Un nouveau Cas d’Anomalie constitutionnelle et familiale du Fibrinogène sans Diathese hémorragique

Streiff, F; Alexandre, P.; Vigneron, C.; Soria, Javier Millán; Soria, C; Mester, L.

doi:10.1055/s-0038-1653709

Cited by 15 publications

(8 citation statements)

References 9 publications

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“…Abnormalities ofthe carbohydrate moiety of the fibrinogen molecule have been described in several of the genetic dysfibrinogenemias, including fibrinogens Nancy and Paris 11 (10). Both fibrinogens Nancy and Paris 11 are reported to have an increased sialic acid content and both are functionally characterized by an abnormality of fibrin monomer polymerization (13,14). We have studied the purified fibrinogen of 12 patients with the dysfibrinogenemia associated with liver disease, and have demonstrated that this abnormal fibrinogen has an increased sialic acid content ranging from 12.7 to 71.4% higher than the normal control.…”

Section: Discussionmentioning

confidence: 99%

Abnormal sialic acid content of the dysfibrinogenemia associated with liver disease.

Martinez¹,

Palascak²,

Kwasniak³

1978

J. Clin. Invest.

114

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A B S T R A C T To evaluate the possibility that the carbohydrate composition of fibrinogen may be altered in the dysfibrinogenemia associated with liver disease, we studied the sialic acid content of purified fibrinogen from 12 patients with liver disease and its relationship to the prolongation of the thrombin time. Purified fibrinogen showed intact Aa-, Ba8-, and y-chains when reduced and analyzed by sodium dodecyl sulfatepolyacrylamide gel electrophoresis and exhibited prolongation of the thrombin time similar to that of the plasma from which it was derived. Sialic acid content of the purified fibrinogen ranged from 12.7 to 71.4% higher in patient fibrinogens when compared to normal controls. A progressive delay in thrombin time was associated with increasing sialic acid content of the patient fibrinogen. Enzymatic removal of sialic acid from four of the abnormal fibrinogens resulted in a shortening of their thrombin times to the range of the desialylated normal control. Periodic acid-Schiff reagent stained only the B,8-and y-chains of the reduced patient fibrinogens after sodium dodecyl sulfate-polyacrylamide gel electrophoresis suggesting that the excess sialic acid is located on these two chains. These studies demonstrate a biochemical alteration of the functionally abnormal fibrinogen fouind in some patients with liver disease, and indicate that the excess sialic acid plays an important role in the ftunctional defect of this protein.

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Section: Discussionmentioning

confidence: 99%

Abnormal sialic acid content of the dysfibrinogenemia associated with liver disease.

Martinez¹,

Palascak²,

Kwasniak³

1978

J. Clin. Invest.

114

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“…Clinical expression of the defect is variable, ranging from no clinical manifestations (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11), to bleeding (9,(12)(13)(14)(15)(16)(17)(18)(19)(20) and even thrombotic episodes (14,20,21). Wound dehiscence also has been reported (1,3).…”

Section: Introductionmentioning

confidence: 99%

Fibrinogen Philadelphia. A hereditary hypodysfibrinogenemia characterized by fibrinogen hypercatabolism.

Martinez

Holburn²,

Shapiro³

et al. 1974

J. Clin. Invest.

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A B STR A CT A new, autosomally inherited abnormal fibrinogen associated with hypofibrinogenemia has been described in several members of a family. Plasma fibrinogen measured either as thrombin-clottable protein or by immunodiffusion revealed a fibrinogen level ranging between 60 and 90 mg/100 ml. The thrombin time of plasma or purified fibrinogen was prolonged and only partially corrected by the addition of calcium. Purified fibrinogen prolonged the thrombin time of normal plasma. Fibrinopeptide release by thrombin was normal in rate and amount, but fibrin monomer aggregation was grossly disturbed, especially in a high ionic strength medium. We have designated this fibrinogen "fibrinogen Philadelphia." Acrylamide gel electrophoresis of mixtures of ["'I]normal and ['I]abnormal fibrinogens revealed a slight increase in the anodal mobility of fibrinogen Philadelphia. Similarly, DEAEcellulose chromatography showed slightly stronger binding of fibrinogen Philadelphia than normal. To elucidate the mechanism responsible for the low plasma fibrinogen concentration, simultaneous metabolic studies of autologous (patient) and homologous (normal) fibrinogen, labeled with 1'I and 181I, respectively, were performed in two affected subjects. Autologous fibrinogen half-life was short and the fractional catabolic *rate was markedly increased in both family members. In contrast, homologous fibrinogen half-life and fractional catabolic rate were normal. These metabolic studies demonstrate that rapid degradation of fibrinogen This work wvas presented in part at the 64th Annual

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“…In fibrinogens Bethesda III [17], Baltimore I [18], Paris II [19], Nancy [20] and Philadelphia [2], the abnormality lies in the elution of the first peak, whereas in Paris I [22], the two fibrinogen peaks emerged later than their presumed counterparts.…”

Section: Discussionmentioning

confidence: 99%

Fibrinogen Sevilla, a congenital dysfibrinogenemia characterized by an abnormal monomer aggregation and a defective plasmin lysis

Fernández

Noguerol

Sosa

et al. 1989

Clinica Chimica Acta

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A dysfibrinogenemia (fibrinogen Sevilla) was detected in a 64-yr-old woman with no previous history of hemorrhagic diathesis or thrombosis. Thrombin and reptilase times were prolonged. The aggregation of fibrin monomers showed a prolonged latency time with a defective slope although fibrinopeptide release and clot stabilization were found to be normal. Plasmin proteolysis was abnormal with a much slower plasmic degradation in patient's purified fibrinogen. By chromatofocussing the patient's fibrinogen showed an abnormality in pattern elution with a second peak eluting at a pH slightly more basic than the normal one @H 5.5). Likewise, the isoelectrofocussing of purified non-reduced patient's fibrinogen in agarose gel showed an abnormal distribution in its focussed bands, especially in a group which focussed in a p&interval between 5.20-5.85. By two-dimensional electrophoresis we did not find any abnormality in the fibrinogen-reduced chains. These results could indicate that the abnormal monomer aggregation, as well as the defective plasmin lysis, could be due to conformational aspects of fibrinogen rather than to structural defects.

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Un nouveau Cas d’Anomalie constitutionnelle et familiale du Fibrinogène sans Diathese hémorragique

Cited by 15 publications

References 9 publications

Abnormal sialic acid content of the dysfibrinogenemia associated with liver disease.

Abnormal sialic acid content of the dysfibrinogenemia associated with liver disease.

Fibrinogen Philadelphia. A hereditary hypodysfibrinogenemia characterized by fibrinogen hypercatabolism.

Fibrinogen Sevilla, a congenital dysfibrinogenemia characterized by an abnormal monomer aggregation and a defective plasmin lysis

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