Abstract
The CD11/CD18 complex consists of three glycoprotein heterodimers [Mac-1, LFA-1, and p150,95 (1–3)] that share identical β subunits non-covalently associated with immunologically distinct α subunits. Mac-1 (CD11b/CD18) is the receptor for iC3b opsonized particles (4–6) and plays a major role in adhesion and adhesion-dependent functions of human myeloid cells (4,7–9). In normal unstimulated neutrophils and monocytes, Mac-1 is present in intracellular compartments as well as on the cell surface (3,10–13). Exposure to chemotactic stimuli (C5a, f-Met-Leu-Phe [fMLP], or Leukotriene B4) or secretagogues (phorbol myristate acetate [PMA] or calcium ionophore A23187) elicits a 5- to 10-fold increase in surface binding of monoclonal antibodies (MAbs) directed at Mac-1 (3,4,14,15) associated with a two to threefold increase in neutrophil adhesiveness (7,16). This surface protein “upregulation” is maximal within 10 minutes at 37 °C and is not impeded by protein or mRNA synthesis inhibitors, suggesting that Mac-1 is translocated from latent intracellular pools to the cell surface in response to inflammatory stimuli.
Supported by National Institutes of Health Grants No. AI19031, AI23521, DE07875, and HL41408, the National Cystic Fibrosis Foundation, and by the US Department of Agriculture-Agricultural Research Service/Children’s Nutrition and Research Center, Baylor College of Medicine and Texas Children’s Hospital. Dr. Anderson was the recipient of a Research Career Development Award (K04-AI/AM 00105) during the performance of these investigations.
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Jones, D.H. et al. (1990). Characterization of a New Mobilizable Mac-1 (CD11b/CD18) Pool That Co-Localizes with Gelatinase in Human Neutrophils. In: Springer, T.A., Anderson, D.C., Rothlein, R., Rosenthal, A.S. (eds) Leukocyte Adhesion Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3234-6_9
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