S100A8 and S100A9 inhibit neutrophil oxidative metabolism in-vitro: Involvement of adenosine metabolites

Herve Y. Sroussi, Yu Lu, Qin L. Zhang, Dana Villines, Phillip Marucha

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Neutrophils are short-lived granulocytic cells of the innate immune system specialized in the production of reactive oxygen species. S100A8 and S100A9 and their heterocomplex calprotectin play a role in neutrophil recruitment and represent 40% of neutrophil cytosolic protein weight. The present study was designed to test the effect of S100A8 and S100A9 on the rate of neutrophil oxidative metabolism. It is hypothesized that the two S100 proteins inhibit neutrophil associated oxidation. Granulocytes freshly isolated from healthy volunteers were tested for their ability to oxidize dichlorofluorescindiacetate (DCFH-DA) in-vitro. The data showed that S100A8 and S100A9 inhibited spontaneous and stimulated oxidation of the DCFH-DA probe by neutrophils. The inhibition of neutrophil oxidative metabolism by S100A8 and S100A9 was markedly reduced by the enzymatic activity of adenosine deaminase. Inhibitors of the P1 adenosine receptors also reduced the anti-oxidative effect of S100A8/A9 providing further support for the involvement of adenosine metabolites in S100A8/ A9 anti-oxidative effect.

Original languageEnglish (US)
Pages (from-to)389-396
Number of pages8
JournalFree Radical Research
Volume44
Issue number4
DOIs
StatePublished - 2010
Externally publishedYes

Fingerprint

Metabolites
Metabolism
Adenosine
Neutrophils
Leukocyte L1 Antigen Complex
Enzyme inhibition
Oxidation
Purinergic P1 Receptors
Adenosine Deaminase
S100 Proteins
Immune system
Reactive Oxygen Species
Proteins
Neutrophil Infiltration
Granulocytes
diacetyldichlorofluorescein
In Vitro Techniques
Immune System
Healthy Volunteers
Weights and Measures

Keywords

  • Adenosine
  • Calprotectin
  • DCFH-DA
  • Neutrophil
  • ROS
  • S100A8
  • S100A9

ASJC Scopus subject areas

  • Biochemistry

Cite this

S100A8 and S100A9 inhibit neutrophil oxidative metabolism in-vitro : Involvement of adenosine metabolites. / Sroussi, Herve Y.; Lu, Yu; Zhang, Qin L.; Villines, Dana; Marucha, Phillip.

In: Free Radical Research, Vol. 44, No. 4, 2010, p. 389-396.

Research output: Contribution to journalArticle

Sroussi, Herve Y. ; Lu, Yu ; Zhang, Qin L. ; Villines, Dana ; Marucha, Phillip. / S100A8 and S100A9 inhibit neutrophil oxidative metabolism in-vitro : Involvement of adenosine metabolites. In: Free Radical Research. 2010 ; Vol. 44, No. 4. pp. 389-396.
@article{233abe97698a41e5a230b09f97e582b6,
title = "S100A8 and S100A9 inhibit neutrophil oxidative metabolism in-vitro: Involvement of adenosine metabolites",
abstract = "Neutrophils are short-lived granulocytic cells of the innate immune system specialized in the production of reactive oxygen species. S100A8 and S100A9 and their heterocomplex calprotectin play a role in neutrophil recruitment and represent 40{\%} of neutrophil cytosolic protein weight. The present study was designed to test the effect of S100A8 and S100A9 on the rate of neutrophil oxidative metabolism. It is hypothesized that the two S100 proteins inhibit neutrophil associated oxidation. Granulocytes freshly isolated from healthy volunteers were tested for their ability to oxidize dichlorofluorescindiacetate (DCFH-DA) in-vitro. The data showed that S100A8 and S100A9 inhibited spontaneous and stimulated oxidation of the DCFH-DA probe by neutrophils. The inhibition of neutrophil oxidative metabolism by S100A8 and S100A9 was markedly reduced by the enzymatic activity of adenosine deaminase. Inhibitors of the P1 adenosine receptors also reduced the anti-oxidative effect of S100A8/A9 providing further support for the involvement of adenosine metabolites in S100A8/ A9 anti-oxidative effect.",
keywords = "Adenosine, Calprotectin, DCFH-DA, Neutrophil, ROS, S100A8, S100A9",
author = "Sroussi, {Herve Y.} and Yu Lu and Zhang, {Qin L.} and Dana Villines and Phillip Marucha",
year = "2010",
doi = "10.3109/10715760903431434",
language = "English (US)",
volume = "44",
pages = "389--396",
journal = "Free Radical Research",
issn = "1071-5762",
publisher = "Informa Healthcare",
number = "4",

}

TY - JOUR

T1 - S100A8 and S100A9 inhibit neutrophil oxidative metabolism in-vitro

T2 - Involvement of adenosine metabolites

AU - Sroussi, Herve Y.

AU - Lu, Yu

AU - Zhang, Qin L.

AU - Villines, Dana

AU - Marucha, Phillip

PY - 2010

Y1 - 2010

N2 - Neutrophils are short-lived granulocytic cells of the innate immune system specialized in the production of reactive oxygen species. S100A8 and S100A9 and their heterocomplex calprotectin play a role in neutrophil recruitment and represent 40% of neutrophil cytosolic protein weight. The present study was designed to test the effect of S100A8 and S100A9 on the rate of neutrophil oxidative metabolism. It is hypothesized that the two S100 proteins inhibit neutrophil associated oxidation. Granulocytes freshly isolated from healthy volunteers were tested for their ability to oxidize dichlorofluorescindiacetate (DCFH-DA) in-vitro. The data showed that S100A8 and S100A9 inhibited spontaneous and stimulated oxidation of the DCFH-DA probe by neutrophils. The inhibition of neutrophil oxidative metabolism by S100A8 and S100A9 was markedly reduced by the enzymatic activity of adenosine deaminase. Inhibitors of the P1 adenosine receptors also reduced the anti-oxidative effect of S100A8/A9 providing further support for the involvement of adenosine metabolites in S100A8/ A9 anti-oxidative effect.

AB - Neutrophils are short-lived granulocytic cells of the innate immune system specialized in the production of reactive oxygen species. S100A8 and S100A9 and their heterocomplex calprotectin play a role in neutrophil recruitment and represent 40% of neutrophil cytosolic protein weight. The present study was designed to test the effect of S100A8 and S100A9 on the rate of neutrophil oxidative metabolism. It is hypothesized that the two S100 proteins inhibit neutrophil associated oxidation. Granulocytes freshly isolated from healthy volunteers were tested for their ability to oxidize dichlorofluorescindiacetate (DCFH-DA) in-vitro. The data showed that S100A8 and S100A9 inhibited spontaneous and stimulated oxidation of the DCFH-DA probe by neutrophils. The inhibition of neutrophil oxidative metabolism by S100A8 and S100A9 was markedly reduced by the enzymatic activity of adenosine deaminase. Inhibitors of the P1 adenosine receptors also reduced the anti-oxidative effect of S100A8/A9 providing further support for the involvement of adenosine metabolites in S100A8/ A9 anti-oxidative effect.

KW - Adenosine

KW - Calprotectin

KW - DCFH-DA

KW - Neutrophil

KW - ROS

KW - S100A8

KW - S100A9

UR - http://www.scopus.com/inward/record.url?scp=77949385445&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77949385445&partnerID=8YFLogxK

U2 - 10.3109/10715760903431434

DO - 10.3109/10715760903431434

M3 - Article

C2 - 20166886

AN - SCOPUS:77949385445

VL - 44

SP - 389

EP - 396

JO - Free Radical Research

JF - Free Radical Research

SN - 1071-5762

IS - 4

ER -