Structural, quantitative and functional comparison of amyloid P component in sera from patients with systemic lupus erythematosus and healthy donors.

Serum amyloid P component (SAP) is a serum protein that has a function as opsonin and is known to bind nuclear material with high affinity. Quantitative and/or qualitative deficiencies in SAP may possibly lead to the impairment of normal homoeostatic mechanisms of tissue turnover. Thus, SAP knockout mice display systemic lupus erythematosus (SLE)-like manifestations such as nephritis and circulating antinuclear antibodies. In the present study, we investigated whether there are changes in the structure, function or serum levels of SAP in serum from SLE patients as compared with those from healthy donors. We found that SAP in SLE sera has the same molecular mass as that of in the sera of normal individuals, when analysed by online immunoaffinity reversed phase mass spectrometry. Also, the serum levels of SAP did not differ significantly between the two groups. Finally, as an estimate of function, SAP from SLE patients appeared to have the same affinity for heparin and nucleosomes as SAP from normal individuals, when analysed by crossed affinity immunoelectrophoresis and enzyme-linked immunosorbent capture assay (ELISA). In conclusion, the data do not support alterations in the levels, structure or function of SAP circulating in SLE patients.