Open AccessStudies in vivo and in vitro of serum amyloid P component in normals and in a patient with AA amyloidosis
Author(s) -
HAWKINS P. N.,
TENNENT G. A.,
WOO P.,
PEPYS M. B.
Publication year - 1991
Publication title -
clinical & experimental immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 135
eISSN - 1365-2249
pISSN - 0009-9104
DOI - 10.1111/j.1365-2249.1991.tb08166.x
Subject(s) - serum amyloid p component , amyloidosis , in vivo , pathogenesis , in vitro , isoelectric focusing , amyloid (mycology) , microbiology and biotechnology , biology , genotype , restriction fragment length polymorphism , aa amyloidosis , polyacrylamide gel electrophoresis , sepharose , biochemistry , chemistry , immunology , medicine , gene , enzyme , genetics , disease , inflammation , familial mediterranean fever , botany , c reactive protein
SUMMARY Pure serum amyloid P component (SAP) was isolated from a normal donor pool, from individuals with the different genotypes of an Msp I restriction fragment length polymorphism (RFLP) linked to the SAP gene, and from a patient with AA amyloidosis. The SAP preparations were all identical and all behaved as a single homogeneous species in polyacrylamide gel electrophoresis, isoelectric focussing, reverse‐phase chromatography, binding in vitro to phosphoethanolamine‐Sepharose (binding constant 2.4× 10 7 l /mol) and AL amyloid fibrils (1.6 × 10 8 l /mol), and binding to amyloid deposits in vivo in mice with casein‐induced amyloidosis. The in vivo metabolism of 125 I‐SAP from a single donor was normal and identical in three healthy individuals representing the three different Msp I RFLP genotypes. There is thus no frequent polymorphism of SAP in normal subjects, and SAP altered with respect to the characteristics studied here is not a necessary condition for pathogenesis of systemic AA amyloidosis.