Histochemical properties and collagen architecture of M. iliotibialis lateralis and M. puboischiofemoralis in male broilers with different growth rates induced by feeding at different planes of nutrition

B. C. Roy, I. Oshima, H. Miyachi, N. Shiba, S. Nishimura, S. Tabata, H. Iwamoto

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Abstract

1. The histochemical properties and the collagen content and architecture of the iliotibialis lateralis (ITL) and puboischiofemoralis (PIF) muscles were assessed in Red Cornish New Hampshire cockerels reared on a high nutrient plane for 80 d (H80d), or a low nutrient plane for 80 d (L80d) or 95 d (L95d). 2. Final live weights were 3410 g in H80d, 2810 g in L80d and 3467 g in L95d. Both ITL and PIF muscle weights were lowest in L80d and did not differ between H80d and L95d. 3. ITL muscle was composed of fast-twitch myofibres such as IIA (high reduced nicotinamide adenine dinucleotide dehydrogenase, NADH-DH activity), IIB (low NADH-DH activity) and IIC (intermediate NADH-DH activity). The high percentage of type IIB myofibres in H80d (766%) and L95d (762%) birds were reflected in low percentages of type IIC myofibres (122%) in H80d birds and type IIA myofibres (82%) in L95d birds. Percentages of IIA, IIB and IIC myofibres in L80d cockerels were 124, 698 and 176%, respectively. 4. The myofibres in PIF muscle were divided into two basic types, I and IIA, and a transitional form (I-tr) from IIA to I. In the caudal region, all myofibres in H80d and L95d cockerels were type I but in L80d cockerels 15% of myofibres were categorised as type I-tr. In the cranial region, the great majority (52 to 63%) of myofibres were type IIA. Type I myofibres occurred at a higher percentage in H80d (305%) than L95d (218%) and type I-tr in L95d (157%) than H80d (73%) and L80d (115%). 5. The total amount of collagen was higher in ITL than PIF muscle in every bird group. In both muscles the highest collagen content was in L95d cockerels but the content did not differ between H80d and L80d birds. The thickness of thick and thin perimysia increased with muscle size. The circular collagen fibre in the thick perimysium was larger in ITL (61 to 70 m) than PIF (37 to 38 m) muscle but did not differ among the bird groups. 6. From these results, it was concluded that feeding on a high nutritional plane promotes growth of the thigh muscles, with accompanying enlargement of the perimysial thickness, no increase in collagen content and various changes of histochemical properties.

Original languageEnglish
Pages (from-to)312-322
Number of pages11
JournalBritish Poultry Science
Volume48
Issue number3
DOIs
Publication statusPublished - Jun 1 2007

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feeding level
collagen
Collagen
broiler chickens
cockerels
Muscles
muscles
Birds
Growth
NAD (coenzyme)
birds
NAD
Cornish (chicken breed)
NADH Dehydrogenase
Weights and Measures
Food
NADH dehydrogenase
nutrients
thighs
Thigh

All Science Journal Classification (ASJC) codes

  • Food Science
  • Animal Science and Zoology

Cite this

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title = "Histochemical properties and collagen architecture of M. iliotibialis lateralis and M. puboischiofemoralis in male broilers with different growth rates induced by feeding at different planes of nutrition",
abstract = "1. The histochemical properties and the collagen content and architecture of the iliotibialis lateralis (ITL) and puboischiofemoralis (PIF) muscles were assessed in Red Cornish New Hampshire cockerels reared on a high nutrient plane for 80 d (H80d), or a low nutrient plane for 80 d (L80d) or 95 d (L95d). 2. Final live weights were 3410 g in H80d, 2810 g in L80d and 3467 g in L95d. Both ITL and PIF muscle weights were lowest in L80d and did not differ between H80d and L95d. 3. ITL muscle was composed of fast-twitch myofibres such as IIA (high reduced nicotinamide adenine dinucleotide dehydrogenase, NADH-DH activity), IIB (low NADH-DH activity) and IIC (intermediate NADH-DH activity). The high percentage of type IIB myofibres in H80d (766{\%}) and L95d (762{\%}) birds were reflected in low percentages of type IIC myofibres (122{\%}) in H80d birds and type IIA myofibres (82{\%}) in L95d birds. Percentages of IIA, IIB and IIC myofibres in L80d cockerels were 124, 698 and 176{\%}, respectively. 4. The myofibres in PIF muscle were divided into two basic types, I and IIA, and a transitional form (I-tr) from IIA to I. In the caudal region, all myofibres in H80d and L95d cockerels were type I but in L80d cockerels 15{\%} of myofibres were categorised as type I-tr. In the cranial region, the great majority (52 to 63{\%}) of myofibres were type IIA. Type I myofibres occurred at a higher percentage in H80d (305{\%}) than L95d (218{\%}) and type I-tr in L95d (157{\%}) than H80d (73{\%}) and L80d (115{\%}). 5. The total amount of collagen was higher in ITL than PIF muscle in every bird group. In both muscles the highest collagen content was in L95d cockerels but the content did not differ between H80d and L80d birds. The thickness of thick and thin perimysia increased with muscle size. The circular collagen fibre in the thick perimysium was larger in ITL (61 to 70 m) than PIF (37 to 38 m) muscle but did not differ among the bird groups. 6. From these results, it was concluded that feeding on a high nutritional plane promotes growth of the thigh muscles, with accompanying enlargement of the perimysial thickness, no increase in collagen content and various changes of histochemical properties.",
author = "Roy, {B. C.} and I. Oshima and H. Miyachi and N. Shiba and S. Nishimura and S. Tabata and H. Iwamoto",
year = "2007",
month = "6",
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language = "English",
volume = "48",
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TY - JOUR

T1 - Histochemical properties and collagen architecture of M. iliotibialis lateralis and M. puboischiofemoralis in male broilers with different growth rates induced by feeding at different planes of nutrition

AU - Roy, B. C.

AU - Oshima, I.

AU - Miyachi, H.

AU - Shiba, N.

AU - Nishimura, S.

AU - Tabata, S.

AU - Iwamoto, H.

PY - 2007/6/1

Y1 - 2007/6/1

N2 - 1. The histochemical properties and the collagen content and architecture of the iliotibialis lateralis (ITL) and puboischiofemoralis (PIF) muscles were assessed in Red Cornish New Hampshire cockerels reared on a high nutrient plane for 80 d (H80d), or a low nutrient plane for 80 d (L80d) or 95 d (L95d). 2. Final live weights were 3410 g in H80d, 2810 g in L80d and 3467 g in L95d. Both ITL and PIF muscle weights were lowest in L80d and did not differ between H80d and L95d. 3. ITL muscle was composed of fast-twitch myofibres such as IIA (high reduced nicotinamide adenine dinucleotide dehydrogenase, NADH-DH activity), IIB (low NADH-DH activity) and IIC (intermediate NADH-DH activity). The high percentage of type IIB myofibres in H80d (766%) and L95d (762%) birds were reflected in low percentages of type IIC myofibres (122%) in H80d birds and type IIA myofibres (82%) in L95d birds. Percentages of IIA, IIB and IIC myofibres in L80d cockerels were 124, 698 and 176%, respectively. 4. The myofibres in PIF muscle were divided into two basic types, I and IIA, and a transitional form (I-tr) from IIA to I. In the caudal region, all myofibres in H80d and L95d cockerels were type I but in L80d cockerels 15% of myofibres were categorised as type I-tr. In the cranial region, the great majority (52 to 63%) of myofibres were type IIA. Type I myofibres occurred at a higher percentage in H80d (305%) than L95d (218%) and type I-tr in L95d (157%) than H80d (73%) and L80d (115%). 5. The total amount of collagen was higher in ITL than PIF muscle in every bird group. In both muscles the highest collagen content was in L95d cockerels but the content did not differ between H80d and L80d birds. The thickness of thick and thin perimysia increased with muscle size. The circular collagen fibre in the thick perimysium was larger in ITL (61 to 70 m) than PIF (37 to 38 m) muscle but did not differ among the bird groups. 6. From these results, it was concluded that feeding on a high nutritional plane promotes growth of the thigh muscles, with accompanying enlargement of the perimysial thickness, no increase in collagen content and various changes of histochemical properties.

AB - 1. The histochemical properties and the collagen content and architecture of the iliotibialis lateralis (ITL) and puboischiofemoralis (PIF) muscles were assessed in Red Cornish New Hampshire cockerels reared on a high nutrient plane for 80 d (H80d), or a low nutrient plane for 80 d (L80d) or 95 d (L95d). 2. Final live weights were 3410 g in H80d, 2810 g in L80d and 3467 g in L95d. Both ITL and PIF muscle weights were lowest in L80d and did not differ between H80d and L95d. 3. ITL muscle was composed of fast-twitch myofibres such as IIA (high reduced nicotinamide adenine dinucleotide dehydrogenase, NADH-DH activity), IIB (low NADH-DH activity) and IIC (intermediate NADH-DH activity). The high percentage of type IIB myofibres in H80d (766%) and L95d (762%) birds were reflected in low percentages of type IIC myofibres (122%) in H80d birds and type IIA myofibres (82%) in L95d birds. Percentages of IIA, IIB and IIC myofibres in L80d cockerels were 124, 698 and 176%, respectively. 4. The myofibres in PIF muscle were divided into two basic types, I and IIA, and a transitional form (I-tr) from IIA to I. In the caudal region, all myofibres in H80d and L95d cockerels were type I but in L80d cockerels 15% of myofibres were categorised as type I-tr. In the cranial region, the great majority (52 to 63%) of myofibres were type IIA. Type I myofibres occurred at a higher percentage in H80d (305%) than L95d (218%) and type I-tr in L95d (157%) than H80d (73%) and L80d (115%). 5. The total amount of collagen was higher in ITL than PIF muscle in every bird group. In both muscles the highest collagen content was in L95d cockerels but the content did not differ between H80d and L80d birds. The thickness of thick and thin perimysia increased with muscle size. The circular collagen fibre in the thick perimysium was larger in ITL (61 to 70 m) than PIF (37 to 38 m) muscle but did not differ among the bird groups. 6. From these results, it was concluded that feeding on a high nutritional plane promotes growth of the thigh muscles, with accompanying enlargement of the perimysial thickness, no increase in collagen content and various changes of histochemical properties.

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