PMID- 23297114
OWN - NLM
STAT- MEDLINE
DCOM- 20131029
LR  - 20161125
IS  - 1097-4644 (Electronic)
IS  - 0730-2312 (Linking)
VI  - 114
IP  - 7
DP  - 2013 Jul
TI  - Hydrogen sulfide reduces cell adhesion and relevant inflammatory triggering by 
      preventing ADAM17-dependent TNF-alpha activation.
PG  - 1536-48
LID - 10.1002/jcb.24495 [doi]
AB  - H2S is the third endogenous gaseous mediator, after nitric oxide and carbon 
      monoxide, possessing pleiotropic effects, including cytoprotection and 
      anti-inflammatory action. We analyzed, in an in vitro model entailing monocyte 
      adhesion to an endothelial monolayer, the changes induced by H2S on various 
      potential targets, including cytokines, chemokines, and proteases, playing a 
      crucial role in inflammation and cell adhesion. Results show that H2S prevents 
      the increase in monocyte adhesion induced by tumor necrosis factor-alpha (TNF-alpha). 
      Under these conditions, downregulation of monocyte chemoattractant protein-1 
      (MCP-1), chemokine C-C motif receptor 2, and increase of cluster of 
      differentiation 36 could be detected in monocytes. In endothelial cells, H2 S 
      treatment reduces the increase in MCP-1, inter-cellular adhesion molecule-1, 
      vascular cell adhesion molecule-1, and of a disintegrin and metalloproteinase 
      metallopeptidase domain 17 (ADAM17), both at the gene expression and protein 
      levels. Cystathionine gamma-lyase and 3-mercaptopyruvate sulfurtransferase, the major 
      H2S forming enzymes, are downregulated in endothelial cells. In addition, H2S 
      significantly reduces activation of ADAM17 by PMA in endothelial cells, with 
      consequent reduction of both ADAM17-dependent TNF-alpha ectodomain shedding and MCP-1 
      release. In conclusion, H2S is able to prevent endothelial activation by 
      hampering endothelial activation, triggered by TNF-alpha. The mechanism of this 
      protective effect is mainly mediated by down-modulation of ADAM17-dependent 
      TNF-converting enzyme (TACE) activity with consequent inhibition of soluble TNF-alpha 
      shedding and its relevant MCP-1 release in the medium. These results are 
      discussed in the light of the potential protective role of H2S in 
      pro-inflammatory and pro-atherogenic processes, such as chronic renal failure.
CI  - Copyright (c) 2013 Wiley Periodicals, Inc.
FAU - Perna, Alessandra F
AU  - Perna AF
AD  - First Division of Nephrology, Department of Cardio-thoracic and Respiratory 
      Sciences, Second University of Naples, School of Medicine and Surgery, Naples, 
      Italy. alessandra.perna@unina2.it
FAU - Sepe, Immacolata
AU  - Sepe I
FAU - Lanza, Diana
AU  - Lanza D
FAU - Capasso, Rosanna
AU  - Capasso R
FAU - Zappavigna, Silvia
AU  - Zappavigna S
FAU - Capasso, Giovambattista
AU  - Capasso G
FAU - Caraglia, Michele
AU  - Caraglia M
FAU - Ingrosso, Diego
AU  - Ingrosso D
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Cell Biochem
JT  - Journal of cellular biochemistry
JID - 8205768
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - EC 3.4.24.- (ADAM Proteins)
RN  - EC 3.4.24.86 (ADAM17 Protein)
RN  - EC 3.4.24.86 (ADAM17 protein, human)
RN  - YY9FVM7NSN (Hydrogen Sulfide)
SB  - IM
MH  - ADAM Proteins/genetics/*metabolism
MH  - ADAM17 Protein
MH  - Blotting, Western
MH  - Cell Adhesion/*drug effects
MH  - Cell Line
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Flow Cytometry
MH  - Humans
MH  - Hydrogen Sulfide/*pharmacology
MH  - Inflammation/*metabolism
MH  - Polymerase Chain Reaction
MH  - Tumor Necrosis Factor-alpha/*metabolism
EDAT- 2013/01/09 06:00
MHDA- 2013/10/30 06:00
CRDT- 2013/01/09 06:00
PHST- 2012/09/28 00:00 [received]
PHST- 2012/12/18 00:00 [accepted]
PHST- 2013/01/09 06:00 [entrez]
PHST- 2013/01/09 06:00 [pubmed]
PHST- 2013/10/30 06:00 [medline]
AID - 10.1002/jcb.24495 [doi]
PST - ppublish
SO  - J Cell Biochem. 2013 Jul;114(7):1536-48. doi: 10.1002/jcb.24495.