The two calcium-binding proteins, S100A8 and S100A9, are involved in the metabolism of arachidonic acid in human neutrophils (Q28146225)

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M Klempt

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V Kaever

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C Sorg

Journal of Biological Chemistry

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language of work or name

English

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publication date

12 November 1999

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published in

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volume

274

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issue

46

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page(s)

32672-9

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cites work

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Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis

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Monoclonal antibody 5.5 reacts with p8,14, a myeloid molecule associated with some vascular endothelium

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Molecular cloning and expression of a novel keratinocyte protein (psoriasis-associated fatty acid-binding protein [PA-FABP]) that is highly up-regulated in psoriatic skin and that shares similarity to fatty acid-binding proteins

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Control of arachidonate levels within inflammatory cells

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Expression of the calcium-binding proteins MRP8 and MRP14 in monocytes is regulated by a calcium-induced suppressor mechanism

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Recombinant liver fatty acid binding protein interacts with fatty acyl-coenzyme A.

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Leukotriene synthesis in calcium-depleted human neutrophils: arachidonic acid release correlates with calcium influx

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Complex pattern of the myelo-monocytic differentiation antigens MRP8 and MRP14 during chronic airway inflammation

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The heterodimer of the Ca2+-binding proteins MRP8 and MRP14 binds to arachidonic acid

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The fatty acid-binding heterocomplex FA-p34 formed by S100A8 and S100A9 is the major fatty acid carrier in neutrophils and translocates from the cytosol to the membrane upon stimulation

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Oxidation regulates the inflammatory properties of the murine S100 protein S100A8

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Cyclooxygenases-1 and −2 of Endothelial Cells Utilize Exogenous or Endogenous Arachidonic Acid for Transcellular Production of Thromboxane

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