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Current knowledge suggests that ZAG mediates progressive weight loss through \u03b2-adrenergic signalling in adipocytes, resulting in the activation of lipolysis and fat mobilization. Here, through cross-linking experiments, amine oxidase copper-containing 3 (AOC3) is identified as a novel ZAG binding partner. AOC3\u2014also known as vascular adhesion protein 1 (VAP-1) and semicarbazide sensitive amine oxidase (SSAO)\u2014deaminates primary amines, thereby generating the corresponding aldehyde, H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    and NH\n                    <jats:sub>3<\/jats:sub>\n                    . It is an ectoenzyme largely expressed by adipocytes and induced in endothelial cells during inflammation. Extravasation of immune cells depends on amine oxidase activity and AOC3-derived H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    has an insulinogenic effect. The observations described here suggest that ZAG acts as an allosteric inhibitor of AOC3 and interferes with the associated pro-inflammatory and anti-lipolytic functions. Thus, inhibition of the deamination of lipolytic hormone octopamine by AOC3 represents a novel mechanism by which ZAG might stimulate lipolysis. Furthermore, experiments involving overexpression of recombinant ZAG reveal that its glycosylation is co-regulated by oxygen availability and that the pattern of glycosylation affects its inhibitory potential. The newly identified protein interaction between AOC3 and ZAG highlights a previously unknown functional relationship, which may be relevant to inflammation, energy metabolism and the development of cachexia.\n                  <\/jats:p>","DOI":"10.1098\/rsob.190035","type":"journal-article","created":{"date-parts":[[2020,4,21]],"date-time":"2020-04-21T19:05:24Z","timestamp":1587495924000},"page":"190035","update-policy":"https:\/\/doi.org\/10.1098\/crossmark-policy","source":"Crossref","is-referenced-by-count":18,"title":["Zinc-\u03b12-glycoprotein as an inhibitor of amine oxidase copper-containing 3"],"prefix":"10.1098","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5586-1172","authenticated-orcid":true,"given":"Matthias","family":"Romauch","sequence":"first","affiliation":[{"name":"Institute of Molecular Biosciences, Karl-Franzens-University, Graz, Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"175","published-online":{"date-parts":[[2020,4,22]]},"reference":[{"key":"e_1_3_5_2_2","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/S0021-9258(18)64243-7","article-title":"Preparation and properties of Zn-\u03b12-glycoprotein of normal human plasma","volume":"236","author":"Burgi W","year":"1961","journal-title":"J. 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