Effect of age, muscle type, and insulin-like growth factor-II genotype on muscle proteolytic and lipolytic enzyme activities in boars.
Recently, a paternally expressed quantitative trait nucleotide (QTN) in the regulatory sequence of the IGF-II gene with effects on muscle growth and fat deposition was discovered in the pig. This QTN is also known as the IGF-II intron3 G3072A mutation. The aim of the current study was to determine the effects of age, muscle type, and IGF-II genotype (Apat, mutant allele vs. Gpat, wild-type allele) on muscle proteolytic and lipolytic enzyme activities. At approximately 4, 8, 16, and 26 wk of age, boars (n = 6 to 15 per genotype x age group) were slaughtered and mu- and m-calpain (CALP), calpastatin (CAST), cathepsins (CATH) B+L and H, acid lipase, and phospholipase activities were measured in Longissimus thoracis et lumborum, Semimembranosus, and Triceps brachii muscle samples taken soon after slaughter. Activities of CATH B+L and H, mu- and m-CALP, and acid lipase were not affected by the IGF-II genotype. Activity of CAST was greater (P < 0.005) and m-CALP:CAST was less (P < 0.05) in Apat animals. Because CAST activity and m-CALP:CAST are known to be related to protein degradation, satellite cell fusion, or both, it is likely that differences in proteolytic enzyme activities are involved in the greater percentage of muscle mass in Apat animals. Age and muscle type influenced proteolytic and lipolytic enzyme activities (P < 0.05), except for mu- and m-CALP (no effect of muscle) and acid lipase (no effect of age). The same pattern in mu-CALP, CAST, and m-CALP:CAST with age was found during growth for the 3 muscles, although clear differences (P < 0.05) between muscles existed. In general, and in agreement with previous reports, greater enzyme activities were found in the more oxidative Triceps brachii muscle compared with the other 2 muscles. A remarkable increase (P < 0.05) from 16 to 26 wk of age in mu-CALP, CAST, mu-CALP:CAST, and CATH H and a large decrease (P < 0.05) in acid phospholipase and m-CALP:CAST was found. For m-CALP and CATH B+L, a gradual decrease (P < 0.05) was found with age. Although age effects on enzyme activities could only partly be interpreted biologically in relation to the muscle growth rate, this study showed that proteolytic and lipolytic enzyme activities change during growth.
Van den Maagdenberg
K
K
Laboratory for Animal Nutrition and Animal Product Quality, Department of Animal Production, Ghent University, Proefhoevestraat 10, 9090 Melle, Belgium.
Claeys
E
E
Stinckens
A
A
Buys
N
N
De Smet
S
S
D000375:Aging / Q000502:physiology*; D000818:Animals; D005786:Gene Expression Regulation; D005838:Genotype; D007335:Insulin-Like Growth Factor II / Q000235:genetics* / Q000378:metabolism; D008049:Lipase / Q000378:metabolism*; D008297:Male; D018482:Muscle, Skeletal / Q000378:metabolism*; D009154:Mutation; D010447:Peptide Hydrolases / Q000378:metabolism*; D010740:Phospholipases / Q000378:metabolism*; D013552:Swine
D007335:Insulin-Like Growth Factor II; D010740:Phospholipases; D008049:Lipase; D010447:Peptide Hydrolases