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Titolo:
Serum amyloid P component controls chromatin degradation and prevents antinuclear autoimmunity
Autore:
Bickerstaff, MCM; Botto, M; Hutchinson, WL; Herbert, J; Tennent, GA; Bybee, A; Mitchell, DA; Cook, HT; Butler, PJG; Walport, MJ; Pepys, MB;
Indirizzi:
ImperialEnglandch Med, Hammersmith Hosp, Immunol Med Unit, London W12 0NN,Imperial Coll Sch Med London England W12 0NN l Med Unit, London W12 0NN, Imperialgland Sch Med, Hammersmith Hosp, Rheumatol Sect, London W12 0NN, En Imperial Coll Sch Med London England W12 0NN ol Sect, London W12 0NN, En ImperialEnglandch Med, Hammersmith Hosp, Dept Histopathol, London W12 0NN,Imperial Coll Sch Med London England W12 0NN istopathol, London W12 0NN, MRC, Mol Biol Lab, Cambridge CB2 2QH, England MRC Cambridge England CB2 2QH , Mol Biol Lab, Cambridge CB2 2QH, England
Titolo Testata:
NATURE MEDICINE
fascicolo: 6, volume: 5, anno: 1999,
pagine: 694 - 697
SICI:
1078-8956(199906)5:6<694:SAPCCC>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
C-REACTIVE PROTEIN; SYSTEMIC LUPUS-ERYTHEMATOSUS; SMALL NUCLEAR RIBONUCLEOPROTEIN; ACUTE-PHASE PROTEINS; MICE; BINDS; PENTRAXINS; ANTIBODIES; CLEARANCE; INVITRO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Pepys, MB ImperialEnglandch Med, Hammersmith Hosp, Immunol Med Unit, London W12 0NN, Imperial Coll Sch Med London England W12 0NN , London W12 0NN,
Citazione:
M.C.M. Bickerstaff et al., "Serum amyloid P component controls chromatin degradation and prevents antinuclear autoimmunity", NAT MED, 5(6), 1999, pp. 694-697

Abstract

Serum amyloid P component (SAP), a highly conserved plasma protein named for its universal presence in amyloid deposits', is the single normal circulating protein that shows specific calcium-dependent binding to DNA and chromatin in physiological conditions(2,3). The avid binding of SAP displaces Hi-type histones and thereby solubilizes native long chromatin, which is otherwise profoundly insoluble at the physiological ionic strength of extracellular fluids(4). Furthermore, SAP binds in vivo both to apoptotic cells(5),the surface blebs of which bear chromatin fragments(6), and to nuclear debris released by necrosis(7). SAP may therefore participate in handling of chromatin exposed by cell death(2-4,7). Here we show that mice with targeteddeletion of the SAP genes spontaneously develop antinuclear autoimmunity and severe glomerulonephritis, a phenotype resembling human systemic lupus erythematosus, a serious autoimmune disease. The SAP(-/-) mice also have enhanced anti-DNA responses to immunization with extrinsic chromatin, and we demonstrate that degradation of long chromatin is retarded in the presence of SAP both in vitro and in vivo. These findings indicate that SAP has an important physiological role, inhibiting the formation of pathogenic autoantibodies against chromatin and DNA, probably by binding to chromatin and regulating its degradation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 20:01:23