PUBLICATION

Dietary Lysine Imbalance Affects Muscle Proteome in Zebrafish (Danio rerio): A Comparative 2D-DIGE Study

Authors
de Vareilles, M., Conceição, L.E., Gómez-Requeni, P., Kousoulaki, K., Richard, N., Rodrigues, P.M., Fladmark, K.E., and Rønnestad, I.
ID
ZDB-PUB-120516-9
Date
2012
Source
Marine biotechnology (New York, N.Y.)   14(5): 643-654 (Journal)
Registered Authors
Keywords
lysine, growth, skeletal muscle, myosin chain isoforms, Pdlim7, zebrafish
MeSH Terms
  • Amino Acids/analysis
  • Animal Feed/analysis
  • Animals
  • Dietary Supplements
  • Electrophoresis, Gel, Two-Dimensional/methods
  • Electrophoresis, Gel, Two-Dimensional/veterinary
  • Image Processing, Computer-Assisted
  • Lysine/administration & dosage
  • Lysine/pharmacology*
  • Muscle, Skeletal/drug effects*
  • Muscle, Skeletal/metabolism
  • Proteome/drug effects*
  • Proteome/metabolism
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/veterinary
  • Zebrafish/metabolism*
PubMed
22580902 Full text @ Mar. Biotechnol.
Abstract

Lysine (Lys) is an indispensable amino acid (AA) and generally the first limiting AA in vegetable protein sources in fish feeds. Inadequate dietary Lys availability may limit protein synthesis, accretion and growth of fish. This experiment aimed to further elucidate the role of Lys imbalance on growth by examining the myotomal muscle proteome of juvenile zebrafish (Danio rerio). Quadruplicate groups of 8 fish were fed either a low-Lys [Lys(), 1.34 g kg1], medium/control (Lys, 2.47 g kg1) or high-Lys [Lys(+), 4.63 g kg1] diet. Fish growth was monitored from 33 to 49 days post-fertilization (dpf) and trunk myotomal muscle proteome of Lys() and Lys(+) treatments were screened by 2D-DIGE and MALDI ToF tandem mass spectrometry. Growth rate was negatively affected by diet Lys(). Out of 527 ± 11 (mean ± S.E.M.) protein spots detected (<10–150 kDa and 4–7 pI value), 30 were over-expressed and 22 under-expressed in Lys() fish (|fold-change| >1.2, p value <0.05). Higher myosin light chains abundance and other myofibrillar proteins in Lys() fish pointed to increased sarcomeric degradation, indicating a higher protein turnover for supplying basal energy-saving metabolism rather than growth and muscle protein accretion. The Lys deficiency also possibly induced a higher feeding activity, reflected in the over-expression of beta enolase and mitochondrial ATP synthase. Contrarily, in the faster growing fish [Lys(+)], over-expression of apolipoprotein A-I, F-actin capping protein and Pdlim7 point to increased energy storage as fat and enhanced muscle growth, particularly by mosaic hyperplasia. Thus using an exploratory approach, this study pinpoints interesting candidates for further elucidating the role of dietary Lys on growth of juvenile fish.

Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping