{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T00:35:43Z","timestamp":1788482143256,"version":"build-2803163510"},"reference-count":33,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2011,11,18]],"date-time":"2011-11-18T00:00:00Z","timestamp":1321574400000},"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":[[2012,4]]},"abstract":"<jats:p>The aim of the present studies was to determine whether the mechanism of biological action of garlic\u2010derived sulfur compounds in human hepatoma (HepG2) cells can be dependent on the presence of labile sulfane sulfur in their molecules. We investigated the effect of allyl sulfides from garlic: monosulfide, disulfide and trisulfide on cell proliferation and viability, caspase 3 activity and hydrogen peroxide (H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub>) production in HepG2 cells. In parallel, we also examined the influence of the previously mentioned compounds on the levels of thiols, glutathione, cysteine and cysteinyl\u2010glycine, and on the level of sulfane sulfur and the activity of its metabolic enzymes: rhodanese, 3\u2010mercaptopyruvate sulfurtransferase and cystathionase. Among the compounds under study, diallyl trisulfide (DATS), a sulfane sulfur\u2010containing compound, showed the highest biological activity in HepG2 cells. This compound increased the H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub> formation, lowered the thiol level and produced the strongest inhibition of cell proliferation and the greatest induction of caspase 3 activity in HepG2 cells. DATS did not affect the activity of sulfurtransferases and lowered sulfane sulfur level in HepG2 cells. It appears that sulfane sulfur containing DATS can be bioreduced in cancer cells to hydroperthiol that leads to H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub> generation, thereby influencing transmission of signals regulating cell proliferation and apoptosis. Copyright \u00a9 2011 John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/cbf.1835","type":"journal-article","created":{"date-parts":[[2011,11,18]],"date-time":"2011-11-18T01:36:49Z","timestamp":1321580209000},"page":"198-204","source":"Crossref","is-referenced-by-count":52,"title":["The effects of garlic\u2010derived sulfur compounds on cell proliferation, caspase 3 activity, thiol levels and anaerobic sulfur metabolism in human hepatoblastoma HepG2 cells"],"prefix":"10.1002","volume":"30","author":[{"given":"Ma\u0142gorzata","family":"Iciek","sequence":"first","affiliation":[{"name":"Chair of Medical Biochemistry Medical College of Jagiellonian University  Krak\u00f3w Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Inga","family":"Kwiecie\u0144","sequence":"additional","affiliation":[{"name":"Chair and Department of Pharmaceutical Botany Medical College of Jagiellonian University  Krak\u00f3w Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gra\u017cyna","family":"Chwatko","sequence":"additional","affiliation":[{"name":"Department of Environmental Chemistry University of \u0141\u00f3d\u017a  \u0141\u00f3d\u017a Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria","family":"Soko\u0142owska\u2010Je\u017cewicz","sequence":"additional","affiliation":[{"name":"Chair of Medical Biochemistry Medical College of Jagiellonian University  Krak\u00f3w Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danuta","family":"Kowalczyk\u2010Pachel","sequence":"additional","affiliation":[{"name":"Chair of Medical Biochemistry Medical College of Jagiellonian University  Krak\u00f3w Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hanna","family":"Rokita","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Genetics and Virology, Faculty of Biochemistry, Biophysics and Biotechnology Jagiellonian University  Krak\u00f3w Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2011,11,18]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tifs.2007.07.011"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1002\/em.20474"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.biopha.2004.01.004"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1093\/jn\/136.3.716S"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1038\/scientificamerican0385-114"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/jf60174a007"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1039\/B703832A"},{"key":"e_1_2_7_9_1","first-page":"215","article-title":"Biosynthesis and biological properties of compounds containing highly reactive, reduced sulfane sulfur","volume":"53","author":"Iciek M","year":"2001","journal-title":"Pol J Pharmacol"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj2640625"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/0020-711X(93)90496-2"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1002\/cbf.1262"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1002\/em.20467"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1080\/01635589709514617"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1002\/em.20431"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1093\/carcin\/bgi306"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M501443200"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1158\/0008-5472.CAN-06-0356"},{"key":"e_1_2_7_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.freeradbiomed.2009.12.022"},{"key":"e_1_2_7_20_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0891-5849(03)00144-8"},{"key":"e_1_2_7_21_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bmcl.2005.05.110"},{"key":"e_1_2_7_22_1","doi-asserted-by":"publisher","DOI":"10.1081\/JLC-100103450"},{"key":"e_1_2_7_23_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.chroma.2003.11.030"},{"key":"e_1_2_7_24_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(55)02207-6"},{"key":"e_1_2_7_25_1","doi-asserted-by":"publisher","DOI":"10.1016\/0009-8981(74)90031-X"},{"key":"e_1_2_7_26_1","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/S0021-9258(18)70476-6","article-title":"A crystalline enzyme that cleaves homoserine and cystathionine. 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