Effect of serum amyloid A on selected in vitro functions of isolated human neutrophils

Moshe E. Gatt; Simcha Urieli-Shoval; Liana Preciado-Patt; Mati Fridkin; Sima Calco; Yehudit Azar; Yaacov Matzner

doi:10.1016/S0022-2143(98)90112-3

Effect of serum amyloid A on selected in vitro functions of isolated human neutrophils

Moshe E. Gatt, Simcha Urieli-Shoval, Liana Preciado-Patt, Mati Fridkin, Sima Calco, Yehudit Azar, Yaacov Matzner^*

^*Corresponding author for this work

Faculty of Medicine

Research output: Contribution to journal › Article › peer-review

48 Scopus citations

Abstract

Serum amyloid A (SAA) is an acute phase reactant whose levels in the blood rise as part of the body's response to stress and inflammation. Previous studies have suggested that SAA may carry an anti-inflammatory potential. We evaluated the effects of SAA on human neutrophils activated by N-formyl-methionyl-leucyl-phenylalanine (fMLP) in vitro. At concentrations higher than 10 μg/mL, SAA inhibited neutrophil myeloperoxidase (MPO) release. This effect was located in the N-terminal-that is, amino acid residues 1-14 - of the SAA molecule. Directed neutrophil migration was inhibited at the same SAA concentrations. Several amino acid residues (1 - 14, 15-104, 83-104) contributed to this effect. Neutrophil O₂- production was inhibited at low concentrations of SAA (0.1 to 1 μg/ml) and was stimulated at concentrations higher than 50 μg/mL. Neutrophil O₂^- production induced by phorbol myristate acetate (PMA) and O₂^- generated by the xanthine-xanthine oxidase reaction were not affected by SAA. These results add to previous data suggesting that SAA, at concentrations recorded in the serum during inflammation, modulates neutrophil function; thus it may play a role in the down-regulation of the inflammatory process.

Original language	American English
Pages (from-to)	414-420
Number of pages	7
Journal	Journal of Laboratory and Clinical Medicine
Volume	132
Issue number	5
DOIs	https://doi.org/10.1016/S0022-2143(98)90112-3
State	Published - Nov 1998

Bibliographical note

Funding Information:
N eutrophils are essential components of the host defense dedicated to the destruction of invading pathogens. They are present in large amounts in the circulation and rapidly migrate to tissue on invasion of certain microorganisms. 1 The complex process of their phagocytic action includes, in addition to migration and adhesion, ingestion (phagocytosis), granule enzyme release (degranulation), respiratory From the Hematology Unit, Hadassah University Hospital, Mount Scopus, Jerusalem; and the Department of Organic Chemistry,W eiz-mann Institute of Science, Rehovot. Supported by the Israel Ministry of Absorption and the Israel Cancer Association. Submitted for publication December3 , 1997; revision submittedJ une 25, 1998; acceptedJ une 29, 1998. Reprint requests: Yaacov Matzner, MD, HematologyU nit, Hadassah University Hospital, Mount Scopus, Jerusalem, Israel 91240. Copyright © 1998 by Mosby, Inc. 0022-2143/98 $5.00 + 0 5/1/92789

Access to Document

10.1016/S0022-2143(98)90112-3

Cite this

@article{482112eb43674bb4be6941209e16328e,

title = "Effect of serum amyloid A on selected in vitro functions of isolated human neutrophils",

abstract = "Serum amyloid A (SAA) is an acute phase reactant whose levels in the blood rise as part of the body's response to stress and inflammation. Previous studies have suggested that SAA may carry an anti-inflammatory potential. We evaluated the effects of SAA on human neutrophils activated by N-formyl-methionyl-leucyl-phenylalanine (fMLP) in vitro. At concentrations higher than 10 μg/mL, SAA inhibited neutrophil myeloperoxidase (MPO) release. This effect was located in the N-terminal-that is, amino acid residues 1-14 - of the SAA molecule. Directed neutrophil migration was inhibited at the same SAA concentrations. Several amino acid residues (1 - 14, 15-104, 83-104) contributed to this effect. Neutrophil O2- production was inhibited at low concentrations of SAA (0.1 to 1 μg/ml) and was stimulated at concentrations higher than 50 μg/mL. Neutrophil O2- production induced by phorbol myristate acetate (PMA) and O2- generated by the xanthine-xanthine oxidase reaction were not affected by SAA. These results add to previous data suggesting that SAA, at concentrations recorded in the serum during inflammation, modulates neutrophil function; thus it may play a role in the down-regulation of the inflammatory process.",

author = "Gatt, {Moshe E.} and Simcha Urieli-Shoval and Liana Preciado-Patt and Mati Fridkin and Sima Calco and Yehudit Azar and Yaacov Matzner",

note = "Funding Information: N eutrophils are essential components of the host defense dedicated to the destruction of invading pathogens. They are present in large amounts in the circulation and rapidly migrate to tissue on invasion of certain microorganisms. 1 The complex process of their phagocytic action includes, in addition to migration and adhesion, ingestion (phagocytosis), granule enzyme release (degranulation), respiratory From the Hematology Unit, Hadassah University Hospital, Mount Scopus, Jerusalem; and the Department of Organic Chemistry,W eiz-mann Institute of Science, Rehovot. Supported by the Israel Ministry of Absorption and the Israel Cancer Association. Submitted for publication December3 , 1997; revision submittedJ une 25, 1998; acceptedJ une 29, 1998. Reprint requests: Yaacov Matzner, MD, HematologyU nit, Hadassah University Hospital, Mount Scopus, Jerusalem, Israel 91240. Copyright {\textcopyright} 1998 by Mosby, Inc. 0022-2143/98 $5.00 + 0 5/1/92789",

year = "1998",

month = nov,

doi = "10.1016/S0022-2143(98)90112-3",

language = "American English",

volume = "132",

pages = "414--420",

journal = "Journal of Laboratory and Clinical Medicine",

issn = "0022-2143",

publisher = "Mosby Inc.",

number = "5",

}

TY - JOUR

T1 - Effect of serum amyloid A on selected in vitro functions of isolated human neutrophils

AU - Gatt, Moshe E.

AU - Urieli-Shoval, Simcha

AU - Preciado-Patt, Liana

AU - Fridkin, Mati

AU - Calco, Sima

AU - Azar, Yehudit

AU - Matzner, Yaacov

N1 - Funding Information: N eutrophils are essential components of the host defense dedicated to the destruction of invading pathogens. They are present in large amounts in the circulation and rapidly migrate to tissue on invasion of certain microorganisms. 1 The complex process of their phagocytic action includes, in addition to migration and adhesion, ingestion (phagocytosis), granule enzyme release (degranulation), respiratory From the Hematology Unit, Hadassah University Hospital, Mount Scopus, Jerusalem; and the Department of Organic Chemistry,W eiz-mann Institute of Science, Rehovot. Supported by the Israel Ministry of Absorption and the Israel Cancer Association. Submitted for publication December3 , 1997; revision submittedJ une 25, 1998; acceptedJ une 29, 1998. Reprint requests: Yaacov Matzner, MD, HematologyU nit, Hadassah University Hospital, Mount Scopus, Jerusalem, Israel 91240. Copyright © 1998 by Mosby, Inc. 0022-2143/98 $5.00 + 0 5/1/92789

PY - 1998/11

Y1 - 1998/11

N2 - Serum amyloid A (SAA) is an acute phase reactant whose levels in the blood rise as part of the body's response to stress and inflammation. Previous studies have suggested that SAA may carry an anti-inflammatory potential. We evaluated the effects of SAA on human neutrophils activated by N-formyl-methionyl-leucyl-phenylalanine (fMLP) in vitro. At concentrations higher than 10 μg/mL, SAA inhibited neutrophil myeloperoxidase (MPO) release. This effect was located in the N-terminal-that is, amino acid residues 1-14 - of the SAA molecule. Directed neutrophil migration was inhibited at the same SAA concentrations. Several amino acid residues (1 - 14, 15-104, 83-104) contributed to this effect. Neutrophil O2- production was inhibited at low concentrations of SAA (0.1 to 1 μg/ml) and was stimulated at concentrations higher than 50 μg/mL. Neutrophil O2- production induced by phorbol myristate acetate (PMA) and O2- generated by the xanthine-xanthine oxidase reaction were not affected by SAA. These results add to previous data suggesting that SAA, at concentrations recorded in the serum during inflammation, modulates neutrophil function; thus it may play a role in the down-regulation of the inflammatory process.

AB - Serum amyloid A (SAA) is an acute phase reactant whose levels in the blood rise as part of the body's response to stress and inflammation. Previous studies have suggested that SAA may carry an anti-inflammatory potential. We evaluated the effects of SAA on human neutrophils activated by N-formyl-methionyl-leucyl-phenylalanine (fMLP) in vitro. At concentrations higher than 10 μg/mL, SAA inhibited neutrophil myeloperoxidase (MPO) release. This effect was located in the N-terminal-that is, amino acid residues 1-14 - of the SAA molecule. Directed neutrophil migration was inhibited at the same SAA concentrations. Several amino acid residues (1 - 14, 15-104, 83-104) contributed to this effect. Neutrophil O2- production was inhibited at low concentrations of SAA (0.1 to 1 μg/ml) and was stimulated at concentrations higher than 50 μg/mL. Neutrophil O2- production induced by phorbol myristate acetate (PMA) and O2- generated by the xanthine-xanthine oxidase reaction were not affected by SAA. These results add to previous data suggesting that SAA, at concentrations recorded in the serum during inflammation, modulates neutrophil function; thus it may play a role in the down-regulation of the inflammatory process.

UR - http://www.scopus.com/inward/record.url?scp=0032213207&partnerID=8YFLogxK

U2 - 10.1016/S0022-2143(98)90112-3

DO - 10.1016/S0022-2143(98)90112-3

M3 - Article

C2 - 9823935

AN - SCOPUS:0032213207

SN - 0022-2143

VL - 132

SP - 414

EP - 420

JO - Journal of Laboratory and Clinical Medicine

JF - Journal of Laboratory and Clinical Medicine

IS - 5

ER -

Effect of serum amyloid A on selected in vitro functions of isolated human neutrophils

Abstract

Bibliographical note

Access to Document

Other files and links

Fingerprint

Cite this