Histological evaluation of the periodontal ligament from aged wistar rats supplemented with ascorbic acid

Ascorbic acid (AA) is able to neutralize reactive oxygen species and is essential for collagen synthesis. In aging process oxidative stress is elevated. This study aims to investigate the effects of AA supplementation on the periodontal ligament (PL) of rats during aging. Twenty five rats were used and divided into groups: J90 (90-day-old control), E345 (345-day-old control), E428 (428-day-old control), EA345 (345-day-old supplemented with AA from 90-day-old on) and EA428 (428-day-old supplemented with AA from 90-day-old on). We analyzed the thickness, density of fibroblasts and blood vessels and collagen fibers types in the PL. In group J90 there was predominantly type III collagen fibers (87.64%). In animals supplemented with AA, the area filled by type I fibers (group EA345: 65.67%, group EA428: 52.23%) was higher than type III fibers. PL in group EA428 was thicker than the one observed in group E428 (P < 0.05). During natural aging process, AA promoted the maturation of collagen fibers and enhanced angiogenesis in periodontal ligament. One can conclude that the supplementation with AA represented a beneficial factor for the development of PL in aged rats.

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Methionine-Specific Staining of Collagen

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010005408x ◽

1982 ◽

Vol 40 ◽

pp. 294-295

Author(s):

E.M. Kuhn ◽

K.D. Marenus ◽

M. Beer

Keyword(s):

Amino Acids ◽

Collagen Fibers ◽

Type Iii Collagen ◽

Type I ◽

Electron Microscopic ◽

Good Correspondence ◽

Specific Staining ◽

Type Iii ◽

Different Types ◽

Sulfur Containing

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

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Significant Type I and Type III Collagen Production from Human Periodontal Ligament Fibroblasts in 3D Peptide Scaffolds without Extra Growth Factors

PLoS ONE ◽

10.1371/journal.pone.0010305 ◽

2010 ◽

Vol 5 (4) ◽

pp. e10305 ◽

Cited By ~ 64

Author(s):

Yoshiyuki Kumada ◽

Shuguang Zhang

Keyword(s):

Growth Factors ◽

Periodontal Ligament ◽

Type Iii Collagen ◽

Type I ◽

Periodontal Ligament Fibroblasts ◽

Collagen Production ◽

Type Iii ◽

Human Periodontal Ligament Fibroblasts ◽

Peptide Scaffolds

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Collagen immunotyping in human liver: light and electron microscope study.

Journal of Histochemistry & Cytochemistry ◽

10.1177/28.11.7000887 ◽

1980 ◽

Vol 28 (11) ◽

pp. 1145-1156 ◽

Cited By ~ 133

Author(s):

J A Grimaud ◽

M Druguet ◽

S Peyrol ◽

O Chevalier ◽

D Herbage ◽

...

Keyword(s):

Type I Collagen ◽

Collagen Fibers ◽

Immunofluorescent Staining ◽

Type Iii Collagen ◽

Type I ◽

Type Iii ◽

Type Iv ◽

Matrix Organization ◽

Human Livers ◽

Type Ab

Types I, III, IV, and AB collagens have been extracted from human cirrhotic livers and specific antibodies have been raised in rabbits and purified. Histological immunofluorescent staining of collagen types in normal and fibrotic human livers reveals the respective distribution of the various collagens among the hepatic connective matrix and the modification of the normal pattern in fibrosis: types I and III appear to be the main components of the fibrotic connective matrix in enlarged portal spaces and of the Dissian reticulin framework; type IV collagen deposits are thickened around portal vessels and ducts and outline lobular capillarized sinusoids; type AB collagen appears as thin punctual deposits in portal and Dissian fibrotic connective matrix. Ultrastructural immunoperoxidase labeling of type I and III collagen makes it possible to identify the typical collagen fibers, using 65 nm periodicity, as type I collagen and the fibrillar associated network as type III collagen. Fibers of type I collagen are preferentially organized in large dense bundles in Dense Connective Matrix Organization (DCMO), since fibrillar type III collagen network is predominant in Loose Connective Matrix Organization (LCMO) surrounding vascular and biliary tracts.

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Specific immunohistochemical localization of osteonectin and collagen types I and III in fetal and adult porcine dental tissues.

Journal of Histochemistry & Cytochemistry ◽

10.1177/33.6.3889139 ◽

1985 ◽

Vol 33 (6) ◽

pp. 531-540 ◽

Cited By ~ 91

Author(s):

P S Tung ◽

C Domenicucci ◽

S Wasi ◽

J Sodek

Keyword(s):

Periodontal Ligament ◽

Type I Collagen ◽

Alveolar Bone ◽

Type Iii Collagen ◽

Similar Distribution ◽

Type I ◽

Collagen Types ◽

Type Iii ◽

Dental Tissues ◽

Strong Staining

Affinity-purified antibodies have been used in combination with the peroxidase-antiperoxidase technique to study the distribution of osteonectin and collagen types I and III in porcine dental tissues. Tissue sections (2 mm thick), including unerupted (fetal) or erupted (adult) teeth, were fixed in periodate-lysine-paraformaldehyde, demineralized in 12% w/v ethylenediaminetetraacetic acid, and after embedding, 6 micron sections were prepared for immunolocalization. Strong staining for osteonectin was observed in dentine of unerupted teeth and in the associated alveolar bone. Light to moderate staining was observed in the dental pulp, stratum intermedium, stellate reticulum, and the reticular elements in the endosteal spaces. In erupted teeth, osteonectin staining in dentine was concentrated around dentinal tubules and the associated alveolar bone stained with variable intensity. Cementum was poorly stained. However, the periodontal ligament and reticular material in the endosteal spaces showed moderate to strong staining. Weaker staining was apparent in the pulp and lamina propria of the gingiva. In comparison, type I collagen showed a similar distribution to osteonectin in both fetal and adult tissues, whereas type III collagen was generally restricted to the periodontal ligament, reticular elements of the endosteal spaces, and Sharpey's fibers in bone and cementum. Both odontoblast and ameloblast layers in fetal tissues stained for osteonectin and type III collagen.

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The effect of oxygen partial pressure on protein synthesis and collagen hydroxylation by mature periodontal tissues maintained in organ cultures

Biochemical Journal ◽

10.1042/bj1780605 ◽

1979 ◽

Vol 178 (3) ◽

pp. 605-612 ◽

Cited By ~ 7

Author(s):

Edwin H. K. Yen ◽

Jaro Sodek ◽

Antony H. Melcher

Keyword(s):

Protein Synthesis ◽

Oxygen Partial Pressure ◽

Partial Pressure ◽

Periodontal Ligament ◽

Type Iii Collagen ◽

Type I ◽

Subsequent Increase ◽

Type Iii ◽

Periodontal Tissues

Mature periodontal tissues from adult-mouse first mandibular molars were cultured in a continuous-flow organ-culture system which allowed the regulation of both ascorbic acid concentration and pO2 (oxygen partial pressure). Protein synthesis was measured by analysing the incorporation of [3H]proline into collagenous and non-collagenous proteins during the last 24h of a 2-day culture. At low pO2 [16.0kPa (approx. 120mmHg)] approx. 60% of protein-incorporated [3H]proline was found in collagenous proteins. However, it was evident that this collagen was considerably underhydroxylated. At high pO2 [56.0kPa (approx. 420mmHg)], both the amount of collagen deposited in the tissues and the degree of hydroxylation were increased considerably. In contrast, no significant effect on non-collagenous protein was observed. Tissues cultured at low pO2 for the first 48h were unable to respond to a subsequent increase in pO2 during the last 24h. Analysis of pepsin-solubilized collagen α-chains labelled with [14C]glycine demonstrated the synthesis of both type-I and type-III collagens by explants cultured for 48h at high pO2. Type-III collagen comprised 20–30% of the radioactivity in α-chains in both the periodontal ligament and the tissues of the alveolar process. The pattern of protein synthesis in the alveolar tissues at high pO2 was similar to that observed in these tissues in vivo. However, in the cultured periodontal ligament the proportions of non-collagenous proteins and type-III collagens were increased in comparison with the tissue in vivo.

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L-Ascorbic Acid 2-Phosphate Enhances the Production of Type I and Type III Collagen Peptides in Cultured Rabbit Keratocytes

Ophthalmic Research ◽

10.1159/000267149 ◽

1992 ◽

Vol 24 (2) ◽

pp. 68-72 ◽

Cited By ~ 21

Author(s):

Shizuya Saika ◽

Kenshiro Uenoyama ◽

Kenji Hiroi ◽

Akira Ooshima

Keyword(s):

Ascorbic Acid ◽

Type Iii Collagen ◽

Type I ◽

Type Iii ◽

Collagen Peptides

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Distribution of Type I and Type III collagen in the Developing Periodontal Ligament of Mice

Matrix ◽

10.1016/s0934-8832(11)80224-6 ◽

1991 ◽

Vol 11 (1) ◽

pp. 25-35 ◽

Cited By ~ 30

Author(s):

Yu Hsin Huang ◽

Yasuyoshi Ohsaki ◽

Kojiro Kurisu

Keyword(s):

Periodontal Ligament ◽

Type Iii Collagen ◽

Type I ◽

Type Iii

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Nature of collagens synthesized by monkey periodontal-ligament fibroblasts in vitro

Biochemical Journal ◽

10.1042/bj1700063 ◽

1978 ◽

Vol 170 (1) ◽

pp. 63-71 ◽

Cited By ~ 24

Author(s):

H F Limeback ◽

J Sodek ◽

D M Brunette

Keyword(s):

Periodontal Ligament ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Deae Cellulose ◽

Type Iii Collagen ◽

Type I ◽

Periodontal Ligament Fibroblasts ◽

Type Iii ◽

Type I Procollagen

1. First subcultures of fibroblast-like cells from adult monkey periodontal ligament were incubated in the presence of 14C-labelled amino acids and produced significant amounts of type-I and type-III collagens. 2. The proportion of type-III collagen produced was calculated on the basis of the recovery of procollagens from DEAE-cellulose chromatography to be approx. 20%, and at least 10% when analysed as collagens on CM-cellulose chromatography. 3. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of the procollagens, the collagens and their CNBr peptides was used to confirm the identity of the collagen types. 4. In serum-free media extensive conversion of type-I procollagen, but not of type-III procollagen, into collagen was observed, suggesting that a specific type-I procollagen peptidase was produced. 5. The pattern of collagen synthesis was not significantly different from that obtained with fibroblasts derived from skin corium of the same animals.

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