Abstract
We have cloned a group of cDNAs representing mRNAs that are rapidly induced following adherence of human monocytes. One of the induced transcripts (MAD-3) encodes a protein of 317 amino acids with one domain containing five tandem repeats of the cdc10/ankyrin motif, which is 60% similar (46% identical) to the ankyrin repeat region of the precursor of NF-kappa B/KBF1 p50. The C-terminus has a putative protein kinase C phosphorylation site. In vitro translated MAD-3 protein was found to specifically inhibit the DNA-binding activity of the p50/p65 NF-kappa B complex but not that of the p50/p50 KBF1 factor or of other DNA-binding proteins. The MAD-3 cDNA encodes an I kappa B-like protein that is likely to be involved in regulation of transcriptional responses to NF-kappa B, including adhesion-dependent pathways of monocyte activation.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Ankyrins
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Base Sequence
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Blood Proteins / physiology
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Blotting, Northern
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Cell Adhesion
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Cloning, Molecular
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DNA / genetics
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DNA-Binding Proteins / genetics*
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DNA-Binding Proteins / metabolism
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DNA-Binding Proteins / physiology
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Gene Expression
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Humans
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I-kappa B Proteins*
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Macromolecular Substances
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Membrane Proteins / physiology
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Molecular Sequence Data
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Monocytes / cytology
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Monocytes / physiology*
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NF-KappaB Inhibitor alpha
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NF-kappa B / antagonists & inhibitors*
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NF-kappa B / metabolism
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RNA, Messenger / genetics
Substances
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Ankyrins
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Blood Proteins
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DNA-Binding Proteins
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I-kappa B Proteins
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Macromolecular Substances
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Membrane Proteins
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NF-kappa B
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NFKBIA protein, human
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RNA, Messenger
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NF-KappaB Inhibitor alpha
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DNA