Immunomoduatory properties of host defence peptide LL-37 during infection and inflammation in human blood cells
department or school: Science, Faculty of
department or school: Microbiology and Immunology, Department of
data provider: DSpace
degree campus: UBCV
creator: Yu, Jie
issued: 2011-02-18T18:52:19Z
issued: 2006
related degree: Master of Science - MSc
degree grantor: University of British Columbia
description: The human cathelicidin, LL-37, is a cationic host defence peptide and serves as an essential component of innate immunity. In addition to its modest antimicrobial activity, LL-37 has been demonstrated to be a multifunctional modulator of innate immune responses, although the mechanism(s) of which have not been elucidated. The present study demonstrated that LL-37 could synergistically enhance IL-1β-induced production of cytokines (IL-6, IL-10) and chemokines (MCP-3) in primary human PBMCs. In contrast to the neutralization of LPS-induced secretion of pro-inflammatory cytokines, LL-37 dramatically augmented LPS-stimulated MCP-3 production. LL-37 by itself induced transient phosphorylation of IkB-α. and the subsequent nuclear translocation of NF - kB subunits p50 and p65, which could be further enhanced in the presence of IL-1β. Similar effects of LL-37 and I L-1β were also observed oh activation of Akt and CREB. Therefore, we propose that, in addition to its well-known anti-inflammatory activity, the human host defence peptide LL-37 also plays an important role in boosting the innate immune responses in combination with inflammatory mediator (IL-1β), which provides a new mechanism for LL-37 in modulating the inflammatory responses in innate immunity.
aggregated CHO: https://circle.library.ubc.ca/rest/handle/2429/31500
note: IMMUNOMODULATORY PROPERTIES OF HOST DEFENCE PEPTIDEJX-37 DURING INFECTION AND INFLAMMATION IN HUMAN BLOOD CELLS by J I E Y U B. Med., Medical School, Shandong University, China 2001 A THESIS SUBMITTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF MASTER OF SCIENCE in THE FACULTY OF GRADUATE STUDIES (Microbiology and Immunology) THE UNIVERSITY OF BRITISH C O L U M B I A November 2006 © J ieYu,2006 A B S T R A C T The human cathelicidin, LL -37 , is a cationic host defence peptide and serves as an essential component of innate immunity. In addition to its modest antimicrobial activity, LL -37 has been demonstrated to be a multifunctional modulator of innate immune responses, although the mechanism(s) of which have not been,elucidated. The present study demonstrated that LL-37 .could synergistically enhance IL- ip- induced production of cytokines (IL-6, IL-10) and chemokines (MCP-3) in primary human P B M C s . In contrast to the neutralization of LPS-induced secretion of pro-inflammatory cytokines, LL -37 dramatically augmented LPS-stimulated M C P - 3 production. LL -37 by itself induced transient phosphorylation of IKB-O. and the subsequent nuclear translocation of N F - K B subunits p50 and p65, which could be further enhanced in the presence of IL-1B. Similar effects of LL -37 and I L - i p were also observed oh activation of Akt and C R E B . Therefore, we propose that, in addition to its well-known anti-inflammatory activity, the human host defence peptide LL -37 also plays an important role in boosting the innate immune responses in combination with inflammatory mediator ( IL- ip) , which provides a new mechanism for LL-37 in modulating the inflammatory responses in innate immunity. i i T A B L E O F C O N T E N T S ABSTRACT i i TABLE OF CONTENTS i i i LIST OF TABLES v LIST OF FIGURES v i LIST OF ABBREVIATIONS v i i ACKNOWLEDGEMENTS ix Chapter 1. GENERAL INTRODUCTION 1 1.1 Innate Immune System 1 1.1.1 T L R s and IL-1R 1 1.1.2 TLRs / IL -1R media…
has type: Thesis/Dissertation
is shown at: 10.14288/1.0100751
language: eng
degree discipline: Microbiology and Immunology
provider: Vancouver : University of British Columbia Library
publisher: University of British Columbia
rights: For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.
scholar level: Graduate
type: Text
identifier URI: http://hdl.handle.net/2429/31500