Aminoacyl-tRNA and tissue free amino acid pools are equilibrated after a flooding dose of phenylalanine

被引:82
作者
Davis, TA [1 ]
Fiorotto, ML [1 ]
Nguyen, HV [1 ]
Burrin, DG [1 ]
机构
[1] Baylor Coll Med, USDA ARS, Childrens Nutr Res Ctr, Dept Pediat, Houston, TX 77030 USA
来源
AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM | 1999年 / 277卷 / 01期
关键词
protein synthesis; skeletal muscle; liver; insulin;
D O I
10.1152/ajpendo.1999.277.1.E103
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
The flooding dose method, which is used to measure tissue protein synthesis, assumes equilibration of the isotopic labeling between the aminoacyl-tRNA pool and the tissue and blood free amino acid pools. However, this has not been verified for a phenylalanine tracer in an in vivo study. We determined the specific radioactivity of [H-3]phenylalanine in the aminoacyl-tRNA and the tissue and blood free amino acid pools of skeletal muscle and liver 30 min after administration of a flooding dose of phenylalanine along with [H-3]phenylalanine. Studies were performed in neonatal pigs in the fasted and refed states and during hyperinsulinemiceuglycemic-amino acid clamps. The results showed that, 30 min after the administration of a flooding dose of phenylalanine, there was equilibration of the specific radioactivity of phenylalanine among the blood, tissue, and tRNA precursor pools. Equilibration of the specific radioactivity of the three precursor pools for protein synthesis occurred in both skeletal muscle and liver. Neither feeding nor insulin status affected the aminoacyl-tRNA specific radioactivity relative to the tissue free amino acid specific radioactivity. The results support the assumption that the tissue free amino acid pool specific radioactivity is a valid measure of the precursor pool specific radioactivity and thus can be used to calculate protein synthesis rates in skeletal muscle and liver when a flooding dose of phenylalanine is administered.
引用
收藏
页码:E103 / E109
页数:7
相关论文
共 37 条
[1]   RESPECTIVE INFLUENCES OF AGE AND WEANING ON SKELETAL AND VISCERAL MUSCLE PROTEIN-SYNTHESIS IN THE LAMB [J].
ATTAIX, D ;
AUROUSSEAU, E ;
BAYLE, G ;
ROSOLOWSKAHUSZCZ, D ;
ARNAL, M .
BIOCHEMICAL JOURNAL, 1988, 256 (03) :791-795
[2]  
BAILLIE AGS, 1991, AM J PHYSIOL, V262, pE1
[3]   SOURCE OF AMINO-ACIDS FOR TRANSFER-RNA ACYLATION - IMPLICATIONS FOR MEASUREMENT OF PROTEIN-SYNTHESIS [J].
BARNES, DM ;
CALVERT, CC ;
KLASING, KC .
BIOCHEMICAL JOURNAL, 1992, 283 :583-589
[4]   SOURCE OF AMINO-ACIDS FOR TRANSFER-RNA ACYLATION IN GROWING CHICKS [J].
BARNES, DM ;
CALVERT, CC ;
KLASING, KC .
AMINO ACIDS, 1994, 7 (03) :267-278
[5]   PRECURSOR POOLS OF PROTEIN-SYNTHESIS - A STABLE-ISOTOPE STUDY IN A SWINE MODEL [J].
BAUMANN, PQ ;
STIREWALT, WS ;
OROURKE, BD ;
HOWARD, D ;
NAIR, KS .
AMERICAN JOURNAL OF PHYSIOLOGY, 1994, 267 (02) :E203-E209
[6]   Spectrophometric assay for measuring branched-chain amino acid concentrations: Application for measuring the sensitivity of protein metabolism to insulin [J].
Beckett, PR ;
Hardin, DS ;
Davis, TA ;
Nguyen, HV ;
WrayCahen, D ;
Copeland, KC .
ANALYTICAL BIOCHEMISTRY, 1996, 240 (01) :48-53
[7]   PHYSIOLOGICAL HYPERINSULINEMIA STIMULATES PROTEIN-SYNTHESIS AND ENHANCES TRANSPORT OF SELECTED AMINO-ACIDS IN HUMAN SKELETAL-MUSCLE [J].
BIOLO, G ;
FLEMING, RYD ;
WOLFE, RR .
JOURNAL OF CLINICAL INVESTIGATION, 1995, 95 (02) :811-819
[8]  
Boirie Y, 1997, AM J CLIN NUTR, V65, P489
[9]   PROTEIN-SYNTHESIS VERSUS ENERGY-STATE IN CONTRACTING MUSCLES OF PERFUSED RAT HINDLIMB [J].
BYLUNDFELLENIUS, AC ;
OJAMAA, KM ;
FLAIM, KE ;
LI, JB ;
WASSNER, SJ ;
JEFFERSON, LS .
AMERICAN JOURNAL OF PHYSIOLOGY, 1984, 246 (04) :E297-E305
[10]   Protein synthesis in skeletal muscle and jejunum is more responsive to feeding in 7- than in 26-day-old pigs [J].
Davis, TA ;
Burrin, DG ;
Fiorotto, ML ;
Nguyen, HV .
AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM, 1996, 270 (05) :E802-E809