Abstract
We report the characterization of a cDNA induced in mouse macrophages that encodes a 332-amino acid protein with extensive sequence identity with members of the mammalian nudC-like genes. The interaction between mNUDC and the regulatory beta subunit of platelet activating factor acetylhydrolase I (PAF-AH(I)) shown in this article indicates a new function of NUDC. Thus, we show that NUDC increases the catalytic activity of PAF-AH(I) and that this regulatory activity is located in the carboxyl terminal half of the protein which is highly conserved. This suggests a novel function for mammalian nudC-like genes as anti-inflammatory proteins.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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1-Alkyl-2-acetylglycerophosphocholine Esterase / metabolism*
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Amino Acid Sequence
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Animals
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Binding Sites
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Cell Cycle Proteins / genetics*
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Cell Cycle Proteins / isolation & purification
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Cell Cycle Proteins / metabolism
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Cell Cycle Proteins / physiology*
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Cells, Cultured
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Emericella / genetics
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Inflammation / enzymology
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Inflammation / genetics*
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Macrophages / enzymology
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Macrophages / metabolism*
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Mice
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Molecular Sequence Data
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Nuclear Proteins / genetics*
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Nuclear Proteins / isolation & purification
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Nuclear Proteins / metabolism
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Nuclear Proteins / physiology*
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Protein Binding
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Protein Subunits / metabolism
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Sequence Homology, Amino Acid
Substances
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Cell Cycle Proteins
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Nuclear Proteins
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Nudc protein, mouse
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Protein Subunits
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1-Alkyl-2-acetylglycerophosphocholine Esterase