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Comparison between 3-methylhistidine production and proteinase activity as measures of skeletal muscle breakdown in protein-deficient growing barrows. | LitMetric

AI Article Synopsis

  • The experiment aimed to investigate how 3-methylhistidine (3MH) production relates to proteinase activity in the skeletal muscles of growing barrows.
  • Barrows were assigned to three different dietary groups: a control diet ad libitum, a restricted control diet, and a protein-free diet over a 14-day period, with blood samples collected to measure 3MH levels, indicating muscle protein breakdown.
  • The results showed that while the protein-free diet led to a higher fractional breakdown rate of muscle protein compared to the control group, no significant differences in proteinase activities were found, suggesting no direct link between muscle protein degradation and proteinase activity during a protein-free diet.

Article Abstract

This experiment was conducted to determine the relationship between 3-methylhistidine (3MH) production and proteinase activity in skeletal muscles of growing barrows. Barrows at 13 wk of age were randomly assigned to either control diet available on an ad libitum basis (21% of ME consisted of protein; control group), control diet fed restricted (pair-fed with barrows in protein-free group; intake-restricted group), or protein-free diet available on an ad libitum basis (protein-free group) for 14 d. During the last 3 d, blood samples were collected for determination 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 calpastatin, mu-calpain, m-calpain, multicatalytic proteinase (MCP), cathepsin B, cathepsins B+L, and cystatins activities. Both muscles were also analyzed for amounts of DNA, RNA, total protein, and myofibrillar and sarcoplasmic proteins. Growth rate (kilograms/day) was influenced by dietary treatments (P < .05). Fractional breakdown rate (FBR, percentage/day) of skeletal muscle, as calculated from 3MH production rate (micromoles.kilogram-1.day-1), was 27% higher for the protein-free group than for the control group. However, no differences in proteinase 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 myofibrillar protein degradation rate and proteinase activities in skeletal muscle during a protein-free feeding strategy.

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Source
http://dx.doi.org/10.2527/1995.7382272xDOI Listing

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