Acquired dysfibrinogenemia caused by monoclonal production of immunoglobulin   light chain

Dear, Amy; Brennan, Stephen O.; Sheat, M J; Faed, James M.; George, Peter M.

doi:10.3324/haematol.11837

Cited by 29 publications

(20 citation statements)

References 17 publications

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“…Nonspecific interactions of paraprotein with fibrinogen have already been described earlier [23, 24]. The nonimmune character of the interaction of the immunoglobulin light chain alone was described by Shigekiyo et al [23], who identified Bence Jones protein (BJP) as a VλII subgroup BJP in a patient with primary amyloidosis and prolonged thrombin and reptilase times.…”

Section: Discussionmentioning

confidence: 97%

“…It was reported that these products of myeloma may impair fibrin formation by either antigen-antibody interactions, nonspecific interactions [23, 24] or increasing plasma viscosity caused by high protein concentration in the blood [25,26,27] or a combination of these causes [28]. Fibrin networks formed in the presence of paraprotein have been described to have viscoelastic properties differing from those of a normal fibrin network.…”

Section: Introductionmentioning

confidence: 99%

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Acquired Dysfibrinogenemia Secondary to Multiple Myeloma

et al. 2008

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Abnormal coagulation properties indicative of a dysfibrinogen were found in the plasma of a 72-year-old male with multiple myeloma (IgGĸ, stage IIIA). The patient had high paraprotein concentration (85.75 g/l) and prolonged thrombin time (76.8 s), activated partial thromboplastin time (39.5 s), prothrombin time (23.5 s) and reptilase time (72.0 s). The fibrinogen level was increased. The fibrin polymerization induced by both thrombin and reptilase was impaired. Scanning electron microscopy revealed abnormal clot morphology. After six months of treatment, the paraprotein level decreased (19.48 g/l) and coagulation normalized as well as fibrin polymerization and fibrin clot morphology. It was found that the paraprotein interacts with the γ-chain of fibrinogen. Acquired dysfibrinogenemia associated with multiple myeloma was diagnosed in the 72-year-old patient.

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Section: Discussionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Acquired Dysfibrinogenemia Secondary to Multiple Myeloma

et al. 2008

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“…Acquired dysfibrinogenemia occurs mainly in the patients with chronic liver disease. Other causes include hepatocellular carcinoma, obstructive biliary disease, and immune disorders (e.g., multiple myeloma and systemic lupus erythematosus) [5][6][7][8][9].…”

Section: Discussionmentioning

confidence: 99%

Dysfibrinogenemia with Subgaleal Hematoma: An Unusual Presentation

Khare

Kumar

Marwah

et al. 2015

Indian J Hematol Blood Transfus

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“…A recent study has demonstrated the ability of immunoglobulin lambda light chain to bind to fibrinogen and inhibit thrombin-catalyzed fibrin polymerization. It is proposed that the lambda light chain non-covalently associates with the alpha region leading to significant polymerization defect 39. Immunoglobulin M has been implicated in venous and arterial thrombosis.…”

Section: Discussionmentioning

confidence: 99%

Microparticle Surface Proteins Are Associated With Experimental Venous Thrombosis: A Preliminary Study

Abdullah¹,

Kachman²,

Walker³

et al. 2008

Clinical and Applied Thrombosis/Hemostasis

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SUMMARYMicroparticles (MPs) are small membrane vesicles released from activated cells and are associated with thrombosis and inflammation. Microparticles contain a unique subset of surface proteins derived from the parent cell and may be responsible for their diverse biological functions. To identify these proteins juvenile baboons (Papio anubis, n=4) underwent iliac vein thrombosis with six-hour balloon occlusion. Plasma samples were taken at baseline and at 2 days post thrombosis for MP analysis. Microparticles were extracted from platelet-poor plasma, digested separately with trypsin and tagged using iTRAQ reagents. The digests were subjected to 2-D LC separation followed by MALDI tandem mass spectrometry. Peak lists were generated and searched against all primate sequences. For protein identity, a minimum of two peptides at 95% confidence was required. Later, iTRAQ ratios were generated comparing relative protein level of day-2 to baseline. The proteomic analysis was performed twice for each blood sample, totaling 8 experiments. Proteins were considered elevated or depressed if the iTRAQ ratio deviated by 20% change from normal and a p-value less than 0.05. Significantly, 7 proteins were differentially expressed on day-2 compared to baseline, and appeared in at least two animals and regulated in at least 4 experiments, and appeared in at least three animals and regulated in at least four experiments. Among these 7 proteins, up-regulated proteins include various forms of fibrinogen and alpha-1-antichymotrypsin, and down-regulated proteins include immunoglobulins. These proteins influence thrombosis and inflammation through hemostatic plug formation (fibrinogen), inhibiting neutrophil adhesion (alpha-1-antichymoptrypsin), and immunoregulation (immunoglobulins). Further studies are needed to confirm the mechanistic role of these proteins in the pathogenesis of venous thrombosis.

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Acquired dysfibrinogenemia caused by monoclonal production of immunoglobulin light chain

Cited by 29 publications

References 17 publications

Acquired Dysfibrinogenemia Secondary to Multiple Myeloma

Acquired Dysfibrinogenemia Secondary to Multiple Myeloma

Dysfibrinogenemia with Subgaleal Hematoma: An Unusual Presentation

Microparticle Surface Proteins Are Associated With Experimental Venous Thrombosis: A Preliminary Study

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