombin were present in the patient's plasma. One form was similar to normal prothrombin; the other had the same mobility as acarboxyprothrombin. In addition, the majority of this fast-migrating peak was not adsorbable onto insoluble barium salts. These observations suggested that some molecules of the patient's prothrombin lacked the normal complement of gamma-carboxyglutamic acid residues. This observation was confirmed by a specific assay for gamma-carboxyglutamate. Since malabsorption of vitamin K, warfarin intoxication, and hepatic dysfunction were excluded as causes of this patient's syndrome, this rare congenital abnormality could represent either a defective gamma-carboxylation mechanism within the hepatocyte or faulty vitamin K transport.

Adolescent↗
PubMed1977

Haemostatic disorders and respiratory distress in the newborn.

Coagulation and fibrinolysis studies were performed on 64 newborns; 16 premature infants with hyaline membrane disease (HMD), 17 newborns with other forms of respiratory distress syndrome (RDS) (8 of them were premature), 31 healthy newborns (11 of them were premature). All the babies were studied once in the first 48 hours of life. There was no significant difference between sick and healthy babies for 5 parameters; platelet count, factor VIII, fibrinogen, fibrin(ogen) degradation products, euglobulin lysis time. Factor II, VII and X were low in all infants, and premature infants had significantly lower levels compared to full term newborns. Factor V, plasminogen, alpha 2 macroglobulin (alpha 2M) and antithrombin III (AT III) levels were significantly lower in sick infants. Except for AT III, these deficiencies were not related to prematurity. No significant difference was found between HMD and other RDS. Of the 33 sick infants, 5 developed laboratory findings consistent with disseminated intravascular coagulation (DIC). The results indicate that the coagulation and fibrinolytic abnormalities reported are not specific to HMD.

Antithrombins↗
PubMed1976

Studies on the structural abnormality of fibrinogen Paris I.

The structural properties of an inherited fibrinogen abnormality designated fibrinogen Paris I were investigated. Dodecyl sulfate gel electrophoresis of unreduced samples revealed no discernible differences in molecular weight from normal; this implied that in fibrinogen Paris I, the normal fibrinogen architecture of six covalently linked chains per molecule is preserved. Examination of dithiothreitol reduced samples before and after treatment with Reptilase or thrombin revealed that the Aalpha- and Bbeta-chains could release the A and B peptides, respectively. A mutant chain (mol wt 52,500, termed gammaParis I) which replaces a large proportion of gamma-chains (mol wt 49,400) was shown, like normal gamma-chains, to lack thrombin- and Reptilase-sensitive sites. The gamma-chains and alpha-chains of Paris I fibrin underwent Factor XIIIa-catalyzed cross-linking slowly; this behavior was not attributable to an intrinsic abnormality of these chains themselves but rather to the inhibitory effect of the mutant gammaParis I chains on this process. Results of DEAE-cellulose gradient elution chromatography of Paris I fibrinogen preparations revealed the presence of small amounts of normal fibrinogen molecules and also indicated that the gammaParis I chains possessed structural overlap with gamma-chains. Unlike gamma-chains however, the gammaParis I chains did not incorporate dansylcadaverine in the prescence of Factor XIIIa, nor, as previously reported, did they undergo cross-linking. The observations indicate that the amine acceptor site found in the COOH-terminal region of the gamma-chain is either not present on the gammaParis I chain or is unavailable for cross-linking. Further support for localization of the abnormality in the COOH-terminal region of the molecule was obtained from the observation that during plasmic hydrolysis of Paris I fibrinogen, at least one unique form of core Fragment D (DParis I) was evolved, whereas Fragment E did not differ from normal.

Amines↗