Studies in vivo and in vitro of serum amyloid P component in normals and in a patient with AA amyloidosis

Clinical and Experimental Immunology
Philip N HawkinsMark B Pepys


Pure serum amyloid P component (SAP) was isolated from a normal donor pool, from individuals with the different genotypes of an MspI 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 x 10(7) l/mol) and AL amyloid fibrils (1.6 x 10(8) l/mol), and binding to amyloid deposits in vivo in mice with casein-induced amyloidosis. The in vivo metabolism of 125I-SAP from a single donor was normal and identical in three healthy individuals representing the three different MspI 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.


Jul 30, 1999·Nature Medicine·Mark B Pepys
Apr 28, 2006·Nature·Mark B PepysStephen P Wood
Nov 23, 2006·Proceedings of the National Academy of Sciences of the United States of America·Sandra B HaudekMark L Entman
Jul 1, 1995·European Journal of Nuclear Medicine·Philip N Hawkins, Mark B Pepys
Aug 2, 2014·Acta Crystallographica. Section D, Biological Crystallography·Simon E KolstoeStephen P Wood
Oct 28, 1998·Scandinavian Journal of Immunology·M NyboS E Svehag
May 17, 2000·FEBS Letters·A R CokerS P Wood
Dec 20, 2000·Proceedings of the National Academy of Sciences of the United States of America·M NoursadeghiMark B Pepys
Dec 30, 2009·Arthritis and Rheumatism·Francesco CarlucciMarina Botto
Oct 30, 2007·Journal of Medical Microbiology·Thomas P GrienerGlen D Armstrong
Apr 18, 2009·Proceedings of the National Academy of Sciences of the United States of America·Simon E KolstoeMark B Pepys
Jan 27, 1994·Nature·J EmsleyS P Wood
Mar 2, 2011·Journal of Molecular Recognition : JMR·Halina MikolajekStephen P Wood


Dec 1, 1990·The Journal of Clinical Investigation·Philip N HawkinsMark B Pepys
Apr 16, 1987·Biochimica Et Biophysica Acta·S MaudsleyMark B Pepys
Jan 1, 1988·International Archives of Allergy and Applied Immunology·B M KubakL A Potempa
Mar 1, 1988·The Journal of Experimental Medicine·Philip N HawkinsMark B Pepys
Oct 14, 1987·Biochemical and Biophysical Research Communications·Mark B Pepys, P J Butler
Sep 25, 1974·Journal of Chromatography·P G Righetti, J W Drysdale
Apr 1, 1968·The Journal of Clinical Investigation·M PrasE C Franklin
Aug 1, 1967·Proceedings of the Society for Experimental Biology and Medicine·E S CathcartA S Cohen
Sep 1, 1984·Scandinavian Journal of Immunology·J J Li, K P McAdam
Jan 1, 1982·Annals of the New York Academy of Sciences·J K Anderson, J E Mole
Jan 1, 1982·Annals of the New York Academy of Sciences·Mark B PepysA Feinstein
Jan 1, 1982·Annals of the New York Academy of Sciences·M L BaltzMark B Pepys
Jan 1, 1982·Journal of Immunological Methods·F C De Beer, Mark B Pepys

Related Concepts

Metabolic Process, Cellular
Gene Polymorphism
Casein allergenic extract
Amyloid fibril protein AL
In Vivo
Pathogenic Aspects
Reactive Systemic Amyloidosis

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