Effect of Dietary Thyroxine on Muscle Protein Metabolism and Abdominal Fat Content in Broiler Chicken in Hot and Moderate Environments

Hayashi, Kunioki; Kukita, Shunichi; Mukai, Michiko; Toyomizu, Masaaki; Tomita, Y.

doi:10.2508/chikusan.61.1107

Cited by 2 publications

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“…The rates of skeletal muscle protein turnover are influenced by environmental temperatures (Hayashi et al 1990(Hayashi et al , 1993Yunianto et al 1997). Both protein synthesis and degradation are energetically expensive and thus environmental temperature intensely influences the growth of animals (Harris et al 1987).…”

Section: Resultsmentioning

confidence: 99%

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Myofibrillar proteolysis in chick muscle cell cultures during heat stress

Nakashima

Nonaka

Shimizu

et al. 2004

Animal Science Journal

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The effect of heat stress on protein oxidation and myofibrillar proteolysis in chick myotubes was investigated. Myotubes were incubated at 37 or 41°C for 6 and 24 h. Protein carbonyl content, as an index of protein oxidation, increased more at 41°C than at 37°C for 6 and 24 h incubations. Nτ‐methylhistidine release as an index of myofibrillar proteolysis also increased more at 41°C than at 37°C for 6 and 24 h incubations. Proteasome activity also increased more under those same conditions. Calpain and cathepsin D but not B + L activities showed a greater increase at 41°C than at 37°C for 24 but not the 6 h incubation. These results indicate that heat stress increases protein oxidation and proteasome activity, resulting in an increase in myofibrillar proteolysis for short‐term incubation and, for long‐term incubation, it increases calpain, proteasome and cathepsin D activities, finally accelerating myofibrillar proteolysis in chick myotubes.

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