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Incomplete Fibrin Formation and Highly Elevated Factor XIII Activity in Multiple Myeloma
Author(s) -
Klingemann H.G.,
Egbring R.,
Havemann K.
Publication year - 1981
Publication title -
scandinavian journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0036-553X
DOI - 10.1111/j.1600-0609.1981.tb00481.x
Subject(s) - fibrin , factor xiii , multiple myeloma , chemistry , paraproteins , polymerization , medicine , immunology , antibody , monoclonal , organic chemistry , monoclonal antibody , polymer
Bleeding is a common complication in patients suffering from multiple myeloma. In some cases a defect in fibrin formation has been suggested as one possible cause of haemorrhagic tendency. As shown in this investigation the defect in fibrin formation, ascertained using PAGE, is due to a lack of α‐chain polymerization of fibrin monomers in 5/11 patients with IgG myeloma and in 2/5 patients with IgM paraproteinaemia. No disturbed fibrin polymerization could be observed in IgA myeloma (n = 6). Factor XIII concentrations of subunit A and to a lesser extent of subunit S (Laurell technique) were highly elevated in all cases with regular fibrin formation. Comparable values were obtained by measuring the transamidase activity of factor XIII by incorporation of 14 C‐labelled purtrescin into casein. Levels up to 600% of normal could be recorded. In contrast, all patients with a lack of α‐chain polymerization had a factor XIII activity within the normal range. Addition of factor XIII concentrate to plasma from patients with defective fibrin formation led in 5/8 cases to a partial cross‐linking of α‐monomers. We conclude that in some cases paraproteins can inhibit the factor XIII and prevent its action on fibrin.