Immunohistochemical localization of proteoglycans in bovine skeletal muscle and adipose connective tissues

Nakano, T.; Li, X.; Sunwoo, Hoon H.; Sim, J. S.

doi:10.4141/a96-090

Cited by 8 publications

(5 citation statements)

References 9 publications

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“…The galactosaminoglycan found in the fat pad (Figs 2 and 3) is probably derived from decorin. This will be confirmed immunohistochemically with the anti‐decorin monoclonal antibody used in the previous study (Nakano et al. 1997b).…”

Section: Discussionsupporting

confidence: 66%

Chemical composition of the infrapatellar fat pad of swine

et al. 2004

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The porcine infrapatellar fat pad is a structure composed of adipocytes and adipose connective tissues. Limited information is available concerning its chemical composition. Samples of the fat pad collected from young hogs were dissected into two portions: a relatively hard core of the pad with cushioning properties (inner tissue), and a soft adipose tissue surrounding the core (outer tissue). The inner tissue contained less moisture and nitrogen than did the outer tissue. The yield of dry-delipidated tissue was also lower in the inner tissue, indicating a higher content of lipid in this tissue. Fatty acid analysis showed that the proportions of C18: 1, C16: 1 and C18: 2n-6 are higher, and the proportion of C16: 0 is lower in the inner than in the outer tissue. Collagen is the major protein, with relatively small amounts of glycosaminoglycans in both tissues. The content of hyaluronic acid relative to sulphated galactosaminoglycan was lower in the inner than in the outer tissue. The electrophoresis pattern of sulphated galactosaminoglycan was also different between the two tissues. These results suggest that chemical composition varies between adipose tissues with different biomechanical function.

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Section: Discussionsupporting

confidence: 66%

Chemical composition of the infrapatellar fat pad of swine

et al. 2004

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“…Proteoglycans bind to collagen in specific locations [39][40][41] and are present in different ratios throughout ECM. Decorin, the major PG in the perimysium, 42 is arch-shaped, 43,44 and its leucine-rich repeats bind to type I collagen 45 near the d and e bands. 40 Due to its binding interaction with type I collagen in vitro, decorin has been proposed to be a regulator of type I collagen fibrillogenesis in skeletal muscle.…”

Section: Skeletal Muscle Ecm Structurementioning

confidence: 99%

Structure and function of the skeletal muscle extracellular matrix

Gillies¹,

Lieber²

2011

Muscle and Nerve

773

686

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The skeletal muscle extracellular matrix (ECM) plays an important role in muscle fiber force transmission, maintenance, and repair. In both injured and diseased states, ECM adapts dramatically, a property thathas clinical manifestations and alters muscle function. Here, we review the structure, composition, and mechanical properties of skeletal muscle ECM, describe the cells that contribute to the maintenance of the ECM and, finally, overview changes that occur with pathology. New scanning electron micrographs of ECM structure are also presented with hypotheses about ECM structure-function relationships. Detailed structure-function relationships of the ECM have yet to be defined and, as a result, we propose areas for future studies.

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“…Decorin is identified in IMCT (Eggen et al. 1994; Nakano et al. 1997), and plays an important role in morphogenesis of IMCT during bovine fetal development (Nishimura et al.…”

Section: Structure and Composition Of Imctmentioning

confidence: 99%

“…Decorin, a small leucine-rich PG (SLRP), regulates collagen fibrillogenesis (Danielson et al 1997) and plays an important role in the stabilization of collagen fibrils (Scott & Thomlinson 1998). Decorin is identified in IMCT (Eggen et al 1994;Nakano et al 1997), and plays an important role in morphogenesis of IMCT during bovine fetal development (Nishimura et al 2002). Decorin also plays important roles in the quiescence of muscle cells (Nishimura et al 2008a) and muscle cell growth by modulating growth factors (Miura et al 2006;Zhu et al 2007;Kishioka et al 2008).…”

Section: Structure and Composition Of Imctmentioning

confidence: 99%

The role of intramuscular connective tissue in meat texture

Nishimura¹

2010

Animal Science Journal

177

103

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The structure, composition and amount of intramuscular connective tissue (IMCT) vary tremendously between muscles, species and breeds, and certainly contribute to meat texture. With animal growth, collagen crosslinks become more stable, and the structural integrity of IMCT increases. These changes increase the mechanical properties of IMCT, contributing to the toughening of meat. Intramuscular fat deposits, mainly in the perimysium between muscle fiber bundles, result in marbling. This causes the remodeling of IMCT structures and reduces the mechanical strength of IMCT, contributing to the tenderization of beef. The IMCT has been thought to be rather immutable compared to myofibrils during postmortem ageing of meat. However, recent studies have shown the disintegration of IMCT during postmortem ageing of meat and its relationship to tenderization of raw meat, although its contribution to cooked meat is still controversial. Given the large influence of IMCT on meat texture, further elucidations of molecular mechanisms which change the structural integrity of IMCT during chronological ageing of animals and postmortem ageing of meat are needed.

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Immunohistochemical localization of proteoglycans in bovine skeletal muscle and adipose connective tissues

Cited by 8 publications

References 9 publications

Chemical composition of the infrapatellar fat pad of swine

Chemical composition of the infrapatellar fat pad of swine

Structure and function of the skeletal muscle extracellular matrix

The role of intramuscular connective tissue in meat texture

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