{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,8]],"date-time":"2026-05-08T23:14:25Z","timestamp":1778282065589,"version":"3.51.4"},"reference-count":48,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2016,11,8]],"date-time":"2016-11-08T00:00:00Z","timestamp":1478563200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cell Biochemistry &amp;amp; Function"],"published-print":{"date-parts":[[2016,12]]},"abstract":"<jats:sec><jats:label\/><jats:p>The goal of the study was to estimate the effect of a selective V\u2010type H<jats:sup>+<\/jats:sup>\u2010ATPase inhibitor bafilomycin A1 and nicotinic acid adenine dinucleotide phosphate (NAADP) on energetic processes in NK\/Ly cell by directly measuring the respiration of isolated mitochondria and ATPase activities.<\/jats:p><jats:p>NAADP (7\u00a0\u03bcM) increased the activity of Na<jats:sup>+<\/jats:sup>\/K<jats:sup>+<\/jats:sup>\u2010ATPase in the postmitochondrial fraction of NK\/Ly cells, but lower concentration of NAADP decreased it (0.1 and 1\u00a0\u03bcM). The increase the activity of plasma membrane Ca<jats:sup>2<\/jats:sup><jats:sup>+<\/jats:sup> ATPase (PMCA) under NAADP application (1 and 7\u00a0\u03bcM) was observed. However, NAADP (1\u00a0\u03bcM) decreased activities of sarcoendoplasmic reticulum Ca<jats:sup>2<\/jats:sup><jats:sup>+<\/jats:sup>\u2010ATPase (SERCA) and basal Mg<jats:sup>2<\/jats:sup><jats:sup>+<\/jats:sup>\u2010ATPase. Bafilomycin A1 (1\u00a0\u03bcM) increased the activity of Na<jats:sup>+<\/jats:sup>\/K<jats:sup>+<\/jats:sup>\u2010ATPase and potentiated the effect of NAADP (1\u00a0\u03bcM) on this pump. At the same time, bafilomycin A1 (1\u00a0\u03bcM) completely prevented all effects of NAADP (1\u00a0\u03bcM) on activities of PMCA, SERCA, and basal Mg<jats:sup>2<\/jats:sup><jats:sup>+<\/jats:sup>\u2010ATPase, confirming that these effects are dependent on acidic stores.<\/jats:p><jats:p>Bafilomycin A1 or NAADP decreased respiratory and oxidative phosphorylation rates in NK\/Ly mitochondria when \u03b1\u2010ketoglutarate was used as substrate in contrast to succinate. Thus, \u03b1\u2010ketoglutarate oxidation is more sensitive to bafilomycin A1 and NAADP influences compared with succinate oxidation. However, bafilomycin A1\u00a0+\u00a0NAADP and any of these compounds separately lead to full uncoupling of mitochondria after ADP addition irrespectively to substrate used. Bafilomycin A1 affects isolated tumor mitochondria more effectively in combination with NAADP. Bafilomycin and NAADP alter some membrane\u2010associated ATPases and inhibit respiration in mitochondria of the Nemeth\u2010Kellner lymphoma.<\/jats:p><\/jats:sec><jats:sec><jats:title>Significance of research paragraph<\/jats:title><jats:p>Bafilomycin A1 potentiates the effect of NAADP by inhibiting the mitochondrial energetic process in lymphoma cells and activity of Na<jats:sup>+<\/jats:sup>\/K<jats:sup>+<\/jats:sup>\u2010ATPase. The obtained data show promising possibility to use bafilomycin A1 and NAADP as chemotherapeutic agents for lymphoma cells treatment. This is important because lymphomas are seventh most common form of cancer. Today the lymphoma mortality is 15% to 30%, whereas the effectiveness of malignant neoplasms treatment is less than 50%.<\/jats:p><\/jats:sec>","DOI":"10.1002\/cbf.3231","type":"journal-article","created":{"date-parts":[[2016,11,8]],"date-time":"2016-11-08T03:27:02Z","timestamp":1478575622000},"page":"579-587","source":"Crossref","is-referenced-by-count":7,"title":["Effect of bafilomycin and NAADP on membrane\u2010associated ATPases and respiration of isolated mitochondria of the murine Nemeth\u2010Kellner lymphoma"],"prefix":"10.1002","volume":"34","author":[{"given":"V.","family":"Hreniukh","sequence":"first","affiliation":[{"name":"Ivan Franko National University of Lviv  4, Hrushevskyi St. Lviv 79005 Ukraine"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S.","family":"Bychkova","sequence":"additional","affiliation":[{"name":"Ivan Franko National University of Lviv  4, Hrushevskyi St. Lviv 79005 Ukraine"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"O.","family":"Kulachkovsky","sequence":"additional","affiliation":[{"name":"Ivan Franko National University of Lviv  4, Hrushevskyi St. Lviv 79005 Ukraine"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A.","family":"Babsky","sequence":"additional","affiliation":[{"name":"Ivan Franko National University of Lviv  4, Hrushevskyi St. Lviv 79005 Ukraine"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2016,11,8]]},"reference":[{"key":"e_1_2_7_2_1","first-page":"16","volume-title":"World Cancer Report 2014","author":"Forman D","year":"2014"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1186\/2049-3002-2-8"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1248\/bpb.33.743"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrc2254"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200801099"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1152\/ajpcell.00407.2003"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1007\/s10565-008-9085-7"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1042\/BST0340922"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.R500012200"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1038\/18032"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.18632\/oncotarget.1699"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2407-14-716"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.4161\/cbt.4.1.1505"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1517\/14728222.12.11.1403"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1021\/cb500665r"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.4236\/ojbd.2013.33A001"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cellbi.2008.06.002"},{"key":"e_1_2_7_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)52451-6"},{"key":"e_1_2_7_20_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)84756-1"},{"key":"e_1_2_7_21_1","doi-asserted-by":"publisher","DOI":"10.1161\/01.RES.0000047507.22487.85"},{"key":"e_1_2_7_22_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M110.125864"},{"key":"e_1_2_7_23_1","doi-asserted-by":"publisher","DOI":"10.2337\/db07-0443"},{"key":"e_1_2_7_24_1","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1681\/ASN.V12154","article-title":"Nicotinic acid adenine dinucleotide phosphate: a new Ca2\n                  + releasing agent in kidney","volume":"12","author":"Cheng J","year":"2001","journal-title":"J Am Soc Nephrol"},{"key":"e_1_2_7_25_1","doi-asserted-by":"publisher","DOI":"10.1042\/0264-6021:3620125"},{"key":"e_1_2_7_26_1","doi-asserted-by":"publisher","DOI":"10.1042\/BJ20051002"},{"key":"e_1_2_7_27_1","doi-asserted-by":"publisher","DOI":"10.1152\/ajpcell.00638.2005"},{"key":"e_1_2_7_28_1","doi-asserted-by":"publisher","DOI":"10.15407\/ubj86.05.065"},{"key":"e_1_2_7_29_1","doi-asserted-by":"publisher","DOI":"10.1177\/153537020122600606"},{"key":"e_1_2_7_30_1","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/S0021-9258(19)57191-5","article-title":"Respiratory enzymes in oxidative phosphorylation. 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