Mycoplasma salivarium induces interleukin-6 and interleukin-8 in human gingival fibroblasts

Shibata, Kenichiro

doi:10.1016/s0928-8244(97)00093-x

Cited by 32 publications

(49 citation statements)

References 22 publications

(29 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Wall-less mycoplasmas lack them except for lipoproteins. Lipoproteins of some mycoplasma species are known to activate monocytes/macrophages, lymphocytes, or fibroblasts (2,3). This study also demonstrated that membrane-bound lipoproteins of M. salivarium possessed the activity to activate HGF or THP-1 cells.…”

Section: Discussionsupporting

confidence: 55%

“…salivarium cells were treated with Triton X-114 to extract lipoproteins (TXLP) according to the method described previously (3). TXLPs in the Triton X-114 phase were precipitated by methanol and used for stimulation after being suspended in sterile PBS by light sonication.…”

Section: Preparation Of Lipoproteins By the Triton X-114 Phase Separamentioning

confidence: 99%

“…Evidence is accumulated that mycoplasmal membrane-bound lipoproteins are responsible for activating monocytes/macrophages or fibroblasts (2-4). Mühlradt et al (5,6) identify a 2-kDa lipopeptide, macrophage-activating lipopeptide (MALP-2), 3 which is capable of activating monocytes/macrophages, and determine that the structure of MALP-2 is S-(2,3-bispalmitoyloxypropyl)-cysteine-GNNDESNISFKEK.…”

mentioning

confidence: 99%

See 2 more Smart Citations

The N-Terminal Lipopeptide of a 44-kDa Membrane-Bound Lipoprotein ofMycoplasma salivariumIs Responsible for the Expression of Intercellular Adhesion Molecule-1 on the Cell Surface of Normal Human Gingival Fibroblasts

Shibata

Hasebe

Into

et al. 2000

The Journal of Immunology

133

165

View full text Add to dashboard Cite

The activities to induce TNF-α production by a monocytic cell line, THP-1, and ICAM-1 expression and IL-6 production by human gingival fibroblasts were detected in plural membrane lipoproteins of Mycoplasma salivarium. Although SDS-PAGE of the lipoproteins digested by proteinase K did not reveal any protein bands with molecular masses higher than approximately10 kDa, these activities were detected in the front of the gel. A lipoprotein with a molecular mass of 44 kDa (Lp44) was purified. Proteinase K did not affect the ICAM-1 expression-inducing activity of Lp44, but lipoprotein lipase abrogated the activity. These results suggested that the proteinase K-resistant and low molecular mass entity, possibly the N-terminal lipid moiety, played a key role in the expression of the activity. The N-terminal lipid moiety of Lp44 was purified from Lp44 digested with proteinase K by HPLC. Judging from the structure of microbial lipopeptides as well as the amino acid sequence and infrared spectrum of Lp44, the structure of the N-terminal lipid moiety of Lp44 was speculated to be S-(2, 3-bisacyloxypropyl)-cysteine-GDPKHPKSFTEWV-. Its analogue, S-(2, 3-bispalmitoyloxypropyl)-cysteine-GDPKHPKSF, was synthesized. The lipopeptide was similar to the N-terminal lipid moiety of Lp44 in the infrared spectrum and the ICAM-1 expression-inducing activity. Thus, this study suggested that the active entity of Lp44 was its N-terminal lipopeptide moiety, the structure of which was very similar to S-(2, 3-bispalmitoyloxypropyl)-cysteine-GDPKHPKSF.

show abstract

Section: Discussionsupporting

confidence: 55%

Section: Preparation Of Lipoproteins By the Triton X-114 Phase Separamentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

The N-Terminal Lipopeptide of a 44-kDa Membrane-Bound Lipoprotein ofMycoplasma salivariumIs Responsible for the Expression of Intercellular Adhesion Molecule-1 on the Cell Surface of Normal Human Gingival Fibroblasts

Shibata

Hasebe

Into

et al. 2000

The Journal of Immunology

133

165

View full text Add to dashboard Cite

show abstract

“…Mycoplasmal cells were treated with Triton X-114 to extract membrane lipoproteins according to the method described previously (27). The cell suspension (0.9 ml) was mixed with 0.1 ml of 20% (v/v) Triton X-114 working stock solution.…”

Section: Methodsmentioning

confidence: 99%

“…Mycoplasmal lipoproteins activate monocytes/ macrophages and fibroblasts to produce inflammatory cytokines (23,27). There is a possibility that cytokines are involved in the cytotoxicity of LPsal and LPfer.…”

Section: Effects Of Mabs To Tnf-α Fasl and Il-1β On The Cytotoxicitmentioning

confidence: 99%

Mycoplasmal Lipoproteins Induce Toll‐Like Receptor 2‐ and Caspases‐Mediated Cell Death in Lymphocytes and Monocytes

Into

Nodasaka

Hasebe

et al. 2002

Microbiology and Immunology

View full text Add to dashboard Cite

Lipoproteins of Mycoplasma salivarium and Mycoplasma fermentans preferentially induced necrotic cell death in lymphocytic cell lines, MOLT‐4 and Raji, and in one monocytic cell line, THP‐1, whereas they preferentially induced apoptotic cell death in another monocytic cell line, HL‐60. These findings were also supported by ultrastructural observations by the use of scanning and transmission electron microscopes and by agarose gel electrophoresis of the genomic DNA. The lipoproteins activated caspase‐3 in both MOLT‐4 and HL‐60 cells, which was assessed by the cleavage of the synthetic substrate DEVD‐pNA and the endogenous substrate poly(ADP‐ribose) polymerase. The cytotoxicity to MOLT‐4 and HL‐60 cells was inhibited by various caspase inhibitors, Ac‐DMQD‐CHO, Ac‐IETD‐CHO, and Z‐VAD‐FMK. The cytotoxicity was also partially suppressed by the monoclonal antibody to Toll‐like receptor 2. Thus this study demonstrated that mycoplasmal lipoproteins induce caspases‐dependent necrotic and apoptotic cell death in lymphocytes and monocytes/macrophages, which is partially induced by TLR2‐mediated signaling.

show abstract

Lipopeptides from Staphylococcus aureus as Tlr2 Ligands: Prediction with mRNA Expression, Chemical Synthesis, and Immunostimulatory Activities

Fujimoto¹,

Hashimoto²,

Furuyashiki³

et al. 2009

ChemBioChem

View full text Add to dashboard Cite

show abstract

Mycoplasma salivarium induces interleukin-6 and interleukin-8 in human gingival fibroblasts

Cited by 32 publications

References 22 publications

The N-Terminal Lipopeptide of a 44-kDa Membrane-Bound Lipoprotein ofMycoplasma salivariumIs Responsible for the Expression of Intercellular Adhesion Molecule-1 on the Cell Surface of Normal Human Gingival Fibroblasts

The N-Terminal Lipopeptide of a 44-kDa Membrane-Bound Lipoprotein ofMycoplasma salivariumIs Responsible for the Expression of Intercellular Adhesion Molecule-1 on the Cell Surface of Normal Human Gingival Fibroblasts

Mycoplasmal Lipoproteins Induce Toll‐Like Receptor 2‐ and Caspases‐Mediated Cell Death in Lymphocytes and Monocytes

Lipopeptides from Staphylococcus aureus as Tlr2 Ligands: Prediction with mRNA Expression, Chemical Synthesis, and Immunostimulatory Activities

Contact Info

Product

Resources

About