Glycoprotein-180 deficiency: genetics and abnormal neutrophil activation
SJ Weisman, RL Berkow, G Plautz, M Torres, WA McGuire, TD Coates, RA Haak, A Floyd, R Jersild and RL Baehner
Neutrophil function was studied in a patient with polymorphonuclear
leukocyte (PMN) glycoprotein-180 deficiency and in her parents. PMNs of the
patient had abnormal chemotaxis, phagocytosis, adherence, surface charge,
and membrane-associated events of activation. Selective defects to C3b,
immunoglobulin G (IgG), phorbol myristate acetate (PMA) and N-
formyl-methionyl-leucyl-phenylalanine (FMLP) are described, although C3b
receptor density was normal. The parents were found to have abnormal
adherence to nylon-wool fibers, abnormal transmembrane potential
depolarization with PMA, and reduced amounts of glycoprotein- 180 in their
PMNs. These studies provide further evidence that the oxidative burst has
several different pathways for activation. They demonstrate that the
absence of a single PMN surface glycoprotein is associated with a broad
spectrum of PMN functional abnormalities. Finally, the observations made in
the parents support an autosomal recessive mode of inheritance.
Volume 65,
Issue 3,
pp. 696-704,
03/01/1985
Copyright © 1985 by The American Society of Hematology
