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Luca Gallelli,1,2 Erika Cione,3 Tian Wang,4 Leiming Zhang4 1Department of Health Science, School of Medicine, Operative Unit of Clinical Pharmacology, Mater Domini University Hospital, Catanzaro, Italy; 2Research Center FAS@UMG, University Magna Graecia of Catanzaro, Catanzaro, Italy; 3Department of Pharmacy, Health and Nutritional Sciences, Department of Excellence 2018– 2022, University of Calabria, Rende, 87036, CS, Italy; 4Key Laboratory of Molecular Pharmacology and Drug Evaluation (Yantai University), Ministry of Education, School of Pharmacy, Yantai University, Yantai, People’s Republic of ChinaCorrespondence: Luca GallelliDepartment of Health Science, School of Medicine, Operative Unit of Clinical Pharmacology, Mater Domini University Hospital, Catanzaro, ItalyTel +39 0961712322Email gallelli@unicz.itLeiming ZhangKey Laboratory of Molecular Pharmacology and Drug Evaluation (Yantai University), Ministry of Education, School of Pharmacy, Yantai University, Yantai, People’s Republic of ChinaTel +86 5356706066Email zhangleiming2009@126.comAbstract: Saponins are a group of compounds used in clinical practice in the management of several diseases. Escin is a natural mixture of triterpene saponins which mainly consist of several isoforms, in which the α- and β-escin are predominant. β-escin is the major active compound that exerts a therapeutic effect by relieving tissue edema, promoting venous drainage, and reducing inflammation. In this review, we describe the features of its glucocorticoid-like activity that could explain its clinical effects. Using PubMed, Embase Cochrane library and reference lists for articles published until October 01, 2020, we documented that escin is likely able to exert its anti-inflammatory and anti-edematous effects through a glucocorticoid-like activity, but without the development of glucocorticoid-like adverse drug reactions.Keywords: escin, mechanism of action, glucocorticoid-like activity, clinical efficacy

Abstract: All-trans-retinoic acid (atRA), an activated metabolite of vitamin A, is incorporated covalently into proteins both in vivo and in vitro. AtRA reduced the transport activity of the oxoglutarate carrier (OGC) isolated from testes mitochondria to 58% of control via retinoylation reaction. Labeling of testes mitochondrial proteins with 3HatRA demonstrated the binding of atRA to a 31.5 KDa protein. This protein was identified as OGC due to the competition for the labeling reaction with 2-oxoglutarate, the specific OGC substrate. The role of retinoylated proteins is currently being explored and here we have the first evidence that retinoic acids bind directly to OGC and inhibit its activity in rat testes mitochondria via retinoylation reaction. This study indicates the evidence of a specific interaction between atRA and OGC and establishes a novel mechanism for atRA action, which could influence the physiological biosynthesis of testosterone in situations such as retinoic acid treatment. [Copyright &y& Elsevier]