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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0018437,
umls-concept:C0023688,
umls-concept:C0085983,
umls-concept:C0185117,
umls-concept:C0205148,
umls-concept:C0205314,
umls-concept:C0330390,
umls-concept:C0596402,
umls-concept:C0679622,
umls-concept:C1711351,
umls-concept:C2911684
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pubmed:issue |
1
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pubmed:dateCreated |
1994-7-21
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pubmed:abstractText |
Extracellular adenosine triphosphate (eATP) has been suggested to play a role in lymphocyte-induced tumor destruction. We now provide evidence that a protein responsible for ATP synthesis in mitochondria may also play a physiologic role in major histocompatibility complex-independent, lymphocyte-mediated cytotoxicity. A 51.5-kD protein (p51.5) bearing structural and immunologic characteristics of the beta subunit of H+ transporting ATP synthase (E.C. 3.6.1.34, beta-H+ATPase, published molecular mass of 51.6 kD) was detected on the plasma membrane of three different human tumor cell lines studied. NH2-terminal amino acid sequence analysis of purified p51.5 from K562 tumor cells revealed 100% homology of 16 residues identified in the first 21 positions to the known sequence of human mitochondrial beta-H+ ATPase. Antibody directed against a 21-mer peptide in the ATP binding region of beta-H+ ATPase (anti-beta) reacted with only one band on Western blots of whole tumor extracts and tumor membrane extracts suggesting that the antiserum reacts with a single species of protein. Anti-beta reacted with the cell membranes of tumor cells as determined by fluorescence-activated flow cytometry and immunoprecipitated a 51.5-kD protein from surface-labeled neoplastic cells (but not human erythrocytes and lymphocytes). Purified p51.5 bound to human lymphocytes and inhibited natural killer (NK) cell-mediated cytotoxicity. Furthermore, anti-beta treatment of the K562 and A549 tumor cell lines inhibited NK (by > 95%) and interleukin 2-activated killer (LAK) cell (by 75%) cytotoxicity, respectively. Soluble p51.5 upon binding to lymphocytes retained its reactivity to anti-beta suggesting that the ATP binding domain and the lymphocyte-receptor binding domain reside in distinct regions of the ligand. These results suggest that beta-H+ ATPase or a nearly identical molecule is an important ligand in the effector phase (rather than the recognition phase) of a cytolytic pathway used by naive NK and LAK cells.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-1400352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-149996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-1514691,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-1694760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-17602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-1918978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-1970818,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2146684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2188665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2206271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2318978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2384670,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2506276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2531032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2538470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2578514,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2683611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2789252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2791674,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2794864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2862839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2863171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2900241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-2907720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-3076768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-3518752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-388439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-3904772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-4212208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-4631074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-6171640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-6180023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-6297790,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-6312454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-6594338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-6756946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-762092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-7682037,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-8376943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-8486720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-8486923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8006588-942051
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0022-1007
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
180
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
273-81
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8006588-Amino Acid Sequence,
pubmed-meshheading:8006588-Cytotoxicity, Immunologic,
pubmed-meshheading:8006588-Humans,
pubmed-meshheading:8006588-Leukemia, Erythroblastic, Acute,
pubmed-meshheading:8006588-Ligands,
pubmed-meshheading:8006588-Membrane Proteins,
pubmed-meshheading:8006588-Molecular Sequence Data,
pubmed-meshheading:8006588-Neoplasm Proteins,
pubmed-meshheading:8006588-Proton-Translocating ATPases,
pubmed-meshheading:8006588-T-Lymphocytes,
pubmed-meshheading:8006588-Tumor Cells, Cultured
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pubmed:year |
1994
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pubmed:articleTitle |
A novel ligand in lymphocyte-mediated cytotoxicity: expression of the beta subunit of H+ transporting ATP synthase on the surface of tumor cell lines.
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pubmed:affiliation |
Department of Medicine, State University of New York Health Science Center at Brooklyn 11203.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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