Biochemical study of collagen turnover in rat incisor periodontal ligament

Orlowski, Walter A.

doi:10.1016/0003-9969(78)90125-5

Cited by 26 publications

(24 citation statements)

References 18 publications

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“…The more rapid turnover of structural noncollagenous proteins agrees well with the data of Orlowski (1978), Sodek (1977) and Slootweg (1976). Apart from the results of Orlowski (1976) only autoradiographic data on the turnover rate of sulphated GAG are available, all indicating a short half-life (Eccles, 1962;Baumhammers and Stallard, 1968).…”

Section: Discussionsupporting

confidence: 89%

“…The half-life of insoluble collagen of the PDL is similar to the values found by A.A.R. Taverne and G. J. M. Tonino (data not presented) and Orlowski (1978) for rat and Guis (1976) and Slootweg (1976) for guinea pig, whereas the values reported by Sodek (1977) indicate a much shorter half-life. However, this may be ascribed to his unconventional approach to study half-life of collagen by measuring the rate of the initial incorporation of ['HI-proline as hydroxyproline in insoluble collagen in contrast with our approach in which after reaching maximal incorporation the decrease of specific radioactivity of incorporated hydroxyproline with time is determined.…”

Section: Discussionsupporting

confidence: 87%

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Composition and metabolism of the extracellular matrix in the periodontal ligament of impeded and unimpeded rat incisors

Bos

Tonino

1984

Archives of Oral Biology

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Summary-Potential differences were studied in the composition and metabolism of the connective tissue components (collagen, non-collagenous proteins and glycosaminoglycans) of the periodontal ligament (PDL) as a result of alterations in the rate of eruption. The amount of collagen, glycosaminoglycan (GAG) or the water 'content of the tissue was the same in the unimpeded and impeded situation. The only difference was in the amount of structural non-collagenous proteins: 33 per cent increase in the unimpeded PDL. The rate of turnover of insoluble collagen, structural non-collagenous proteins and the sulphated GAG, studied in uivo by administration of [3H]-proline or ["S]-sulphate, did not differ significantly in both situations: their extremely short half-lives were respectively 9.7, 3.5 and 1.7 days. Increase in the rate of eruption and hence in the remodelling process does not result in alterations in the metabolic activity of the PDL components.Their metabolism is probably already at maximal rate and may permit the more rapid rate of eruption when the opposing force of the antagonists is diminished during the non-occlusional state of the incisors.

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Section: Discussionsupporting

confidence: 89%

Section: Discussionsupporting

confidence: 87%

Composition and metabolism of the extracellular matrix in the periodontal ligament of impeded and unimpeded rat incisors

Bos

Tonino

1984

Archives of Oral Biology

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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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Distribution of ³H‐proline within transseptal fibers of the rat following release of orthodontic forces

Row

Johnson

1990

Am. J. Anat.

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Maxillary right first molar teeth of rats were tipped mesially with an orthodontic appliance for 2 weeks (experimental group), 3H-proline was injected, and orthodontic forces were removed 6 hr later (time 0). The contralateral molar teeth of treated (internal control group) and age- and weight-matched untreated animals (external control group) were also studied. Diastemata were created between the molar teeth by the orthodontic appliance, and transseptal fibers between first and second (P less than 0.001) and second and third molars (P less than 0.005) were significantly lengthened as compared to external and internal controls at time 0. Diastemata between molar teeth were closed 5 days after removal of orthodontic force. Transseptal fibers adjacent to the source of the orthodontic force (mesial region) had the highest mean number of 3H-proline-labeled proteins at time 0 and at all times following removal of the force (P less than 0.001), and had the highest rate of labeled protein removal (P less than 0.001). Half-lives for removal of 3H-proline-labeled transseptal fiber proteins were significantly greater in mesial and distal regions and significantly less in middle regions of experimentals than in corresponding regions of external controls (P less than 0.001). These data suggest the following: 1) transseptal fibers adjust their length by rapid remodeling in regions experiencing a tensile force; 2) collagenous protein turnover within the middle third of the transseptal fibers is more rapid subsequent to release of orthodontic force than during normal physiologic drift, suggesting that this region adapts rapidly to changes in adjacent tooth position and that these fibers do not play a significant role in relapse of orthodontically relocated teeth; and 3) significant differences in turnover rates of 3H-proline-labeled transseptal ligament proteins of external and internal control quadrants suggest that tooth movement produces both local and systemic effects on collagenous protein metabolism.

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Biochemical study of collagen turnover in rat incisor periodontal ligament

Cited by 26 publications

References 18 publications

Composition and metabolism of the extracellular matrix in the periodontal ligament of impeded and unimpeded rat incisors

Composition and metabolism of the extracellular matrix in the periodontal ligament of impeded and unimpeded rat incisors

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

Distribution of ³H‐proline within transseptal fibers of the rat following release of orthodontic forces

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Biochemical study of collagen turnover in rat incisor periodontal ligament

Cited by 26 publications

References 18 publications

Composition and metabolism of the extracellular matrix in the periodontal ligament of impeded and unimpeded rat incisors

Composition and metabolism of the extracellular matrix in the periodontal ligament of impeded and unimpeded rat incisors

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

Distribution of 3H‐proline within transseptal fibers of the rat following release of orthodontic forces

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Distribution of ³H‐proline within transseptal fibers of the rat following release of orthodontic forces