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Glycoprotein-180 deficiency: genetics and abnormal neutrophil activation. Blood 1985 Mar;65(3):696-704

Date

03/01/1985

Pubmed ID

2982441

Abstract

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.

Author List

Weisman SJ, Berkow RL, Plautz G, Torres M, McGuire WA, Coates TD, Haak RA, Floyd A, Jersild R, Baehner RL

Author

Steven J. Weisman MD Professor in the Anesthesiology department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Blood Protein Disorders
Cell Adhesion
Cell Migration Inhibition
Chemotaxis
Child, Preschool
Female
Glycoproteins
Humans
Leukocytosis
Membrane Fluidity
Membrane Glycoproteins
Membrane Potentials
Neutrophils
Phagocytosis
Receptors, Complement
Receptors, Fc
Rosette Formation
Skin Window Technique
Superoxides
jenkins-FCD Prod-484 8aa07fc50b7f6d102f3dda2f4c7056ff84294d1d