ACUTE-PHASE HIGH-DENSITY-LIPOPROTEIN IN THE RAT DOES NOT CONTAIN SERUM AMYLOID A-PROTEIN
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BALTZ, ML
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ROYAL POSTGRAD MED SCH, DEPT MED,IMMUNOL MED UNIT,MRC, ACUTE PHASE PROT RES GRP,DU CANE RD, LONDON W12 0HS, ENGLANDROYAL POSTGRAD MED SCH, DEPT MED,IMMUNOL MED UNIT,MRC, ACUTE PHASE PROT RES GRP,DU CANE RD, LONDON W12 0HS, ENGLAND
BALTZ, ML
[1
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ROWE, IF
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ROYAL POSTGRAD MED SCH, DEPT MED,IMMUNOL MED UNIT,MRC, ACUTE PHASE PROT RES GRP,DU CANE RD, LONDON W12 0HS, ENGLANDROYAL POSTGRAD MED SCH, DEPT MED,IMMUNOL MED UNIT,MRC, ACUTE PHASE PROT RES GRP,DU CANE RD, LONDON W12 0HS, ENGLAND
ROWE, IF
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]
CASPI, D
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ROYAL POSTGRAD MED SCH, DEPT MED,IMMUNOL MED UNIT,MRC, ACUTE PHASE PROT RES GRP,DU CANE RD, LONDON W12 0HS, ENGLANDROYAL POSTGRAD MED SCH, DEPT MED,IMMUNOL MED UNIT,MRC, ACUTE PHASE PROT RES GRP,DU CANE RD, LONDON W12 0HS, ENGLAND
CASPI, D
[1
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TURNELL, WG
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ROYAL POSTGRAD MED SCH, DEPT MED,IMMUNOL MED UNIT,MRC, ACUTE PHASE PROT RES GRP,DU CANE RD, LONDON W12 0HS, ENGLANDROYAL POSTGRAD MED SCH, DEPT MED,IMMUNOL MED UNIT,MRC, ACUTE PHASE PROT RES GRP,DU CANE RD, LONDON W12 0HS, ENGLAND
TURNELL, WG
[1
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PEPYS, MB
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ROYAL POSTGRAD MED SCH, DEPT MED,IMMUNOL MED UNIT,MRC, ACUTE PHASE PROT RES GRP,DU CANE RD, LONDON W12 0HS, ENGLANDROYAL POSTGRAD MED SCH, DEPT MED,IMMUNOL MED UNIT,MRC, ACUTE PHASE PROT RES GRP,DU CANE RD, LONDON W12 0HS, ENGLAND
PEPYS, MB
[1
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[1] ROYAL POSTGRAD MED SCH, DEPT MED,IMMUNOL MED UNIT,MRC, ACUTE PHASE PROT RES GRP,DU CANE RD, LONDON W12 0HS, ENGLAND
Serum amyloid A protein (SAA) is an acute-phase apolipoprotein of high-density lipoprotein (HDL). Its N-terminal sequence is identical with that of amyloid A protein (AA), the subunit of AA amyloid fibrils. However, rats do not develop AA amyloidosis, and we report here that neither normal nor acute-phase rat HDL contains a protein corresponding to SAA of other species. mRNA coding for a sequence homologous with the C-terminal but not with the N-terminal part of human SAA is synthesized in greatly increased amounts in acute-phase rat liver. These observations indicate that the failure of rats to develop AA amyloid results from the absence of most of the AA-like part of their SAA-like protein, and that the N-terminal portion of SAA probably contains the lipid-binding sequences.