The inhibition of protein synthesis by IgG containing anti-ribosome P autoantibodies from systemic lupus erythematosus patients.
Autoantibodies found in approximately 15% of patients with systemic lupus erythematosus recognize three 60 S ribosomal phosphoproteins P0, P1, and P2. Fab fragments obtained from sera of these patients inhibited globin mRNA translation in an in vitro protein synthesizing system which was reversed by the addition of excess ribosomes. Further studies suggested that these antibodies bind to ribosomes in the intact cell. Thus, when IgG fractions from these sera were microinjected into cultured human fibroblasts [35S]methionine incorporation into cellular proteins was inhibited.
Stacey
D W
DW
Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110.
Skelly
S
S
Watson
T
T
Elkon
K
K
Weissbach
H
H
Brot
N
N
D000818:Animals; D001323:Autoantibodies / Q000276:immunology*; D002478:Cells, Cultured; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology*; D066298:In Vitro Techniques; D008180:Lupus Erythematosus, Systemic / Q000276:immunology* / Q000378:metabolism; D014176:Protein Biosynthesis; D011817:Rabbits; D012269:Ribosomal Proteins / Q000276:immunology; D012270:Ribosomes / Q000276:immunology*
D001323:Autoantibodies; D007074:Immunoglobulin G; D012269:Ribosomal Proteins