{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,31]],"date-time":"2026-07-31T22:32:50Z","timestamp":1785537170653,"version":"3.56.0"},"reference-count":26,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2018,11,30]],"date-time":"2018-11-30T00:00:00Z","timestamp":1543536000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100004366","name":"Tabriz University of Medical Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004366","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["iubmb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["IUBMB Life"],"published-print":{"date-parts":[[2019,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Protein acylation is a posttranslational modification in which an amino acid residue of a protein is acylated by a fatty acid. This process plays a key role in regulating proteomic function. Studies of protein acylation have relied on the development and application of extremely complicated molecular methods. However, global protein acylation can be profiled following hydrolysis of fatty acyl groups from cellular proteins. The present study aimed to develop a method for analysis of global protein acylation using gas\u2013liquid chromatography (GLC). The total protein was extracted from the human hepatocellular carcinoma (HepG2) cell line. Protein sedimentation and extensive wash were combined with differential O\u2010, S\u2010, or N\u2010acyl hydrolysis using sodium hydroxide (NaOH), hydroxylamine (NH<jats:sub>2<\/jats:sub>OH), or hydrochloric acid (HCl), respectively. GLC with a flame ionization detector system was used to analyze changes in the fatty acid composition of the released lipids. The effect of selective inhibition of monounsaturated fatty acid (MUFA) synthesis on global protein acylation and the expression of reprogramming markers were determined to further validate the proposed profiling approach. In all hydrolysis conditions, the amount of myristate released was significantly higher than of other fatty acids. Notable differences were observed in the release of individual fatty acids among the hydrolyzing agents. Only NH<jats:sub>2<\/jats:sub>OH could release significant amounts of palmitoleate (&gt;2.5\u2010fold vs. NaOH and HCl). The acylation assay indicates that treatment with a chemical inhibitor of monounsaturated fatty acid synthesis led to an overall increase in saturated fatty acid O\u2010 and N\u2010acylation, and a decrease in palmitoleate O\u2010 and S\u2010acylation of cellular proteins (&lt;\u221215%). This was accompanied by significant reductions in the gene expression of the reprogramming markers <jats:italic>Oct4<\/jats:italic> (\u221226%, <jats:italic>P<\/jats:italic> &lt; 0.01) and <jats:italic>Sox2<\/jats:italic> (\u221240%, <jats:italic>P<\/jats:italic> &lt; 0.01). GLC\u2010based analysis of global protein acylation affords a semi\u2010quantitative method that can be used to assess the gross changes in the protein acylation profile during cell differentiation and reprogramming. \u00a9 2018 IUBMB Life, 71(3):340\u2013346, 2019<\/jats:p>","DOI":"10.1002\/iub.1975","type":"journal-article","created":{"date-parts":[[2018,11,30]],"date-time":"2018-11-30T17:41:25Z","timestamp":1543599685000},"page":"340-346","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["A method for the gross analysis of global protein acylation by gas\u2013liquid chromatography"],"prefix":"10.1002","volume":"71","author":[{"given":"Fatemeh","family":"Mohammadzadeh","sequence":"first","affiliation":[{"name":"Liver and Gastrointestinal Diseases Research Center Tabriz University of Medical Sciences  5166614756, Tabriz 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