{"id":80379,"date":"2025-12-18T16:11:59","date_gmt":"2025-12-18T16:11:59","guid":{"rendered":"https:\/\/cri1149.fr\/publication\/deciphering-opsonized-zymosan-induced-phosphorylation-of-p47phox-and-nadph-oxidase-activation-in-human-neutrophils\/"},"modified":"2026-03-06T12:13:48","modified_gmt":"2026-03-06T12:13:48","slug":"deciphering-opsonized-zymosan-induced-phosphorylation-of-p47phox-and-nadph-oxidase-activation-in-human-neutrophils","status":"publish","type":"publication","link":"https:\/\/cri1149.fr\/en\/publication\/deciphering-opsonized-zymosan-induced-phosphorylation-of-p47phox-and-nadph-oxidase-activation-in-human-neutrophils\/","title":{"rendered":"Deciphering opsonized zymosan-induced p47phox phosphorylation and NADPH oxidase activation in human neutrophils"},"content":{"rendered":"\n

Neutrophils play a key role in innate immunity by eliminating microbes through phagocytosis and superoxide anion production via the phagocyte NADPH oxidase. The signaling pathways regulating activation of this oxidase in neutrophils have been extensively studied using soluble agonists, but are less well understood during phagocytosis, a fundamental function of neutrophils. <\/p>\n\n

The aim of this study was to examine phosphorylation of the cytosolic NADPH oxidase protein p47phox in human neutrophils stimulated with serum-opsonized zymosan (OZ), which induces phagocytosis, using antibodies directed against phosphorylated sites. The results show that OZ induces rapid phosphorylation of p47phox at residues Ser304, Ser315, Ser320 and Ser328, followed by equally rapid dephosphorylation. <\/p>\n\n

Interestingly, despite the transient nature of this phosphorylation, OZ-induced NADPH oxidase activity remained sustained for longer, both in intact cells and in isolated membranes. OZ-induced phosphorylation of p47phox at these sites was concentration-dependent and preceded particle ingestion. <\/p>\n\n

Zymosan opsonized with IgG or C3bi also induced rapid phosphorylation and dephosphorylation of p47phox at residues Ser304, Ser315, Ser320 and Ser328, suggesting the involvement of Fc\u03b3R and CR3 receptors in this process.<\/p>\n\n

Inhibitors of Src and Syk tyrosine kinases, PI3K, PLC, PLD, calcium (Ca++) and PKC\u03b22 inhibited OZ-induced phosphorylation of p47phox at these residues.<\/p>\n\n

These results suggest that :<\/p>\n\n

    \n
  1. OZ-induced phosphorylation of p47phox at residues Ser304, Ser315, Ser320 and Ser328 is required to initiate NADPH oxidase activation, but not for its maintenance during phagocytosis;<\/li>\n\n\n\n
  2. membrane receptors Fc\u03b3R and CR3 are involved in this phosphorylation;<\/li>\n\n\n\n
  3. les kinases Src et Syk, la PI3K, la PLD, le calcium et la PKC\u03b22 contr\u00f4lent la phosphorylation de p47phox au cours de la phagocytose.<\/li>\n<\/ol>\n\n
    \"\"<\/figure>\n","protected":false},"featured_media":0,"template":"","meta":{"_acf_changed":false},"category_publication":[],"class_list":["post-80379","publication","type-publication","status-publish","hentry"],"acf":{"numero_de_publication":"Blood.","date_de_publication":"20250722","numero_doi":"10.1182\/blood.2024027018","equipe":[376],"auteurs-liste":[{"texte_libre":false,"auteur-lien":77800,"auteur-text":""},{"texte_libre":false,"auteur-lien":13174,"auteur-text":""},{"texte_libre":false,"auteur-lien":80345,"auteur-text":""},{"texte_libre":false,"auteur-lien":80319,"auteur-text":""},{"texte_libre":false,"auteur-lien":13071,"auteur-text":""}],"auteurs-manuel":"","liens_externes":[{"url":"https:\/\/pubmed.ncbi.nlm.nih.gov\/40561248\/"}],"liens":null,"paragraphe":"

    Neutrophils play a key role in innate immunity by eliminating microbes through phagocytosis and superoxide anion production via the phagocyte NADPH oxidase. The signaling pathways regulating activation of this oxidase in neutrophils have been extensively studied using soluble agonists, but are less well understood during phagocytosis, a fundamental function of neutrophils. <\/p>\n

    The aim of this study was to examine phosphorylation of the cytosolic NADPH oxidase protein p47phox in human neutrophils stimulated with serum-opsonized zymosan (OZ), which induces phagocytosis, using antibodies directed against phosphorylated sites. The results show that OZ induces rapid phosphorylation of p47phox at residues Ser304, Ser315, Ser320 and Ser328, followed by equally rapid dephosphorylation. <\/p>\n

    Interestingly, despite the transient nature of this phosphorylation, OZ-induced NADPH oxidase activity remained sustained for longer, both in intact cells and in isolated membranes. OZ-induced phosphorylation of p47phox at these sites was concentration-dependent and preceded particle ingestion. <\/p>\n

    Zymosan opsonized with IgG or C3bi also induced rapid phosphorylation and dephosphorylation of p47phox at residues Ser304, Ser315, Ser320 and Ser328, suggesting the involvement of Fc\u03b3R and CR3 receptors in this process.<\/p>\n

    Inhibitors of Src and Syk tyrosine kinases, PI3K, PLC, PLD, calcium (Ca++) and PKC\u03b22 inhibited OZ-induced phosphorylation of p47phox at these residues.<\/p>\n

    These results suggest that :<\/p>\n\n

      \n \t
    1. \n

      OZ-induced phosphorylation of p47phox at residues Ser304, Ser315, Ser320 and Ser328 is required to initiate NADPH oxidase activation, but not for its maintenance during phagocytosis;<\/p>\n<\/li>\n \t

    2. \n

      membrane receptors Fc\u03b3R and CR3 are involved in this phosphorylation;<\/p>\n<\/li>\n \t

    3. \n

      les kinases Src et Syk, la PI3K, la PLD, le calcium et la PKC\u03b22 contr\u00f4lent la phosphorylation de p47phox au cours de la phagocytose.<\/p>\n<\/li>\n<\/ol>\n\"\"","paragraphe_en":"","documents":null},"yoast_head":"\nDeciphering opsonized zymosan-induced p47phox phosphorylation and NADPH oxidase activation in human neutrophils - CRI<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/cri1149.fr\/en\/publication\/deciphering-opsonized-zymosan-induced-phosphorylation-of-p47phox-and-nadph-oxidase-activation-in-human-neutrophils\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Deciphering opsonized zymosan-induced p47phox phosphorylation and NADPH oxidase activation in human neutrophils - CRI\" \/>\n<meta property=\"og:description\" content=\"Neutrophils play a key role in innate immunity by eliminating microbes through phagocytosis and superoxide anion production via the phagocyte NADPH oxidase. 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