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Molecules 2014, 19(1), 1328-1343; https://doi.org/10.3390/molecules19011328

EGF Receptor-Dependent Mechanism May be Involved in the Tamm–Horsfall Glycoprotein-Enhanced PMN Phagocytosis via Activating Rho Family and MAPK Signaling Pathway

1
Institute of Clinical Medicine, National Yang-Ming University College of Medicine, Taipei 11221, Taiwan
2
Institute of Molecular Medicine, National Taiwan University College of Medicine, Taipei 10002, Taiwan
3
Institute of Clinical Medicine, National Taiwan University College of Medicine, Taipei 10002, Taiwan
4
Section of Nephrology, Taipei Veterans General Hospital, Taipei 11221, Taiwan
5
Section of Allergy, Immunology & Rheumatology, Taipei Veterans General Hospital, Taipei 11221, Taiwan
6
Department of Internal Medicine, National Taiwan University Hospital and National Taiwan University College of Medicine, Taipei 10002, Taiwan
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Received: 3 December 2013 / Revised: 13 January 2014 / Accepted: 16 January 2014 / Published: 21 January 2014
(This article belongs to the Special Issue Oligosaccharides and Glyco-Conjugates)
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Abstract

Our previous studies showed that urinary Tamm–Horsfall glycoprotein (THP) potently enhanced polymorphonuclear neutrophil (PMN) phagocytosis. However, the domain structure(s), signaling pathway and the intracellular events responsible for THP-enhanced PMN phagocytosis remain to be elucidated. THP was purified from normal human urine. The human promyelocytic leukemia cell line HL-60 was induced to differentiate into PMNs by all-trans retinoid acid. Pretreatment with different MAPK and PI3K inhibitors was used to delineate signaling pathways in THP-enhanced PMN phagocytosis. Phosphorylation of molecules responsible for PMN phagocytosis induced by bacterial lipopolysaccharide (LPS), THP, or human recombinant epidermal growth factor (EGF) was evaluated by western blot. A p38 MAPK inhibitor, SB203580, effectively inhibited both spontaneous and LPS- and THP-induced PMN phagocytosis. Both THP and LPS enhanced the expression of the Rho family proteins Cdc42 and Rac that may lead to F-actin re-arrangement. Further studies suggested that THP and EGF enhance PMN and differentiated HL-60 cell phagocytosis in a similar pattern. Furthermore, the EGF receptor inhibitor GW2974 significantly suppressed THP- and EGF-enhanced PMN phagocytosis and p38 and ERK1/2 phosphorylation in differentiated HL-60 cells. We conclude that EGF receptor-dependent signaling may be involved in THP-enhanced PMN phagocytosis by activating Rho family and MAP kinase. View Full-Text
Keywords: Tamm-Horsfall glycoprotein; phagocytosis; EGF-like domains; Rho family; MAP kinase Tamm-Horsfall glycoprotein; phagocytosis; EGF-like domains; Rho family; MAP kinase
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Li, K.-J.; Siao, S.-C.; Wu, C.-H.; Shen, C.-Y.; Wu, T.-H.; Tsai, C.-Y.; Hsieh, S.-C.; Yu, C.-L. EGF Receptor-Dependent Mechanism May be Involved in the Tamm–Horsfall Glycoprotein-Enhanced PMN Phagocytosis via Activating Rho Family and MAPK Signaling Pathway. Molecules 2014, 19, 1328-1343.

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