Precursor protein

 

Detection of the precursor protein is the finishing touch of amyloid characterisation. In AL amyloidosis free kappa or lambda light chains can be detected by immunofixation of blood or concentrated urine. A promising new technique is the so-called free light chain test. In AA amyloidosis the precursor protein SAA (serum amyloid A protein) reflects as acute phase reactant (similar to C-reactive protein) the severity of the underlying inflammatory disorder. In ATTR amyloidosis mutated TTR (transthyretin) can be detected in blood by iso-electric focusing.

Detection of these precursor proteins has more than only illustrative value. Therapy is aimed at the removal of the presence and further supply of the precursor protein in the deposition process. Monitoring of the presence and altitude of serum levels of the precursor protein during therapy can provide insight in the effectiveness of treatment.

 

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Publications of our group:

 

Dofferhoff AS, Bom VJ, Vries-Hospers HG, van Ingen J, vd-Meer J, Hazenberg BP et al. Patterns of cytokines, plasma endotoxin, plasminogen activator inhibitor, and acute-phase proteins during the treatment of severe sepsis in humans. Crit Care Med 1992; 20(2):185-92

Dofferhoff AS, Bom VJ, van Ingen J, Vries-Hospers HG, Hazenberg BP, van der Meer J et al. Patterns of cytokines, plasma endotoxin, and acute phase proteins during the treatment of severe sepsis in humans. Prog Clin Biol Res 1991; 36743-54

Yap SH, Moshage HJ, Hazenberg BP, Roelofs HM, Bijzet J, Limburg PC et al. Tumor necrosis factor (TNF) inhibits interleukin (IL)-1 and/or IL-6 stimulated synthesis of C-reactive protein (CRP) and serum amyloid A (SAA) in primary cultures of human hepatocytes. Biochim Biophys Acta 1991; 1091(3):405-8

Moshage HJ, Roelofs HM, van Pelt JF, Hazenberg BP, van Leeuwen MA, Limburg PC et al. The effect of interleukin-1, interleukin-6 and its interrelationship on the synthesis of serum amyloid A and C-reactive protein in primary cultures of adult human hepatocytes. Biochem Biophys Res Commun 1988; 155(1):112-7 > pdf >