1998
DOI: 10.1016/s0955-2863(98)00039-4
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Changes in collagen cross-link ratios in bone and urine of guinea pigs fed graded dietary vitamin C: a functional index of vitamin C status

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Cited by 13 publications
(6 citation statements)
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“…As in our first study (Tsuchiya & Bates, 1997), the concentration of hydroxyproline per unit wet weight of femur did not differ significantly between feed groups. In our second study (Tsuchiya & Bates, 1998), a small and unexpected increase in femur shaft hydroxyproline per unit wet weight was seen when the vitamin C content of the diet was decreased. Taking all three studies together, it appears that femur shaft collagen, unlike dorsal skin collagen, does not fall precipitously in animals that are deprived of vitamin C, nor is it significantly affected in animals whose growth is retarded by total food restriction.…”
Section: Discussionmentioning
confidence: 58%
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“…As in our first study (Tsuchiya & Bates, 1997), the concentration of hydroxyproline per unit wet weight of femur did not differ significantly between feed groups. In our second study (Tsuchiya & Bates, 1998), a small and unexpected increase in femur shaft hydroxyproline per unit wet weight was seen when the vitamin C content of the diet was decreased. Taking all three studies together, it appears that femur shaft collagen, unlike dorsal skin collagen, does not fall precipitously in animals that are deprived of vitamin C, nor is it significantly affected in animals whose growth is retarded by total food restriction.…”
Section: Discussionmentioning
confidence: 58%
“…vitamin C inadequacy) in man. As noted previously (Tsuchiya & Bates, 1998), the high sensitivity of bone and urinary collagen crosslink ratios to moderate degrees of vitamin C-restriction in guinea-pigs helps to complete the sequence from a pathological lesion (scurvy), via a defined biochemical reaction (altered cross-link ratios), to a potential non-invasive biochemical probe of vitamin C status.…”
Section: Discussionmentioning
confidence: 73%
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“…[12][13][14] L-Ascorbic acid (vitamin C), a representative water-soluble vitamin, has a variety of biological, pharmaceutical and dermatological functions; it promotes collagen biosynthesis, provides photoprotection, causes melanin reduction, scavenges free radicals, and enhances the immunity (antiviral effect). [15][16][17][18][19] These properties are closely related to the well-known antioxidant properties of this compound. However, the transdermal permeability of vitamin C is low.…”
Section: Introductionmentioning
confidence: 82%
“…This vitamin is a cofactor for two enzymes, lysyl and prolyl hydroxylases, which are related to collagen hydroxylation. The function of AA as a cofactor for these enzymes is to avoid their iron atom oxidation and, consequently, protect them from autoinactivation (Azulay et al 2003, Tuero 2000, Parsons et al 2006, Murad et al 1981, Tsuchiya and Bates 1998, Senturk et al 2004. AA also enhances the collagen synthesis because it increases the gene expression of fibroblasts (Tuero 2000, Senturk et al 2004.…”
mentioning
confidence: 99%