{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T01:38:57Z","timestamp":1787017137442,"version":"build-2736575974"},"reference-count":77,"publisher":"Canadian Science Publishing","issue":"2","license":[{"start":{"date-parts":[[2024,2,1]],"date-time":"2024-02-01T00:00:00Z","timestamp":1706745600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.nrcresearchpress.com\/page\/about\/CorporateTextAndDataMining"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["HL-74185, HL-139047, DK116591, and AR-71789"],"award-info":[{"award-number":["HL-74185, HL-139047, DK116591, and AR-71789"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["cdnsciencepub.com"],"crossmark-restriction":false},"short-container-title":["Can. J. Physiol. Pharmacol."],"published-print":{"date-parts":[[2024,2,1]]},"abstract":"<jats:p>\n                    Previous studies from our laboratory revealed that the gaseous molecule hydrogen sulfide (H\n                    <jats:sub>2<\/jats:sub>\n                    S), a metabolic product of epigenetics, involves trans-sulfuration pathway for ensuring metabolism and clearance of homocysteine (Hcy) from body, thereby mitigating the skeletal muscle\u2019s pathological remodeling. Although the master circadian clock regulator that is known as brain and muscle aryl hydrocarbon receptor nuclear translocator like protein 1 (i.e., BMAL 1) is associated with S-adenosylhomocysteine hydrolase (SAHH) and Hcy metabolism but how trans-sulfuration pathway is influenced by the circadian clock remains unexplored. We hypothesize that alterations in the functioning of circadian clock during sleep and wake cycle affect skeletal muscle\u2019s biology. To test this hypothesis, we measured serum matrix metalloproteinase (MMP) activities using gelatin gels for analyzing the MMP-2 and MMP-9. Further, employing casein gels, we also studied MMP-13 that is known to be influenced by the growth arrest and DNA damage-45 (GADD45) protein during sleep and wake cycle. The wild type and cystathionine \u03b2 synthase-deficient (CBS\n                    <jats:sup>\u2212\/+<\/jats:sup>\n                    ) mice strains were treated with H\n                    <jats:sub>2<\/jats:sub>\n                    S and subjected to measurement of trans-sulfuration factors from skeletal muscle tissues. The results suggested highly robust activation of MMPs in the wake mice versus sleep mice, which appears somewhat akin to the \u201c1-carbon metabolic dysregulation\u201d, which takes place during remodeling of extracellular matrix during muscular dystrophy. Interestingly, the levels of trans-sulfuration factors such as CBS, cystathionine \u03b3 lyase (CSE), methyl tetrahydrofolate reductase (MTHFR), phosphatidylethanolamine N-methyltransferase (PEMT), and Hcy-protein bound paraoxonase 1 (PON1) were attenuated in CBS\n                    <jats:sup>\u2212\/+<\/jats:sup>\n                    mice. However, treatment with H\n                    <jats:sub>2<\/jats:sub>\n                    S mitigated the attenuation of the trans-sulfuration pathway. In addition, levels of mitochondrial peroxisome proliferator-activated receptor-gamma coactivator 1-\u03b1 (PGC 1-\u03b1) and mitofusin-2 (MFN-2) were significantly improved by H\n                    <jats:sub>2<\/jats:sub>\n                    S intervention. Our findings suggest participation of the circadian clock in trans-sulfuration pathway that affects skeletal muscle remodeling and mitochondrial regeneration.\n                  <\/jats:p>","DOI":"10.1139\/cjpp-2023-0186","type":"journal-article","created":{"date-parts":[[2023,11,18]],"date-time":"2023-11-18T16:34:05Z","timestamp":1700325245000},"page":"105-115","update-policy":"https:\/\/doi.org\/10.1139\/csp-crossmark-policy","source":"Crossref","is-referenced-by-count":2,"title":["Role of circadian clock system in the mitochondrial trans-sulfuration pathway and tissue remodeling"],"prefix":"10.1139","volume":"102","author":[{"given":"Suresh C.","family":"Tyagi","sequence":"first","affiliation":[{"name":"Department of Physiology, School of Medicine, University of Louisville","place":["Louisville, USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sathnur","family":"Pushpakumar","sequence":"additional","affiliation":[{"name":"Department of Physiology, School of 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