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Dive into the research topics where Hisao Iwamoto is active.

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Featured researches published by Hisao Iwamoto.


Meat Science | 2003

Relationship among collagen amount, distribution and architecture in the M. longissimus thoracis and M. pectoralis profundus from pigs.

Yoshi-Nori Nakamura; Hisao Iwamoto; Yoshitaka Ono; Nobuya Shiba; Shotaro Nishimura; Shoji Tabata

The relative distribution of types I and III collagens and collagen fibre architecture in the perimysium and endomysium were compared to the longissimus thoracis (LT) and pectoralis profundus (PP) muscles in pigs. The LT muscle was composed of type I myofibres 16.8%, IIA 12.9% and IIB 70.2%, and the PP muscle was 25.4, 23.1 and 51.5%, respectively. The total collagen amount differed significantly between the LT (2.66 mg/g) and PP (4.13 mg/g) muscle (P<0.001). On image analysis of the immunohistochemical preparations for types I and III collagens, the percentage area of the perimysium to the total collagen area showed significant differences between the muscles, where perimysial type I collagen occupied 25.4% of the total area in the LT muscle and 45.7% in the PP and perimysial type III 37.6 and 54.5%, respectively (P<0.001). In scanning electron microscopic photographs of the macerated preparation, very thick collagen layers composed of several fibre bands were observed in the perimysia of the PP muscle and appeared differently from the thinner perimysia with a few bands in the LT. Similar architecture of endomysial collagen fibres were observed around every myofibre type in the PP muscle and also in the LT. The fine surface cover of reticular collagen fibres around an adipocyte was shown as a global cast. These results suggested that the total collagen amount of the PP muscle was related mainly to the well developed perimysia composed of several collagen bands, indicating tougher meat compared with the LT muscle.


British Poultry Science | 2006

Effects of nutritional level on muscle development, histochemical properties of myofibre and collagen architecture in the pectoralis muscle of male broilers

Bimol Chandra Roy; Ichiro Oshima; Hideyuki Miyachi; Nobuya Shiba; Shotaro Nishimura; Shoji Tabata; Hisao Iwamoto

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 × 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.


British Poultry Science | 1993

Different growth rates of male chicken skeletal muscles related to their histochemical properties

Hisao Iwamoto; Y. Hara; Takafumi Gotoh; Yoshitaka Ono; Hitoshi Takahara

1. Early, M. pubo-ischio-femoralis pars medialis (PIF muscle) and late, M. iliotibialis lateralis pars postacetabularis (ITL muscle), maturing muscles were studied. These two muscles contained different populations of histochemical fibre types. 2. The profile measurements of the muscles showed diphasic allometric growth relative to the weights. In the early stage of growth (up to 15 weeks after hatching), the muscle length, width and depth all increased, while in the later stage (from 15 to 35 weeks) muscle growth resulted mainly from the marked increase in the depth and to a lesser degree, from an increase in the width. 3. Type I fibres, observed predominantly in PIF muscle matured earlier than the Type II fibres of ITL muscle. 4. From these results, the detailed process of skeletal muscle growth in the chicken was discussed.


British Poultry Science | 1992

Breed differences in the histochemical properties of the M. Iliotibialis lateralis myofibre of domestic cocks

Hisao Iwamoto; Y. Hara; Yoshitaka Ono; Hitoshi Takahara

1. Reduced nicotinamide adenine dinucleotide dehydrogenase (NADH-DH) activity in the M. iliotibialis lateralis was compared histochemically among 7 breeds of cocks. This muscle was composed only of Type-IIA and -IIB fibres. 2. Apparent breed differences were observed in muscle development, the NADH-DH activity in every fibre type, fibre type distribution and fibre diameters. 3. From the results of this study, it was concluded that the muscle characteristics of various breeds were based not only on the fibre type composition, but also the different activities of oxidative enzyme in every type.


British Poultry Science | 2004

Developmental states of the collagen content, distribution and architecture in the pectoralis, iliotibialis lateralis and puboischiofemoralis muscles of male Red Cornish x New Hampshire and normal broilers.

Yoshi-Nori Nakamura; Hisao Iwamoto; N. Shiba; Hideyuki Miyachi; Shoji Tabata; Shotaro Nishimura

1. Developmental states of the collagen content, distribution and architecture in the pectoralis (PT), iliotibialis lateralis (ITL) and puboischiofemoralis (PIF) muscles of male Red Cornish × New Hampshire (RN, 80 d, body weight 2·9 kg) and normal (3·1 kg) broilers were evaluated. 2. In PT muscle the total amount of collagen was significantly greater in RN broilers (3·33 mg/g) than in normal ones (1·71 mg/g). This higher collagen content in RN broilers was based mainly on the closer mesh sizes of endomysial honeycomb. The collagen structures in the perimysia also differed between broiler types, when more collagen fibres were observed in RN broilers. 3. ITL muscle contained total collagen of 4·10 to 5·00 mg/g. Types I and III collagens were distributed on the perimysia at higher percentages in RN broilers (31·6%, 37·2%) than normal (15·6%, 30·8%), respectively. The thick bands of tough collagen fibres characteristic of ITL muscle perimysium in cockerels had not yet developed in these broilers. 4. Total collagen was 4·63 to 6·29 mg/g in PIF material with fascia. In PIF muscle the perimysial collagen fibres had not yet attained their full growth but consisted of densely packed fibrils. PIF muscle was characterised by the earlier maturing collagen structure. 5. These results show that a perimysial collagen structure in broilers is still in an undeveloped state. It is supposed that tenderness of broiler meat is attributed mainly to characteristics of the collagen distribution, in which the majority of types I and III collagens is distributed on the closer mesh of endomysial honeycomb.


British Poultry Science | 2000

Myofibre composition and total collagen content in M. iliotibialis lateralis and M. pectoralis of Silkie and White Leghorn chickens.

K. Sakakibara; Shoji Tabata; Nobuya Shiba; Takafumi Gotoh; Shotaro Nishimura; Hisao Iwamoto

1. Using adult Silkie and White Leghorn (WL) chickens, fibre composition and total collagen content were compared between M. iliotibialis lateralis (ITL) and M. pectoralis (PT). 2. Fibres were divided into type IIR and IIW showing strong and weak reduced nicotinamide adenine dinucleotide dehydrogenase activities, respectively. 3. Fibre composition differed markedly between ITL and PT muscle. ITL muscle was composed of both types IIR and IIW fibre but PT muscle of only type IIW. Breed difference on composition was noted only in ITL muscle of cocks (type IIR; Silkie 53.8% and WL 37.0%). 4. Total collagen content was greater in ITL muscles and in cocks in both muscles. However, a breed difference was observed only in the PT muscle of hens. 5. In conclusion, the total collagen content was affected by muscle location within the body and by sex rather than by fibre composition.


British Poultry Science | 1993

Breed differences in the histochemical properties of the M. pubo‐ischi‐ofemoralis pars medialis myofibre of domestic cocks

Hisao Iwamoto; Y. Hara; Yoshitaka Ono; Hitoshi Takahara

1. Histochemical properties of M. pubo-ischio-femoralis pars medialis (PIF muscle) were compared in 7 breeds of cocks. This muscle was largely composed of Type I fibres and their transitional form (Type I tr). Type IIA fibres were observed in the cranial part. 2. The weight and cross-sectional area of the PIF muscle increased with increasing body weight. However, the relative muscle development to body weight differed among the 7 breeds. 3. A quarter of Type I fibres were of the transitional variety in bantam fowls. Conversely, few, if any, Type I tr fibres were observed in the large breeds where the muscle was poorly developed. 4. As the histochemical properties of Type I fibres made an effective response to the different body weights and the relative PIF muscle development among breeds, it was concluded that PIF muscle performed an important function in supporting the body weight and maintaining posture.


British Poultry Science | 2004

Growth changes of the collagen content and architecture in the pectoralis and iliotibialis lateralis muscles of cockerels

Yoshi-Nori Nakamura; Hisao Iwamoto; N. Shiba; Hideyuki Miyachi; Shoji Tabata; Shotaro Nishimura

1. Growth changes of the collagen content and architecture in the pectoralis (PT) and iliotibialis lateralis (ITL) muscles were examined using cockerels from 1 to 14 weeks of age. 2. Total collagen content in PT muscle showed little change, but in ITL muscle reached a maximum at 5 weeks and thereafter decreased slightly until 14 weeks. The collagen content was markedly larger in ITL muscle after 5 weeks. Pyridinoline content of collagen increased abruptly from 5 to 14 weeks in both muscles, but no difference between muscle types was detected. 3. The cell size of the endomysial honeycombs increased with the development of myofibres, and the mesh size of the perimysium around the honeycombs enlarged. 4. In both muscles endomysia were an incomplete network of collagen fibrils with many foramina at one week, became a very thin membrane of felt-like fabric in 2 to 5 weeks and thereafter increased in thickness until 11 to 14 weeks. 5. Perimysial width around the secondary fasciculus differed between the muscle types after 5 weeks. In the wider perimysium of ITL muscle, the collagen fibres increased in number and size to make a stack of collagen bands around the fasciculus. In the narrower perimysium of PT muscle, a few platelets of collagen fibres also developed. 6. The perimysial collagen fibre at 1 to 2 weeks had a smooth surface and appeared to be composed of fine collagen fibrils. The fibre at 11 to 14 weeks showed a rugged surface and was composed of coarser collagen bundles that combined with each other into a net-like configuration with very slim meshes. 7. Our results showed that the collagenous components of chicken intramuscular connective tissue changed markedly during the early period of muscle growth in distribution, architecture and quality but with little difference in quantity.


Animal Reproduction Science | 2000

Testis developments and puberty in the male Tokara (Japanese native) goat

Shotaro Nishimura; Kaoru Okano; K Yasukouchi; Takafumi Gotoh; Shoji Tabata; Hisao Iwamoto

In male Tokara (Japanese native) goats, testis development and the onset of puberty were studied histologically and observing sexual behaviour. Testes weight increased from 36+/-5.4 (S.E.) g (n=5) at 3 months of age to 126+/-6.3 g (n=6) at 12 months. The degree of the testis development differed among kids at 3 months of age and only one of four had produced spermatozoa in the testis. Large number of spermatozoa were always present in seminiferous tubules and epididymal ducts from 4 months of age. The diameter of seminiferous tubules increased from 133+/-9.9 microm (n=4) at 3 months to 198+/-1.0 microm (n=3) at 6 months with little increase thereafter. Mounting and pelvic thrusts onto a teaser doe started at from 9 to 14 weeks of age. Ejaculated semen contained sperm with good motility for the first time from 17 weeks. The male Tokara goat reaches puberty at around 4 months of age but testis development continues to 12 months.


British Poultry Science | 2001

Scanning electron microscopic observation of the architecture of collagen fibres in chicken M. iliotibialis lateralis

Hisao Iwamoto; Shoji Tabata; K. Sakakibara; Shotaro Nishimura; Takafumi Gotoh; Y. Koga

Abstract 1. The collagen architecture of M. iliotibialis lateralis in chicken was observed under the scanning electron microscope after muscle maceration in NaOH. 2. Immunohistochemical methods showed Type I and III collagens to be distributed over both perimysium and endomysium. 3. Thick perimysium around secondary myofibre fasciculi was composed of many large longitudinal collagen bundles and a few small circumferential bundles. In contrast, thin perimysium around primary myofibre fasciculi showed mainly circumferential bundles. 4. Endomysium had a honeycomb-like structure and consisted of a fine collagen mesh, its main fibre striation being circumferential. 5. It is suggested that functional demand differs between thick perimysium and thin endomysium.

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