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rdf:type |
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lifeskim:mentions |
umls-concept:C0001480,
umls-concept:C0017963,
umls-concept:C0205245,
umls-concept:C1321758,
umls-concept:C1419881,
umls-concept:C1514562,
umls-concept:C1655807,
umls-concept:C1704675,
umls-concept:C1707271,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
10
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pubmed:dateCreated |
2002-3-4
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pubmed:abstractText |
Human p43 is associated with macromolecular tRNA synthase complex and known as a precursor of endothelial monocyte-activating polypeptide II (EMAP II). Interestingly, p43 is also secreted to induce proinflammatory genes. Although p43 itself seems to be a cytokine working at physiological conditions, most of the functional studies have been obtained with its C-terminal equivalent, EMAP II. To gain an insight into the working mechanism of p43/EMAP II, we used EMAP II and searched for an interacting cell surface molecule. The level of EMAP II-binding molecule(s) was significantly increased in serum-starved tumor cells. Thus, the EMAP II-binding molecule was isolated from the membrane of the serum-starved CEM cell. The isolated protein was determined to be the alpha subunit of ATP synthase. The interaction of EMAP II and alpha-ATP synthase was confirmed by enzyme-linked immunosorbent assay and in vitro pull down assays and blocked with the antibodies raised against EMAP II and alpha-ATP synthase. The binding of EMAP II to the surface of serum-starved cells was inhibited in the presence of soluble alpha-ATP synthase. EMAP II inhibited the growth of endothelial cells, and this effect was relieved by soluble alpha-ATP synthase. Anti-alpha-ATP synthase antibody also showed an inhibitory effect on the proliferation of endothelial cells mimicking the activity of EMAP II. These results suggest the potential interaction of p43/EMAP II with alpha-ATP synthase and its role in the proliferation of endothelial cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP Synthetase Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Serum-Free,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factor Tu,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TUFM protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/small inducible cytokine subfamily...
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8388-94
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11741979-ATP Synthetase Complexes,
pubmed-meshheading:11741979-Amino Acid Sequence,
pubmed-meshheading:11741979-Animals,
pubmed-meshheading:11741979-Antigens, Neoplasm,
pubmed-meshheading:11741979-Aorta,
pubmed-meshheading:11741979-Cattle,
pubmed-meshheading:11741979-Cell Division,
pubmed-meshheading:11741979-Cell Line,
pubmed-meshheading:11741979-Culture Media, Serum-Free,
pubmed-meshheading:11741979-Cytokines,
pubmed-meshheading:11741979-Dose-Response Relationship, Drug,
pubmed-meshheading:11741979-Endothelium, Vascular,
pubmed-meshheading:11741979-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:11741979-Flow Cytometry,
pubmed-meshheading:11741979-Glutathione Transferase,
pubmed-meshheading:11741979-Humans,
pubmed-meshheading:11741979-Microscopy, Confocal,
pubmed-meshheading:11741979-Mitochondrial Proteins,
pubmed-meshheading:11741979-Molecular Sequence Data,
pubmed-meshheading:11741979-Neoplasm Proteins,
pubmed-meshheading:11741979-Peptide Elongation Factor Tu,
pubmed-meshheading:11741979-Protein Binding,
pubmed-meshheading:11741979-Protein Structure, Tertiary,
pubmed-meshheading:11741979-RNA-Binding Proteins,
pubmed-meshheading:11741979-Recombinant Fusion Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation.
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pubmed:affiliation |
Laboratory of Immunology, College of Pharmacy, Seoul National University, Shillimdong, Kwanakgu, Seoul 151-742, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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