Ca mobilization and signaling pathways induced by rRgpB in human gingival fibroblast.
10.3724/zdxbyxb-2021-0109
- Author:
Kexin LU
1
;
Yanmin WU
1
;
Shenglai LI
1
;
Diya ZHANG
1
Author Information
1. Oral Surgery.
- Publication Type:Journal Article
- Keywords:
Calciumion;
Gingipains;
Human gingival fibroblasts;
Protease-activated receptor;
Signaling pathways
- MeSH:
Fibroblasts;
Humans;
JNK Mitogen-Activated Protein Kinases/metabolism*;
MAP Kinase Signaling System;
Phosphorylation;
Signal Transduction;
p38 Mitogen-Activated Protein Kinases/metabolism*
- From:
Journal of Zhejiang University. Medical sciences
2021;50(2):171-178
- CountryChina
- Language:English
-
Abstract:
: To assess the () recombinant gingivalis gingipain R2 (rRgpB)-induced Ca mobilization in human gingival fibroblast (HGF) mediated by protease-activated receptor (PAR) and its downstream signal transduction pathways. : Flow cytometry was used to detect the expression of PAR in HGF. The proliferation of HGF was measured by CCK-8. The dynamic changes of intracellular Ca concentration in HGF induced by rRgpB and the blocking effect of PAR-1 antagonist were observed by laser confocal microscopy. Western blot was performed to determine the phosphorylation levels of c-Jun N-terminal kinase (JNK), extracellular signal-regulated kinase (ERK) 1/2, p38 mitogen-activated protein kinase (p38 MAPK) and p65 in HGF. : PAR-1 and PAR-3 were expressed in HGF, and the rRgpB could promote the proliferation of HGF. rRgpB caused a transient increase in [Ca], which could be completely suppressed by vorapaxar, a PAR-1 antagonist. The phosphorylation levels of JNK, ERK1/2 and p65 were significantly up-regulated after the induction of rRgpB for and (all <0.05), which was completely inhibited by vorapaxar. However, the phosphorylation level of p38 MAPK had no significant change after rRgpB stimulation. : rRgpB causes an increase in [Ca] in HGF mediated by PAR-1. JNK, ERK1/2 and nuclear factor-κB may be involved in intracellular signal transduction after PAR-1 activation.
