Hna. Vandenhemelgrooten et al., COMPARISON BETWEEN 3-METHYLHISTIDINE PRODUCTION AND PROTEINASE ACTIVITY AS MEASURES OF SKELETAL-MUSCLE BREAKDOWN IN PROTEIN-DEFICIENT GROWING BARROWS, Journal of animal science, 73(8), 1995, pp. 2272-2281
This experiment was conducted to determine the relationship between S-
methylhistidine (3MH) production and proteinase activity in skeletal m
uscles of growing barrows, Barrows at 13 wk of age were randomly assig
ned to either control diet available on an ad libitum basis (21% of ME
consisted of protein; control group), control diet fed restricted (pa
ir-fed with barrows in protein-free group; intake-restricted group), o
r protein-free diet available on an ad libitum basis (protein-free gro
up) for 14 d. During the last 3 d, blood samples were collected for de
termination of 3MH production rate, which is a measure of myofibrillar
protein breakdown. At slaughter, two muscles were taken: masseter (M)
and longissimus (L) muscles. The muscle samples were analyzed for cal
pastatin, p-calpain, m-calpain, multicatalytic proteinase (MCP), cathe
psin B, cathepsins B+L, and cystatins activities. Both muscles were al
so analyzed for amounts of DNA, RNA, total protein, and myofibrillar a
nd sarcoplasmic proteins. Growth rate (kilograms/day) was influenced b
y dietary treatments (P < .05). Fractional breakdown rate (FBR, percen
tage/day) of skeletal muscle, as calculated from 3MH production rate (
micromoles . kilogram(-1). day(-1)), was 27% higher for the protein-fr
ee group than for the control group. However, no differences in protei
nase activities were observed, except for lower MCP activity in the M
muscle of the protein-free group than in that of the other groups (P <
.05). In the present study, no direct relation was observed between m
yofibrillar protein degradation rate and proteinase activities in skel
etal muscle during a protein-free feeding strategy.