Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The age-related decrease in hydroxyproline : creatinine ratio in young guinea pigs was significantly smaller in vitamin C-deficient animals than in pair-fed controls. The same was true for proline : creatinine and total amino nitrogen : creatinine ratios, but hydroxyproline : total amino nitrogen and proline : total amino nitrogen ratios were not significantly affected by deficiency. 2. Although the proline : hydroxyproline ratio was unaffected in unfractionated urine, acute or chronic deficiency produced a small but significant increase in this ratio in collagenase digests of the acetone-insoluble fraction. 3. In scorbutic animals, therefore, collagen probably turns over more rapidly than in animals matched for inanition. Some at least, of this increase could represent the rapid turnover of underhydroxylated nascent collagen. Because it contains the degradation products from collagen from many tissues, differing widely in sensitivity to vitamin C status, the urine is unlikely, however, to provide a specific and sensitive functional index of vitamin C status.
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PMID:Vitamin C deficiency in guinea pigs: changes in urinary excretion of proline, hydroxyproline and total amino nitrogen. 46 70

1. After the administration of labelled proline to guinea pigs deprived of ascorbic acid for 15 days, the dorsal skin was examined 5 days later in an attempt to detect the presence of hydroxyproline-deficient collagen (protocollagen). The extent of incorporation of proline into skin collagens indicated a severe impairment of collagen synthesis. 2. A comparison of proline and hydroxyproline specific radioactivities in diffusible peptides obtained by treatment with collagenase of either purified skin collagens or direct hot-trichloroacetic acid extracts of skin failed to indicate the presence of protocollagen. Possible reasons for this are discussed. 3. The incorporation results did not indicate an inability of normal collagen, i.e. collagen hydroxylated to the normal degree, to cross-link in scurvy. 4. Incorporation of labelled proline into aortic elastin isolated from the same animals did not indicate a decrease in elastin biosynthesis in ascorbic acid deficiency, beyond that attributable to the inanition accompanying the vitamin deficiency. The proline/hydroxyproline specific-radioactivity ratio in elastin from scorbutic guinea pigs was about 6:1 in contrast with the 1:1 ratio in control groups. It is concluded that the formation of elastin hydroxyproline was ascorbate-dependent and that a hydroxyproline-deficient elastin is formed and retained in scurvy. The formation of desmosines was unimpaired in scorbutic animals. 5. Studies with chick embryos confirmed the formation of elastin hydroxyproline from free proline. Incorporation of free hydroxyproline into elastin hydroxyproline was negligible. 6. Digestion of solubilized samples with collagenase indicated that the hydroxyproline in guinea-pig aortic elastin preparations was not derived from contamination by collagen. It is suggested that most if not all of the hydroxyproline in the guinea pig elastin preparations investigated can be considered an integral part of the elastin molecule.
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PMID:Studies in vivo on the biosynthesis of collagen and elastin in ascorbic acid-deficient guinea pigs. 430 21