{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T03:04:04Z","timestamp":1788318244564,"version":"build-2803163510"},"reference-count":63,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2024,1,29]],"date-time":"2024-01-29T00:00:00Z","timestamp":1706486400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100010653","name":"Masaryk University","doi-asserted-by":"publisher","award":["MUNI\/A\/1280\/2022"],"award-info":[{"award-number":["MUNI\/A\/1280\/2022"]}],"id":[{"id":"10.13039\/501100010653","id-type":"DOI","asserted-by":"publisher"}]},{"name":"University of Vienna","award":["MUNI\/A\/1280\/2022"],"award-info":[{"award-number":["MUNI\/A\/1280\/2022"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Bafilomycin A1 inhibits V-type H+ ATPases on the molecular level, which acidifies endo-lysosomes. The main objective of the study was to assess the effect of bafilomycin A1 on Ca2+ content, NAADP-induced Ca2+ release, and ATPase activity in rat hepatocytes and human colon cancer samples. Chlortetracycline (CTC) was used for a quantitative measure of stored calcium in permeabilized rat hepatocytes. ATPase activity was determined by orthophosphate content released after ATP hydrolysis in subcellular post-mitochondrial fraction obtained from rat liver as well as from patients\u2019 samples of colon mucosa and colorectal cancer samples. In rat hepatocytes, bafilomycin A1 decreased stored Ca2+ and prevented the effect of NAADP on stored Ca2+. This effect was dependent on EGTA\u2013Ca2+ buffers in the medium. Bafilomycin A1 significantly increased the activity of Ca2+ ATPases of endoplasmic reticulum (EPR), but not plasma membrane (PM) Ca2+ ATPases in rat liver. Bafilomycin A1 also prevented the effect of NAADP on these pumps. In addition, bafilomycin A1 reduced Na+\/K+ ATPase activity and increased basal Mg2+ ATPase activity in the subcellular fraction of rat liver. Concomitant administration of bafilomycin A1 and NAADP enhanced these effects. Bafilomycin A1 increased the activity of the Ca2+ ATPase of EPR in the subcellular fraction of normal human colon mucosa and also in colon cancer tissue samples. In contrast, it decreased Ca2+ ATPase PM activity in samples of normal human colon mucosa and caused no changes in colon cancer. Bafilomycin A1 decreased Na+\/K+ ATPase activity and increased basal Mg2+ ATPase activity in normal colon mucosa samples and in human colon cancer samples. It can be concluded that bafilomycin A1 targets NAADP-sensitive acidic Ca2+ stores, effectively modulates ATPase activity, and assumes the link between acidic stores and EPR. Bafilomycin A1 may be useful for cancer therapy.<\/jats:p>","DOI":"10.3390\/ijms25031657","type":"journal-article","created":{"date-parts":[[2024,1,29]],"date-time":"2024-01-29T08:54:03Z","timestamp":1706518443000},"page":"1657","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Bafilomycin A1 Molecular Effect on ATPase Activity of Subcellular Fraction of Human Colorectal Cancer and Rat Liver"],"prefix":"10.3390","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5107-3352","authenticated-orcid":false,"given":"Solomiia","family":"Bychkova","sequence":"first","affiliation":[{"name":"Department of Human and Animal Physiology, Faculty of Biology, Ivan Franko National University of Lviv, 79005 Lviv, Ukraine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6620-1751","authenticated-orcid":false,"given":"Mykola","family":"Bychkov","sequence":"additional","affiliation":[{"name":"Department of Therapy No. 1, Medical Diagnostic and Hematology and Transfusiology of Faculty of Postgraduate Education, Danylo Halytsky Lviv National Medical University, 79010 Lviv, Ukraine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2435-9726","authenticated-orcid":false,"given":"Dani","family":"Dordevic","sequence":"additional","affiliation":[{"name":"Department of Plant Origin Food Sciences, Faculty of Veterinary Hygiene and Ecology, University of Veterinary Sciences Brno, 612 42 Brno, Czech Republic"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0999-7957","authenticated-orcid":false,"given":"Monika","family":"V\u00edt\u011bzov\u00e1","sequence":"additional","affiliation":[{"name":"Department of Experimental Biology, Faculty of Science, Masaryk University, 625 00 Brno, Czech Republic"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9746-3284","authenticated-orcid":false,"given":"Simon K.-M. 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