{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T14:46:43Z","timestamp":1786978003438,"version":"build-2736575974"},"reference-count":84,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2024,2,19]],"date-time":"2024-02-19T00:00:00Z","timestamp":1708300800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["J Biochem &amp;amp; Molecular Tox"],"published-print":{"date-parts":[[2024,3]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    The present work elucidates the role of colchicine (COL) on albumin glycation and cellular oxidative stress in diabetic cardiomyopathy (DCM). Human serum albumin (HSA) was glycated with methylglyoxal\u00a0in the presence of COL (2.5, 3.75, and 5\u2009\u00b5M), whereas positive and negative control samples were maintained separately. The effects of COL on HSA glycation, structural and functional modifications in glycated HSA were analyzed using different spectroscopical and\u00a0fluorescence techniques. Increased fructosamine, carbonyl, and pentosidine formation in glycated HSA samples were inhibited in the presence of COL. Structural conformation of HSA and glycated HSA samples was examined by field emission scanning electron microscopy, circular dichroism, Fourier transform infrared, and proton nuclear magnetic resonance analyses, where COL maintained both secondary and tertiary structures of HSA against glycation. Functional marker assays included ABTS\n                    <jats:sup>\u2022+<\/jats:sup>\n                    radical scavenging and total antioxidant activities, advanced oxidative protein product formation, and turbidimetry, which showed preserved functional properties of glycated HSA in COL\u2010containing samples. Afterward, rat cardiomyoblast (H9c2 cell line) was treated with glycated HSA\u2013COL complex (400\u2009\u03bcg\/mL) for examining various cellular antioxidants (nitric oxide, catalase, superoxide dismutase, and glutathione) and detoxification enzymes (aldose reductase, glyoxalase I, and\u00a0II) levels. All three concentrations of COL exhibited effective anti\u2010glycation properties, enhanced cellular antioxidant levels, and detoxification enzyme activities. The report comprehensively analyzes the potential anti\u2010glycation and properties of COL during its initial assessment.\n                  <\/jats:p>","DOI":"10.1002\/jbt.23664","type":"journal-article","created":{"date-parts":[[2024,2,19]],"date-time":"2024-02-19T05:00:20Z","timestamp":1708318820000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Protective effect of colchicine on albumin glycation and cellular oxidative stress: Insights into diabetic cardiomyopathy"],"prefix":"10.1002","volume":"38","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8943-1987","authenticated-orcid":false,"given":"Muskan Rajkumar","family":"Thakur","sequence":"first","affiliation":[{"name":"Symbiosis School of Biological Sciences (SSBS) Symbiosis International (Deemed University) (SIU) Pune Maharashtra 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