Age related changes in the reducible cross‐links of collagen

Bailey, Allen J.; Shimokomaki, Massami

doi:10.1016/0014-5793(71)80338-1

Cited by 156 publications

(63 citation statements)

References 7 publications

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“…The SEL group was significantly (P < 0.01) more tender than any of the other groups studied when comparing WBS values. It has been well documented that heat liable collagen content decreases with advancing age (Hill, 1966;Herring et al, 1967;Bailey and Shimokomaki, 1971), which would explain the differences noticed between SEL and the other 4 groups. Aberle et al (1981) concluded feeding cattle high-energy diets would promote rapid rates of protein synthesis and produce beef with a high proportion of newly synthesized, heat liable collagen.…”

Section: Warner-bratzler Shear Forcementioning

confidence: 85%

Benchmarking carcass characteristics and muscles from commercially identified beef and dairy cull cow carcasses for Warner-Bratzler shear force and sensory attributes1

Stelzleni

Patten

Johnson

et al. 2007

Journal of Animal Science

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Calkins, Chris R.; and Gwartney, B. L., "Benchmarking carcass characteristics and muscles from commercially identified beef and dairy cull cow carcasses for Warner-Bratzler shear force and sensory attributes" (2006 ABSTRACT: The objective of this study was to benchmark carcasses and muscles from commercially identified fed (animals that were perceived to have been fed an increased plane of nutrition before slaughter) and nonfed cull beef and dairy cows and A-maturity, USDA Select steers, so that the muscles could be identified from cull cow carcasses that may be used to fill a void of intermediately priced beef steaks.

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Section: Warner-bratzler Shear Forcementioning

confidence: 85%

Benchmarking carcass characteristics and muscles from commercially identified beef and dairy cull cow carcasses for Warner-Bratzler shear force and sensory attributes1

Stelzleni

Patten

Johnson

et al. 2007

Journal of Animal Science

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“…The texture sensation of meat is influenced by the presence of several factors including the amount of intramuscular fat, water holding capacity, the state of the actomyosin complex and the quantity and, mostly, the quality of collagen. Earlier works by Bailey and co-workers demonstrated that collagen covalent cross-linking mediated by lysyl oxidase enzyme increased with the ageing of animals (Bailey and Shimokomaki, 1971;Robins et al 1973), and correlated with increased toughness. Indeed, hydroxylysinoketonorleucine (HLKNL), the main form of collagen crosslinking in an immature animal decreases with aging (Shimokomaki et al, 1972) and is replaced by hydroxylysylpyridinium (HP) (Fujimoto et al, 1977;Eyre and Oguchi, 1980).…”

Section: Introductionmentioning

confidence: 93%

Chemical basis for beef charqui meat texture

Youssef

Garcia

Yamashita

et al. 2007

Braz. arch. biol. technol.

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“…This disease has been termed "hydroxylysine-deficient collagen disease" (1). Skin (10). Such age-related changes in the distribution of reducible components of collagen also occur in human connective tissues (10), cartilage presumably included.…”

Section: Bonementioning

confidence: 99%

“…Hydroxylysine is a precursor in the biosynthesis of certain collagen crosslinks (3,4 don, bone, and cartilage collagens (3)(4)(5)(6)(7)(8)(9)(10)(11). Each tissue reveals a unique distribution of these reducible crosslinks that changes as the tissue matures and ages (8,10).…”

mentioning

confidence: 99%

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Reducible Crosslinks in Hydroxylysine-Deficient Collagens of a Heritable Disorder of Connective Tissue

Eyre

Glimcher

1972

Proc. Natl. Acad. Sci. U.S.A.

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Reducible compounds that participate in crosslinking were analyzed in hydroxylysine-deficient collagens of patients with a heritable disorder of connective tissue. After treatment with [3H1sodium borohydride, new compounds, as well as a totally different pattern of tritiated compounds, were found in hydroxylysine-deficient collagen from skin as compared with age-matched controls. The amount of desmosines detected indicated that more elastin was present in abnormal skin than in control skin.Bone collagen, which was not as deficient in hydroxylysine as skin collagen, had the same compounds as normal bone collagen, but their relative proportions were altered, consistent with a deficiency of hydroxylysine, a precursor of the crosslinks. Although the content of hydroxylysine in collagen of cartilage is essentially normal in these patients, analysis after reduction revealed a different pattern of reduced compounds from that of normal cartilage. It is speculated that Type II collagen, the major collagen component in cartilage, contains a normal amount of hydroxylysine, while Type I collagen, which is the major source of the crosslinks, is hydroxylysine-deficient. This distribution would explain the findings of an abnormal profile of reducible compounds despite an almost normal total hydroxylysine content.The finding that the deficiency of hydroxylysine in the collagen of these patients is accompanied by changes in number, chemical nature, and, probably, distribution of crosslinkages, and the previously reported alterations in the solubility characteristics, suggest that at least some skeletal and connective tissue abnormalities are directly related to underlying molecular pathology.

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Age related changes in the reducible cross‐links of collagen

Cited by 156 publications

References 7 publications

Benchmarking carcass characteristics and muscles from commercially identified beef and dairy cull cow carcasses for Warner-Bratzler shear force and sensory attributes1

Benchmarking carcass characteristics and muscles from commercially identified beef and dairy cull cow carcasses for Warner-Bratzler shear force and sensory attributes1

Chemical basis for beef charqui meat texture

Reducible Crosslinks in Hydroxylysine-Deficient Collagens of a Heritable Disorder of Connective Tissue

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