Abstract
The neutrophil Mac-1 and gp100MEL-14 adhesion proteins are involved in neutrophil extravasation during inflammation. Both the expression and activity of Mac-1 are greatly increased after neutrophil activation. In contrast, neutrophils shed gp100MEL-14 from the cell surface within 4 minutes after activation with chemotactic factors or phorbol esters, releasing a 96-kilodalton fragment of the antigen into the supernatant. Immunohistology showed that gp100MEL-14 was downregulated on neutrophils that had extravasated into inflamed tissue. The gp100MEL-14 adhesion protein may participate in the binding of unactivated neutrophils to the endothelium; rapid shedding of gp100MEL-14 may prevent extravasation into and damage of normal tissues by activated neutrophils.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Antigens, Differentiation / immunology*
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Antigens, Surface / immunology*
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Bone Marrow Cells
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Cell Adhesion
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Cell Adhesion Molecules
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Chemotactic Factors / physiology*
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Complement C5 / physiology
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Complement C5a
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Fluorescent Antibody Technique
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Interleukin-1 / physiology
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Interleukin-8
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Kinetics
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Leukotriene B4 / physiology
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Lipopolysaccharides / physiology
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Lymphocyte Activation
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Macrophage Activation
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Macrophage-1 Antigen
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Mice
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Mice, Inbred BALB C
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Neutrophils / cytology
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Neutrophils / immunology*
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Tetradecanoylphorbol Acetate
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Tumor Necrosis Factor-alpha / physiology
Substances
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Antigens, Differentiation
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Antigens, Surface
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Cell Adhesion Molecules
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Chemotactic Factors
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Complement C5
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Interleukin-1
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Interleukin-8
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Lipopolysaccharides
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Macrophage-1 Antigen
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Tumor Necrosis Factor-alpha
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Leukotriene B4
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Complement C5a
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Tetradecanoylphorbol Acetate