{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T23:48:44Z","timestamp":1768520924206,"version":"3.49.0"},"reference-count":27,"publisher":"Wiley","issue":"20","license":[{"start":{"date-parts":[[2008,9,25]],"date-time":"2008-09-25T00:00:00Z","timestamp":1222300800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Rapid Comm Mass Spectrometry"],"published-print":{"date-parts":[[2008,10,30]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Transthyretin (TTR) is a sensitive marker of protein\u2010energy malnutrition and changes in serum and expression levels during protein and energy deficiency are well described. However, little is known about structural modifications of TTR during protein and\/or energy deprivation. Therefore, the aim of this study was to determine the effects of protein inadequacies on post\u2010translational modifications of TTR. For this purpose, male Wistar rats were fed a diet with either casein or gelatine as sole protein source subsequent to a protein wash\u2010out period. Changes in TTR serum levels as well as other markers of nutritional status as body weight, food consumption, total serum protein and serum RBP4 levels as well as antioxidative capacity were determined. Post\u2010translational modifications of TTR were examined by matrix\u2010assisted laser desorption\/ionisation time\u2010of\u2010flight mass spectrometry (MALDI\u2010TOFMS) analysis. The rats from the gelatine group revealed a marked change in the post\u2010translational modification pattern of TTR which was reflected by a significant elevation of sulfonated TTR and which was inversely correlated to the antioxidative capacity. Additionally, the elevation of sulfonated TTR was accompanied by a decrease in body weight and food consumption, low antioxidative capacity as well as a deprivation of serum TTR, RBP4 and total serum protein levels in the animals of the gelatine group. Protein\u2010energy malnutrition leads therefore next to changes in TTR serum concentration, also to changes in the post\u2010translational modification pattern of TTR. Such changes are probably induced by protein\u2010energy malnutrition\u2010driven oxidative stress and might be linked to alterations in protein function and stability. Copyright \u00a9 2008 John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/rcm.3728","type":"journal-article","created":{"date-parts":[[2008,9,25]],"date-time":"2008-09-25T13:11:12Z","timestamp":1222348272000},"page":"3270-3274","source":"Crossref","is-referenced-by-count":11,"title":["Structural modifications of serum transthyretin in rats during protein\u2010energy malnutrition"],"prefix":"10.1002","volume":"22","author":[{"given":"Andrea","family":"Henze","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sascha","family":"Rohn","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Beate","family":"Gericke","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jens","family":"Raila","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Florian J.","family":"Schweigert","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,9,25]]},"reference":[{"key":"e_1_2_5_2_2","first-page":"1575","volume":"65","author":"Beck FK","year":"2002","journal-title":"Am. 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