Abstract
A 4 y/o female with delayed umbilical cord severance, granulocytosis, periodontitis & recurrent soft tissue infections demonstrated severely diminished leukocyte mobilization (Rebuck window). SDS-PAGE of patient PMN homogenates revealed deficient (<5% normal) GP138, a major surface glycoprotein complex of normal PMNs. As shown with a NaB3H4 labelling technique, GP138 was undetectable on the surface of patient PMNs & was diminished (20% normal) on maternal PMNs. Adhesion-dependent functions of patient PMNs including directed migration, attachment & spreading (plastic or glass), aggregation (C5a, fMLP or PMA), orientation in chemotactic gradients, antibody-dependent cellular cytotoxicity (due to diminished target cell binding), & phagocytic ingestion of particles selectively opsonized by C3b (Oil-Red-O, 14C Staph. & zymosan) were profoundly diminished (p <.001 in each assay). Fc receptor "facilitated" phagocytosis & spreading & EA rosette formation by patient PMNs were normal. Adhesion independent patient PMN functions including specific binding of f-Met-Leu-3H-Phe & fMLP, C5a &/or PMA mediated shape change, O2- generation, degranulation (MPO & lactoferrin), microtubule assembly (tubulin IF) & alterations of membrane fluidity (ESR) or surface charge (cell electrophoresis) were normal. Thus, GP138 represents a critical surface glycoprotein(s) which is functionally related to the C3b receptor & is required for adhesion-dependent functions facilitating the inflammatory response in host defense.
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Anderson, D., Schmalstieg, F., Kohl, S. et al. ABNORMAL PMN FUNCTIONS ASSOCIATED WITH A HERITABLE DEFICIENCY OF A HIGH M.W. GLYCOPROTEIN (GP138). Pediatr Res 18 (Suppl 4), 251 (1984). https://doi.org/10.1203/00006450-198404001-00951
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DOI: https://doi.org/10.1203/00006450-198404001-00951
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