TY - JOUR
T1 - A constitutive antibody in normal human serum directed against rabbit bone marrow cells
T2 - Lack in parturients, neonates, and hematologic disorders
AU - Manor, Daphna
AU - Nussinovich, Rachel
AU - Yeheskel, Avivah
AU - Kaempfer, Raymond
PY - 1990/12
Y1 - 1990/12
N2 - Normal human serum effectively inhibits a bioassay for erythropoietin based on DNA synthesis by rabbit erythroid precursors. This heat-sensitive inhibitory activity is readily lost on dilution of serum, revealing the presence of erythropoletin-potentiating activity. Inhibitory activity is caused by a rapid cytotoxic effect on rabbit bone marrow cells; mouse cells are less sensitive. Cytotoxic activity is removed from serum by adsorption to protein A, is not expressed at 4° C, and is neutralized by anti-C3c complement antibody. Cytotoxicity is inhibited by EGTA; the effect of EGTA is reversed by addition of Ca2+ ions. These findings show that cytotoxicity is exerted through an antibody via the classical pathway of complement-dependent cell lysis. Although serum from healthy, adult human donors consistently contains cytotoxic activity, no such activity is observed in most serum samples from neonates, parturients, and patients with severe anemia. Patients with polycythemia or chronic renal failure occasionally lack cytotoxic activity in their serum. Serum samples lacking cytotoxic activity were found to be deficient in the antibody component in 34 out of 35 cases examined. These results show that an antibody directed against rabbit cells is constitutively present in normal human serum but is absent in a number of pathologic situations as well as being absent in neonates and parturients.
AB - Normal human serum effectively inhibits a bioassay for erythropoietin based on DNA synthesis by rabbit erythroid precursors. This heat-sensitive inhibitory activity is readily lost on dilution of serum, revealing the presence of erythropoletin-potentiating activity. Inhibitory activity is caused by a rapid cytotoxic effect on rabbit bone marrow cells; mouse cells are less sensitive. Cytotoxic activity is removed from serum by adsorption to protein A, is not expressed at 4° C, and is neutralized by anti-C3c complement antibody. Cytotoxicity is inhibited by EGTA; the effect of EGTA is reversed by addition of Ca2+ ions. These findings show that cytotoxicity is exerted through an antibody via the classical pathway of complement-dependent cell lysis. Although serum from healthy, adult human donors consistently contains cytotoxic activity, no such activity is observed in most serum samples from neonates, parturients, and patients with severe anemia. Patients with polycythemia or chronic renal failure occasionally lack cytotoxic activity in their serum. Serum samples lacking cytotoxic activity were found to be deficient in the antibody component in 34 out of 35 cases examined. These results show that an antibody directed against rabbit cells is constitutively present in normal human serum but is absent in a number of pathologic situations as well as being absent in neonates and parturients.
UR - http://www.scopus.com/inward/record.url?scp=0025678984&partnerID=8YFLogxK
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C2 - 2246552
AN - SCOPUS:0025678984
SN - 0022-2143
VL - 116
SP - 771
EP - 778
JO - Translational Research
JF - Translational Research
IS - 6
ER -