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The collagen content of skin and gingival tissues in ascorbic acid‐deficient monkeys
Author(s) -
ØSstergaard E.,
Löe Harald
Publication year - 1975
Publication title -
journal of periodontal research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.31
H-Index - 83
eISSN - 1600-0765
pISSN - 0022-3484
DOI - 10.1111/j.1600-0765.1975.tb00014.x
Subject(s) - hydroxyproline , ascorbic acid , proline , collagenase , granulation tissue , chemistry , biochemistry , wound healing , medicine , enzyme , amino acid , food science , surgery
Five green monkeys were used In this study. Three animals were fed a scorbutigenic diet and the remaining two served as controls. Biopsies were dissected from the vestibular gingiva and dorsal skin and polyvinyl sponges were implanted subcutaneously during 4 week periods throughout the experimental period. The animals were sacrificed after 12 weeks and the periodontal ligament was removed. Collagen extracts were prepared from the gingival and granulation tissues and treated with bacterial collagenase. Following acid hydrolysis the total amount of proline and hydroxyproline was determined in the various tissue preparations. In the tissues examined, the content of hydroxyproline decreased in the scorbutic animals throughout the experimental period. The decrease in the hydroxyproline content of the gingiva started within the first 4 weeks and was faster than that of the skin, indicating that the extent of decrease is dependent of the turnover rate of the collagen in the tissues. The synthesis of hydroxyproline was almost totally impaired in the granulation tissue formed in the sponges implanted after the 8th week of experimentation. Collagenase treatment of collagen extracts resulted in a release of proline and hydroxyproline in a higher ratio in extracts from the experimental animals than in extracts from the controls. It is concluded that ascorbic acid is a prerequisite for the maintenance of the collagen pool in the tissues and that lack of this vitamin results in the formation of a collagenase degradable protein fraction with a low hydroxyproline content.