Favorable interleukin-8 induction in human gingival epithelial cells by the antimicrobial peptide LL-37

Author(s):  
Pattanin Montreekachon
2005 ◽  
Vol 73 (1) ◽  
pp. 622-626 ◽  
Author(s):  
Hiroshi Egusa ◽  
Hiroki Nikawa ◽  
Seicho Makihira ◽  
Anahid Jewett ◽  
Hirofumi Yatani ◽  
...  

ABSTRACT Increased induction of interleukin 8 (IL-8) and intercellular adhesion molecule 1 (ICAM-1) by oral epithelial cells may play a role in the host defense mechanism in oropharyngeal candidiasis; however, little is known about the expression feature of these molecules on human gingival epithelial cells (HGECs) during Candida albicans infection. In this report we present evidence that neutralization with antibody against ICAM-1 inhibited both the adherence of C. albicans to HGECs and the Candida-induced production of IL-8, suggesting a role for ICAM-1 in recognition and signaling in HGECs to express IL-8 upon infection with C. albicans.


2007 ◽  
Vol 76 (1) ◽  
pp. 198-205 ◽  
Author(s):  
Shinsuke Onishi ◽  
Kiyonobu Honma ◽  
Shuang Liang ◽  
Panagiota Stathopoulou ◽  
Denis Kinane ◽  
...  

ABSTRACT Tannerella forsythia is a gram-negative anaerobe strongly associated with chronic human periodontitis. This bacterium expresses a cell surface-associated and secreted protein, designated BspA, which has been recognized as an important virulence factor. The BspA protein belongs to the leucine-rich repeat (LRR) and bacterial immunoglobulin-like protein families. BspA is, moreover, a multifunctional protein which interacts with a variety of host cells, including monocytes which appear to respond to BspA through Toll-like receptor (TLR) signaling. Since gingival epithelium forms a barrier against periodontal pathogens, this study was undertaken to determine if gingival epithelial cells respond to BspA challenge and if TLRs play any role in BspA recognition. This study was also directed towards identifying the BspA domains responsible for cellular activation. We provide direct evidence for BspA binding to TLR2 and demonstrate that the release of the chemokine interleukin-8 from human gingival epithelial cells by BspA is TLR2 dependent. Furthermore, the LRR domain of BspA is involved in activation of TLR2, while TLR1 serves as a signaling partner. Thus, our findings suggest that BspA is an important modulator of host innate immune responses through activation of TLR2 in cooperation with TLR1.


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