抄録
This paper describes a sister and brother with recurrent infections resulting from an adhesion defect of neutrophils due to a deficiency in neutrophil membrane proteins.
Neutrophil function tests of both patients revealed a gross reduction in adhesion and chemotaxis and to a lesser extent in phagocytosis. Their parents' neutrophils showed a mild reduction in adhesion. Analysis of membrane proteins by conventional sodium dodecyl sulfate polyacrylamide gel electrophoresis disclosed a total deficiency of 110K glycoprotein (gp 110) in neutrophils of the siblings and a 50% reduction in those of the parents. These results indicate that the disease was inherited in an autosomal recessive fashion.
The patients' neutrophils attached on a glass surface showed a considerable reduction of pseudopods compared to a normal control, whereas when suspended in an aqueous solution, they showed normal morphological changes in reaction to a chemotactic factor, a finding indicating that their neutrophils have a normally functioning cytoskeleton. A polyclonal rabbit antiserum to the deficient membrane proteins identified yet another membrane protein, p98, in addition to gp 110, deficient in the patients' neutrophils. The polyclonal antiserum showed a strong inhibitory activity against adhesion and chemotaxis and to a lesser extent against phagocytosis of normal neutrophils, a finding indicating that the membrane proteins deficient in the patients' neutrophils are essential n adhesion of the neutrophils.
