title: Chronic protein deficiency differentially affects the kinetics of plasma proteins in young pigs.
abstract: The use of plasma protein concentrations to assess protein-nutritional status has been questioned because concentrations and kinetics are affected by factors other than protein intake. To determine the effect of protein deficiency on plasma protein concentration and synthesis, two groups of four piglets consumed diets containing either 20 or 3% protein. After 8 wk, 2H3-leucine was infused intravenously to measure the fractional and absolute synthesis rates (FSR and ASR) of albumin, transferrin, retinol binding protein (RBP), transthyretin (TTR), a new peptide called TTR2, the high density apolipoprotein (HDL-apoA-1), fibrinogen, and haptoglobin. Compared with controls, protein-deficient pigs had significantly lower (P < 0.05) plasma albumin, RBP and TTR2 concentrations, significantly slower (P < 0.05) FSR of fibrinogen, HDL-apoA-1, transferring and TTR2, significantly lower (P < 0.05) ASR of albumin, fibrinogen, transferrin, and TTR2, and a significantly higher (P < 0.05) ASR of TTR. Fibrinogen and transferrin concentrations did not differ between groups, but transthyretin concentration was higher in protein-deficient pigs. These results suggest that protein-nutritional status cannot be predicted from the concentrations of all plasma proteins, that chronic protein deficiency affects the rate of synthesis of only some plasma proteins, and that the kinetic response of plasma proteins to protein restriction cannot be predicted from measurements of plasma concentrations.
authors.affiliation: USDA/Agricultural Research Service Children's Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine, Houston, TX 77030, USA.
authors.forename: F
authors.initials: F
authors.lastname: Jahoor
authors.forename: S
authors.initials: S
authors.lastname: Bhattiprolu
authors.forename: M
authors.initials: M
authors.lastname: Del Rosario
authors.forename: D
authors.initials: D
authors.lastname: Burrin
authors.forename: L
authors.initials: L
authors.lastname: Wykes
authors.forename: M
authors.initials: M
authors.lastname: Frazer
mesh_terms: D000375:Aging / Q000378:metabolism* / Q000502:physiology; D000818:Animals; D016632:Apolipoprotein A-I / Q000096:biosynthesis / Q000378:metabolism; D001798:Blood Proteins / Q000096:biosynthesis / Q000378:metabolism*; D005260:Female; D005340:Fibrinogen / Q000096:biosynthesis / Q000378:metabolism; D006242:Haptoglobins / Q000096:biosynthesis / Q000378:metabolism; D007930:Leucine; D008297:Male; D011228:Prealbumin / Q000096:biosynthesis / Q000378:metabolism; D011488:Protein Deficiency / Q000378:metabolism* / Q000503:physiopathology; D012177:Retinol-Binding Proteins / Q000096:biosynthesis / Q000378:metabolism; D054839:Retinol-Binding Proteins, Plasma; D012709:Serum Albumin / Q000096:biosynthesis / Q000378:metabolism; D013552:Swine; D014168:Transferrin / Q000096:biosynthesis / Q000378:metabolism; D014316:Tritium
chemical_list: D016632:Apolipoprotein A-I; D001798:Blood Proteins; D006242:Haptoglobins; D011228:Prealbumin; D012177:Retinol-Binding Proteins; D054839:Retinol-Binding Proteins, Plasma; D012709:Serum Albumin; D014168:Transferrin; D014316:Tritium; D005340:Fibrinogen; D007930:Leucine