title: Effects of nutritional level on muscle development, histochemical properties of myofibre and collagen architecture in the pectoralis muscle of male broilers.
abstract: 1. The effects of nutritional level on muscle development, histochemical properties of myofibre and collagen architecture in the pectoralis muscle were evaluated using male broilers of Red Cornish x New Hampshire stock, reared on diets of high nutritional value for up to 80 d (H80d) and low nutritional value for up to 80 d (L80d, same age as H80d) or 95 d (L95d, same body weight as H80d). 2. The total live weight and the weight of pectoralis muscle were lower in L80d than in both H80d and L95d. The muscle weight as a percentage of live weight was 8.7% in L80d, 10.7% in H80d and 11.5% in L95d. 3. Pectoralis muscle was composed only of type IIB myofibres and showed no differences in myofibre type composition among the chicken groups. The largest diameter of type IIB myofibres was observed in L95d, followed by H80d and the smallest in L80d. 4. The total amount of intramuscular collagen did not differ among the chicken groups (1.92 to 1.99 mg/g). Types I and III collagens were immunohistochemically detected in both the perimysia and endomysia. The thin perimysia around the primary myofibre fascicles showed larger width in H80d than L80d and L95d, and also the thick perimysia around the secondary fascicles in H80d than L80d. 5. The collagen structure of the perimysium was most developed in H80d, followed by L95d and on the least in L80d. The development of perimysial collagen fibres could be enhanced by a rapid growth rate of the muscle induced by high nutritional level and depressed by a slow growth rate with low nutritional foods. 6. The endomysial collagen architecture was observed as a felt-like tissue of the fibril bundles with many slits. The thinnest endomysial wall was observed in L80d, followed by H80d and the thickest in L95d. 7. From these results, it was indicated that foods of high nutritional value could enhance growth of the pectoralis muscle of broilers, and this is accompanied by hypertrophy of the type IIB myofibres and development of the perimysial collagen architecture.
authors.affiliation: Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka-shi, Japan.
authors.forename: B C
authors.initials: BC
authors.lastname: Roy
authors.forename: I
authors.initials: I
authors.lastname: Oshima
authors.forename: H
authors.initials: H
authors.lastname: Miyachi
authors.forename: N
authors.initials: N
authors.lastname: Shiba
authors.forename: S
authors.initials: S
authors.lastname: Nishimura
authors.forename: S
authors.initials: S
authors.lastname: Tabata
authors.forename: H
authors.initials: H
authors.lastname: Iwamoto
mesh_terms: D000821:Animal Feed; D000824:Animal Nutritional Physiological Phenomena; D000818:Animals; D002645:Chickens / Q000254:growth & development / Q000378:metabolism*; D003094:Collagen / Q000378:metabolism*; D004032:Diet / Q000662:veterinary; D008297:Male; D018485:Muscle Fibers, Skeletal / Q000166:cytology* / Q000378:metabolism* / Q000648:ultrastructure; D018482:Muscle, Skeletal / Q000166:cytology / Q000254:growth & development*
chemical_list: D003094:Collagen