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Title: Characterisation of molecular forms of human immunoglobulin light chains in urine of patients with monoclonal gammapathy
Abstract:
Free light chains are biochemical marker of monoclonal gammapathies. Particular properties of FLC have influence on the formation of protein aggregates in protein deposition diseases (LCDD, AL, cast nephropathy and others) giving wide spectrum of symptoms: cardiological, nephrological, neurological and others.Monomer and joined by disulphide bond dimer are most important forms of FLCs. FLC of lambda type exist mainly as dimers while percentage values of dimers for kappa light chains is widely distributed.The data indicating that dimer/monomer ratio is characteristic for the patient and doesn’t change during progression of the disease was presented. Literature data indicate, that dimeric form of FLCs are involved in pathogenesis of amyloidosis and are considered as a worse prognostic factor.Posttranslational modifications of FLC have impact on physicochemical properties of this protein. It may cause great variation of molecular mass of FLC and its tendency to oligomerisation.FLCs (predominantly kappa) are extensively thiolated. Cysteine was proved to be a main low molecular thiole forming mixed disulphides with FLC. Relative concentration of bound thiols is independent of FLC’s type but differs between monoclonal and polyclonal FLCs. Relative concentration of bound cysteinylglycine is four times higher for monoclonal FLCs as compared to polyclonal.In this paper presence of FLC l ; adder phenomenon was demonstrated also for monoclonal FLCs. Existence of uniformly separated protein bands on high resolution electrophoretic separations may be explained by heterogeneous protein thiolation.
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Last modified:
Mar 16, 2023
In our library since:
Sep 17, 2015
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6
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http://dl.cm-uj.krakow.pl:8080/publication/4016
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| Edition name | Date |
|---|---|
| ZB-122378 | Mar 16, 2023 |
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