Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment: implications for the resolution of inflammation.

Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment: implications for the resolution of inflammation. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment: implications for the resolution of inflammation. Abstract Text:

Yulia Y Tyurina,Liana V Basova,Nagarjun V Konduru,Vladimir A Tyurin,Ala I Potapovich,Peter Cai, Bayir,Detcho Stoyanovsky,Bruce R Pitt,Anna A Shvedova,Bengt Fadeel,Valerian E Kagan,

Macrophage recognition of apoptotic cells depends on externalization of phosphatidylserine (PS), which is normally maintained within the cytosolic leaflet of the plasma membrane by aminophospholipid translocase (APLT). APLT is sensitive to redox modifications of its -SH groups. Because activated macrophages produce reactive oxygen and nitrogen species, we hypothesized that macrophages can directly participate in apoptotic cell clearance by S-nitrosylation/oxidation and inhibition of APLT causing PS externalization. Here we report that exposure of target HL-60 cells to nitrosative stress inhibited APLT, induced PS externalization, and enhanced recognition and elimination of "nitrosatively" modified cells by RAW 264.7 macrophages. Using S-nitroso-L-cysteine-ethyl ester (SNCEE) and S-nitrosoglutathione (GSNO) that cause intracellular and extracellular trans-nitrosylation of proteins, respectively, we found that SNCEE (but not GSNO) caused significant S-nitrosylation/oxidation of thiols in HL-60 cells. SNCEE also strongly inhibited APLT, activated scramblase, and caused PS externalization. However, SNCEE did not induce caspase activation or nuclear condensation/fragmentation suggesting that PS externalization was dissociated from the common apoptotic pathway. Dithiothreitol reversed SNCEE-induced S-nitrosylation, APLT inhibition, and PS externalization. SNCEE but not GSNO stimulated phagocytosis of HL-60 cells. Moreover, phagocytosis of target cells by lipopolysaccharide-stimulated macrophages was significantly suppressed by an NO. scavenger, DAF-2. Thus, macrophage-induced nitrosylation/oxidation plays an important role in cell clearance, and hence in the resolution of inflammation.

Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment: implications for the resolution of inflammation. Publishing Authors By Initials

YY Tyurina,LV Basova,NV Konduru,VA Tyurin,AI Potapovich,P Cai,H Bayir,D Stoyanovsky,BR Pitt,AA Shvedova,B Fadeel,VE Kagan,

For similar s-nitrosothiols: s-nitrosoglutathione research abstracts see: s-nitrosothiols: s-nitrosoglutathione research

PUBMED ID PMID:

MEDLINE DATE:

Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment: implications for the resolution of inflammation. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 8498-509

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 17

MONTH: 01

YEAR: 2007

Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment: implications for the resolution of inflammation. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment: implications for the resolution of inflammation. Keywords Mesh Terms:

KEYWORDS: S-Nitrosoglutathione

MESH TERMS: chemistry

Chemical & Substance for Abstract: Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment: implications for the resolution of inflammation. Information

Substance Name: Caspase 7

Registry Number: EC 3.4.22.-

Grant and Affiliation Information for Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment: implications for the resolution of inflammation.

AFFILIATION: Center for Free Radical and Antioxidant Health, Department of Environmental and Occupational Health, and Cancer Institute, University of Pittsburgh, Pittsburgh, Pennsylvania 15219, USA.

Country: United States

AGENCY: United States NIAID

GRANT: U19 AI068021

ACRONYM: AI

MEDLINETA: J Biol Chem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment: implications for the resolution of inflammation Related Publications

• A method for the determination of gentisic acid in serum.
• Application of the ICF in aphasia.
• Cardiolipin switch in mitochondria: shutting off the reduction of cytochrome c and turning on the peroxidase activity.
• Cardiolipin-specific peroxidase reactions of cytochrome C in mitochondria during irradiation-induced apoptosis.
• Commentary on dose escalation and biochemical failure in prostate cancer: in regard to eade et Al. (Int j radiat oncol biol phys 2007;68:682-689).
• Developing a multidisciplinary geriatric oncology program in a community cancer center.
• Feeling listened to: a lived experience of humanbecoming.
• Influenzal meningitis, recovery of a case of 4 weeks' duration with the use of a new drug, polymyxin B (aerosporin).
• Interactions of cardiolipin and lyso-cardiolipins with cytochrome c and tBid: conflict or assistance in apoptosis.
• Is a relay mechanism of antioxidant effect of tocopherols valuable for membrane systems?
• Layer-by-layer growth of metal-metal bonded supramolecular thin films and its use in the fabrication of lateral nanoscale devices.
• Lysyl oxidase: an oxidative enzyme and effector of cell function.
• Mitochondrial targeting of selective electron scavengers: synthesis and biological analysis of hemigramicidin-TEMPO conjugates.
• National Burn Repository 2006: a ten-year review.
• Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment: implications for the resolution of inflammation.
• Selective early cardiolipin peroxidation after traumatic brain injury: an oxidative lipidomics analysis.
• Structural requirements for optimized delivery, inhibition of oxidative stress, and antiapoptotic activity of targeted nitroxides.
• Targeting mitochondria.
• The hierarchy of structural transitions induced in cytochrome c by anionic phospholipids determines its peroxidase activation and selective peroxidation during apoptosis in cells.
• Toxicology of the antibiotics.
• Traumatic brain injury in older adults: epidemiology, outcomes, and future implications.
• Using the proper vocabulary.
• [Control of anaerobic preparations (on the 40th anniversary of the State Scientific Control Institute of Veterinary Preparations)]
• [Emphysematous carbuncle]
• [Epizootiology and prevention of anaerobic spore infections]
• [Pharmacology of sulfanilamides.]
• [RESULTS OF THE STUDY OF THE ULTRAFINE STRUCTURE OF HUMAN SPERMATOZOA IN OLIGOZOOSPERMIA AND NECROSPERMIA.]
• [Simple methods of water.]
• [Technic of renal surgery with the use of heterogenic fibrin pellicle; experimental research.]
• [Virulence of Clostridium perfringens D-the pathogene of sheep enterotexemia]