Collagen turnover in the gingiva and other mature connective tissues of the marmoset Saguinus oedipus

Page, Roy C.; Ammons, William F.

doi:10.1016/0003-9969(74)90133-2

Cited by 58 publications

(29 citation statements)

References 18 publications

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“…The hypothesis which appears most compatible with our observations is that of selection of an unusual cell population by the (32). These variations in collagen type, amount, and turnover time may be functions of the particular cell populations maldng up the tissue at a given point in time, rather than modulation of the activities of a single cell type.…”

supporting

confidence: 76%

Diphenylhydantoin (dilantin) gingival hyperplasia: drug-induced abnormality of connective tissue.

Hassell¹,

Page²,

Narayanan³

et al. 1976

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

189

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supporting

confidence: 76%

Diphenylhydantoin (dilantin) gingival hyperplasia: drug-induced abnormality of connective tissue.

Hassell¹,

Page²,

Narayanan³

et al. 1976

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

189

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“…Although extensive studies assessing the rate of collagen and protein turnover in periodontal tissues have been performed [6][7][8][9][10], relatively little is known about the non-collagenous matrix of the periodontium [3]. The turnover rate of collagens and non-collagenous proteins in the periodontium has been shown to be high [6][7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

“…The turnover rate of collagens and non-collagenous proteins in the periodontium has been shown to be high [6][7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

“…These changes are generally considered to be a consequence, not a cause, of the aging process [11]. Age is considered to be one of the factors affecting the synthesis of collagenr [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15] and protein [11] in connective tissues. A marked reduction in protein and collagen production with increasing donor age has been shown in cultures established from normal human gingiva [11].…”

Section: Introductionmentioning

confidence: 99%

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Hydroxyproline and Total Protein Levels in Gingiva and Gingival Crevicular Fluid in Periodontally Healthy Human Subjects.

Akalın

Şengün

Renda

et al. 1992

The Journal of Nihon University School of Dentistry

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Age is known to be one of the factors which affect the rate of collagen and protein turnover in the connective tissues of the periodontium. The aim of the present study was to determine the levels of hydroxyproline (Hyp) and total protein in both the gingiva and gingival crevicular fluid (GCF) of periodontally healthy human subjects of two different age groups. The subjects of the young group were selected from among patients scheduled for extraction of upper and lower first or second premolars for orthodontic reasons. The second (older) group included individuals whose teeth were to be extracted for endodontic reasons. GCF was obtained before gingival sampling. The tissues surrounding the sockets were harvested immediately after extraction of the indicated teeth. All samples were analyzed biochemically. No significant difference was found in gingival and GCF levels of Hyp (which is unique to collagen) between the groups. Total protein levels in gingiva were significantly higher in the young group than in the older group. GCF total protein levels showed no significant difference between the groups. The higher gingival protein levels in the younger group seem to conform to previous findings.

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“…Recent biochemical studies [23,24] have shown that in comparison with that in other connective tissues, the turnover of collagen in the periodontal tissues is rapid. The reasons for this are not clear, but it has been suggested that intermittent occlusal forces acting on the collagen fibers, particularly during mastication, may be of relevance [24].…”

Section: Discussionmentioning

confidence: 98%

Rabbit cranial sutures in vitro: A new experimental model for studying the response of fibrous joints to mechanical stress

et al. 1979

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An organ culture system has been developed whereby mechanical stress can be applied to cranial sutures under controlled experimental conditions. The application of a continuous tensile mechanical stress (30 g) to cranial sutures from newborn rabbits (1--2 days) was accompanied by a significant increase in the incorporation of 3H-leucine and 3H-proline into suture protein. The specific activities of 3H-hydroxyproline indicated that mechanical stress produced a two-fold increase in the incorporation of 3H-proline into collagen. However, the proportion of the total radioactivity recoverable in collagen (45.63 +/- 2.33% for nonstressed; 40.58 +/- 2.17% for stressed sutures) was not significantly different. These data suggest that the increase in collagen synthesis occurs as part of a general stimulation of protein synthesis, and do not support the view that mechanical stress is the principal mechanism regulating the turnover of collagen in fibrous joints. These initial studies demonstrate that an in vitro experimental model has considerable potential for investigating the morphological and metabolic response of fibrous joints to mechanical deformation.

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Collagen turnover in the gingiva and other mature connective tissues of the marmoset Saguinus oedipus

Cited by 58 publications

References 18 publications

Diphenylhydantoin (dilantin) gingival hyperplasia: drug-induced abnormality of connective tissue.

Diphenylhydantoin (dilantin) gingival hyperplasia: drug-induced abnormality of connective tissue.

Hydroxyproline and Total Protein Levels in Gingiva and Gingival Crevicular Fluid in Periodontally Healthy Human Subjects.

Rabbit cranial sutures in vitro: A new experimental model for studying the response of fibrous joints to mechanical stress

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