Neutrophil adhesion abnormality with deficient surface membrane proteins (gp 110 and p 98): the effect of their antibodies on the function of normal neutrophils.

A sister and brother previously described with neutrophil adhesion defects and a lack of two neutrophil membrane proteins, glycoprotein with a molecular weight of 110 K and 115 K, were further studied. Rabbit polyclonal IgG antibodies were raised against neutrophil membrane proteins of approximately 110 K from normal individuals, and absorbed with the siblings' neutrophil membrane proteins. The antibodies thus absorbed reacted with two normal neutrophil membrane proteins, a 110 K glycoprotein and a 98 K protein, which were totally deficient in the siblings' neutrophils. The polyclonal antibodies were also reactive with a 95 K membrane protein of normal lymphocytes. The protein was missing in the siblings' lymphocytes. Three membrane proteins, Mac-1, LFA-1, and p 150, 95 each consisting of a specific alpha-subunit and a beta-subunit common to them, have been reported to be deficient in neutrophils from several patients with a neutrophil adhesion disease. Using monoclonal antibodies to Mac-1 alpha, LFA-1 alpha, and to the beta-subunit, it was deduced that the siblings' neutrophils lacked the above three membrane proteins. The disease in the siblings is thus identical with that previously described. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of immunoprecipitates, formed by reacting labeled normal neutrophil membrane proteins with our polyclonal antibodies, revealed three bands, almost identical with that of immunoprecipitates formed with the anti-beta-subunit monoclonal antibody. This finding indicates that the polyclonal antibodies reacted mainly with the beta-subunit of the membrane proteins.(ABSTRACT TRUNCATED AT 250 WORDS)