PubMed:11741979 JSONTXT

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":113,"end":129},"obj":"Cell"},{"id":"T2","span":{"begin":251,"end":259},"obj":"Cell"},{"id":"T4","span":{"begin":756,"end":767},"obj":"Cell"},{"id":"T5","span":{"begin":1307,"end":1324},"obj":"Cell"},{"id":"T6","span":{"begin":1476,"end":1493},"obj":"Cell"},{"id":"T7","span":{"begin":1653,"end":1670},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000115"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000576"},{"id":"A3","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0001054"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0001063"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000115"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000115"},{"id":"A7","pred":"cl_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL:0000115"}],"text":"Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation.\nHuman 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."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":82},"obj":"Sentence"},{"id":"T2","span":{"begin":83,"end":144},"obj":"Sentence"},{"id":"T3","span":{"begin":145,"end":296},"obj":"Sentence"},{"id":"T4","span":{"begin":297,"end":365},"obj":"Sentence"},{"id":"T5","span":{"begin":366,"end":536},"obj":"Sentence"},{"id":"T6","span":{"begin":537,"end":669},"obj":"Sentence"},{"id":"T7","span":{"begin":670,"end":768},"obj":"Sentence"},{"id":"T8","span":{"begin":769,"end":865},"obj":"Sentence"},{"id":"T9","span":{"begin":866,"end":942},"obj":"Sentence"},{"id":"T10","span":{"begin":943,"end":1152},"obj":"Sentence"},{"id":"T11","span":{"begin":1153,"end":1274},"obj":"Sentence"},{"id":"T12","span":{"begin":1275,"end":1385},"obj":"Sentence"},{"id":"T13","span":{"begin":1386,"end":1528},"obj":"Sentence"},{"id":"T14","span":{"begin":1529,"end":1671},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation.\nHuman 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."}

{"project":"FSU-PRGE","denotations":[{"id":"T1","span":{"begin":40,"end":43},"obj":"protein"},{"id":"T2","span":{"begin":52,"end":81},"obj":"protein"},{"id":"T3","span":{"begin":151,"end":154},"obj":"protein"},{"id":"T4","span":{"begin":189,"end":202},"obj":"protein"},{"id":"T5","span":{"begin":239,"end":285},"obj":"protein"},{"id":"T6","span":{"begin":287,"end":294},"obj":"protein"},{"id":"T7","span":{"begin":312,"end":315},"obj":"protein"},{"id":"T8","span":{"begin":375,"end":378},"obj":"protein"},{"id":"T9","span":{"begin":400,"end":408},"obj":"protein"},{"id":"T10","span":{"begin":528,"end":535},"obj":"protein"},{"id":"T11","span":{"begin":586,"end":589},"obj":"protein"},{"id":"T12","span":{"begin":590,"end":597},"obj":"protein"},{"id":"T13","span":{"begin":607,"end":614},"obj":"protein"},{"id":"T14","span":{"begin":683,"end":690},"obj":"protein"},{"id":"T15","span":{"begin":779,"end":786},"obj":"protein"},{"id":"T16","span":{"begin":912,"end":941},"obj":"protein"},{"id":"T17","span":{"begin":962,"end":969},"obj":"protein"},{"id":"T18","span":{"begin":974,"end":992},"obj":"protein"},{"id":"T19","span":{"begin":1121,"end":1128},"obj":"protein"},{"id":"T20","span":{"begin":1133,"end":1151},"obj":"protein"},{"id":"T21","span":{"begin":1168,"end":1175},"obj":"protein"},{"id":"T22","span":{"begin":1255,"end":1273},"obj":"protein"},{"id":"T23","span":{"begin":1275,"end":1282},"obj":"protein"},{"id":"T24","span":{"begin":1366,"end":1384},"obj":"protein"},{"id":"T25","span":{"begin":1391,"end":1409},"obj":"protein"},{"id":"T26","span":{"begin":1520,"end":1527},"obj":"protein"},{"id":"T27","span":{"begin":1580,"end":1583},"obj":"protein"},{"id":"T28","span":{"begin":1584,"end":1591},"obj":"protein"},{"id":"T29","span":{"begin":1597,"end":1615},"obj":"protein"}],"text":"Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation.\nHuman 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."}

{"project":"PIR-corpus2","denotations":[{"id":"T1","span":{"begin":40,"end":43},"obj":"protein"},{"id":"T2","span":{"begin":52,"end":72},"obj":"protein"},{"id":"T3","span":{"begin":151,"end":154},"obj":"protein"},{"id":"T4","span":{"begin":174,"end":210},"obj":"protein"},{"id":"T5","span":{"begin":226,"end":285},"obj":"protein"},{"id":"T6","span":{"begin":312,"end":315},"obj":"protein"},{"id":"T7","span":{"begin":375,"end":378},"obj":"protein"},{"id":"T8","span":{"begin":400,"end":408},"obj":"protein"},{"id":"T9","span":{"begin":528,"end":535},"obj":"protein"},{"id":"T10","span":{"begin":586,"end":589},"obj":"protein"},{"id":"T11","span":{"begin":590,"end":597},"obj":"protein"},{"id":"T12","span":{"begin":607,"end":614},"obj":"protein"},{"id":"T13","span":{"begin":683,"end":710},"obj":"protein"},{"id":"T14","span":{"begin":779,"end":783},"obj":"protein"},{"id":"T15","span":{"begin":912,"end":928},"obj":"protein"},{"id":"T16","span":{"begin":962,"end":969},"obj":"protein"},{"id":"T17","span":{"begin":974,"end":992},"obj":"protein"},{"id":"T18","span":{"begin":1121,"end":1128},"obj":"protein"},{"id":"T19","span":{"begin":1133,"end":1151},"obj":"protein"},{"id":"T20","span":{"begin":1168,"end":1175},"obj":"protein"},{"id":"T21","span":{"begin":1247,"end":1273},"obj":"protein"},{"id":"T22","span":{"begin":1275,"end":1282},"obj":"protein"},{"id":"T23","span":{"begin":1358,"end":1384},"obj":"protein"},{"id":"T24","span":{"begin":1386,"end":1418},"obj":"protein"},{"id":"T25","span":{"begin":1520,"end":1527},"obj":"protein"},{"id":"T26","span":{"begin":1580,"end":1583},"obj":"protein"},{"id":"T27","span":{"begin":1584,"end":1591},"obj":"protein"},{"id":"T28","span":{"begin":1597,"end":1615},"obj":"protein"},{"id":"T31","span":{"begin":145,"end":150},"obj":"long_form"}],"text":"Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation.\nHuman 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."}

{"project":"PIR-corpus1","denotations":[{"id":"T1","span":{"begin":40,"end":43},"obj":"protein"},{"id":"T2","span":{"begin":52,"end":72},"obj":"protein"},{"id":"T3","span":{"begin":151,"end":154},"obj":"protein"},{"id":"T4","span":{"begin":189,"end":210},"obj":"protein"},{"id":"T5","span":{"begin":239,"end":285},"obj":"protein"},{"id":"T6","span":{"begin":287,"end":294},"obj":"acronym"},{"id":"T7","span":{"begin":312,"end":315},"obj":"protein"},{"id":"T8","span":{"begin":375,"end":378},"obj":"protein"},{"id":"T9","span":{"begin":400,"end":408},"obj":"protein"},{"id":"T10","span":{"begin":528,"end":535},"obj":"protein"},{"id":"T11","span":{"begin":586,"end":597},"obj":"protein"},{"id":"T12","span":{"begin":607,"end":614},"obj":"protein"},{"id":"T13","span":{"begin":683,"end":710},"obj":"protein"},{"id":"T14","span":{"begin":779,"end":783},"obj":"protein"},{"id":"T15","span":{"begin":879,"end":886},"obj":"protein"},{"id":"T16","span":{"begin":912,"end":928},"obj":"protein"},{"id":"T17","span":{"begin":962,"end":969},"obj":"protein"},{"id":"T18","span":{"begin":974,"end":992},"obj":"protein"},{"id":"T19","span":{"begin":1095,"end":1105},"obj":"protein"},{"id":"T20","span":{"begin":1121,"end":1128},"obj":"protein"},{"id":"T21","span":{"begin":1133,"end":1151},"obj":"protein"},{"id":"T22","span":{"begin":1168,"end":1175},"obj":"protein"},{"id":"T23","span":{"begin":1255,"end":1273},"obj":"protein"},{"id":"T24","span":{"begin":1275,"end":1282},"obj":"protein"},{"id":"T25","span":{"begin":1366,"end":1384},"obj":"protein"},{"id":"T26","span":{"begin":1386,"end":1418},"obj":"protein"},{"id":"T27","span":{"begin":1520,"end":1527},"obj":"protein"},{"id":"T28","span":{"begin":1580,"end":1591},"obj":"protein"},{"id":"T29","span":{"begin":1597,"end":1615},"obj":"protein"}],"text":"Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation.\nHuman 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."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":756,"end":761},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002664"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation.\nHuman 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."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":756,"end":761},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"}],"text":"Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation.\nHuman 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."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":145,"end":150},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"}],"text":"Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation.\nHuman 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."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":113,"end":129},"obj":"Body_part"},{"id":"T2","span":{"begin":251,"end":259},"obj":"Body_part"},{"id":"T4","span":{"begin":826,"end":834},"obj":"Body_part"},{"id":"T7","span":{"begin":1307,"end":1324},"obj":"Body_part"},{"id":"T8","span":{"begin":1476,"end":1493},"obj":"Body_part"},{"id":"T9","span":{"begin":1653,"end":1670},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000115"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000576"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0001054"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A5","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A6","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000115"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/CL_0000115"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL_0000115"}],"text":"Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation.\nHuman 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."}