{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,20]],"date-time":"2026-07-20T14:19:03Z","timestamp":1784557143874,"version":"3.55.0"},"reference-count":82,"publisher":"Bioscientifica","issue":"3","content-domain":{"domain":["joe.bioscientifica.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2014,6]]},"abstract":"<jats:p>\n                    Leptin is a potent anorexigen, but little is known about the physiological conditions under which this cytokine regulates food intake in fish. In this study, we characterized the relationships between food intake, O\n                    <jats:sub>2<\/jats:sub>\n                    -carrying capacity, liver leptin-A1 (\n                    <jats:italic>lep-a1<\/jats:italic>\n                    ) gene expression, and plasma leptin-A1 in rainbow trout infected with a pathogenic hemoflagellate,\n                    <jats:italic>Cryptobia salmositica<\/jats:italic>\n                    . As\n                    <jats:italic>lep<\/jats:italic>\n                    gene expression is hypoxia-sensitive and\n                    <jats:italic>Cryptobia<\/jats:italic>\n                    -infected fish are anemic, we hypothesized that\n                    <jats:italic>Cryptobia<\/jats:italic>\n                    -induced anorexia is mediated by leptin. A 14-week time course experiment revealed that\n                    <jats:italic>Cryptobia<\/jats:italic>\n                    -infected fish experience a transient 75% reduction in food intake, a sharp initial drop in hematocrit and hemoglobin levels followed by a partial recovery, a transient 17-fold increase in\n                    <jats:italic>lep-a1<\/jats:italic>\n                    gene expression, and a sustained increase in plasma leptin-A1 levels. In the hypothalamus, peak anorexia was associated with decreases in mRNA levels of neuropeptide Y (\n                    <jats:italic>npy<\/jats:italic>\n                    ) and cocaine- and amphetamine-regulated transcript (\n                    <jats:italic>cart<\/jats:italic>\n                    ), and increases in agouti-related protein (\n                    <jats:italic>agrp<\/jats:italic>\n                    ) and pro-opiomelanocortin A2 (\n                    <jats:italic>pomc<\/jats:italic>\n                    ). In contrast, in non-infected fish pair-fed to infected animals,\n                    <jats:italic>lep-a1<\/jats:italic>\n                    gene expression and plasma levels did not differ from those of non-infected satiated fish. Pair-fed fish were also characterized by increases in hypothalamic\n                    <jats:italic>npy<\/jats:italic>\n                    and\n                    <jats:italic>agrp<\/jats:italic>\n                    , no changes in\n                    <jats:italic>pomc-a2<\/jats:italic>\n                    , and a reduction in\n                    <jats:italic>cart<\/jats:italic>\n                    mRNA expression. Finally, peak infection was characterized by a significant positive correlation between O\n                    <jats:sub>2<\/jats:sub>\n                    -carrying capacity and food intake. These findings show that hypoxemia, and not feed restriction, stimulates leptin-A1 secretion in\n                    <jats:italic>Cryptobia<\/jats:italic>\n                    -infected rainbow trout and suggest that leptin contributes to anorexia by inhibiting hypothalamic\n                    <jats:italic>npy<\/jats:italic>\n                    and stimulating\n                    <jats:italic>pomc-a2<\/jats:italic>\n                    .\n                  <\/jats:p>","DOI":"10.1530\/joe-13-0615","type":"journal-article","created":{"date-parts":[[2014,4,16]],"date-time":"2014-04-16T22:08:10Z","timestamp":1397686090000},"page":"441-455","update-policy":"https:\/\/doi.org\/10.1530\/crossmarkpolicy-1","source":"Crossref","is-referenced-by-count":29,"title":["Hypoxemia-induced leptin secretion: a mechanism for the control of food intake in diseased fish"],"prefix":"10.1530","volume":"221","author":[{"given":"Lauren E","family":"MacDonald","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah L","family":"Alderman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah","family":"Kramer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick T K","family":"Woo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicholas J","family":"Bernier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"416","reference":[{"key":"1_46988653","doi-asserted-by":"crossref","first-page":"1044","DOI":"10.1016\/j.peptides.2010.02.026","volume":"31","year":"2010","journal-title":"Peptides","ISSN":"https:\/\/id.crossref.org\/issn\/0196-9781","issn-type":"print"},{"key":"2_47939918","first-page":"2380","volume":"18","year":"2008","journal-title":"Journal of 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