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

Matrix ◽  
1991 ◽  
Vol 11 (1) ◽  
pp. 25-35 ◽  
Author(s):  
Yu Hsin Huang ◽  
Yasuyoshi Ohsaki ◽  
Kojiro Kurisu
Keyword(s):  
Periodontal Ligament ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii

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

2013 ◽  
Vol 85 (1) ◽  
pp. 327-335 ◽  
Author(s):  
Jacqueline N. Zanoni ◽  
Nathalia M. Lucas ◽  
Aline R. Trevizan ◽  
Ivan D.S. Souza
Keyword(s):  
Ascorbic Acid ◽  
Periodontal Ligament ◽  
Aging Process ◽  
Natural Aging ◽  
Collagen Fibers ◽  
Histological Evaluation ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
The One

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.

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

1985 ◽  
Vol 33 (6) ◽  
pp. 531-540 ◽  
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.

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

1979 ◽  
Vol 178 (3) ◽  
pp. 605-612 ◽  
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.

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

1978 ◽  
Vol 170 (1) ◽  
pp. 63-71 ◽  
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.

Methionine-Specific Staining of Collagen

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).

scholarly journals Subpopulations of rat lung fibroblasts with different amounts of type I and type III collagen mRNAs.

1990 ◽  
Vol 265 (11) ◽  
pp. 6286-6290
Author(s):  
E Breen ◽  
V M Falco ◽  
M Absher ◽  
K R Cutroneo
Keyword(s):  
Lung Fibroblasts ◽  
Type Iii Collagen ◽  
Type I ◽  
Rat Lung ◽  
Type Iii

Infliximab Increases the Tissue Contents of Type-I and Type-III Collagen in Colorectal Segments Without Fecal Stream After Hartmann’s Procedure

2021 ◽  
Author(s):  
Bruna Zini de Paula Freitas ◽  
Fábio Guilherme Campos ◽  
Danilo Toshio Kanno ◽  
Andress Godoy Delben ◽  
José Aires Pereira ◽  
...  
Keyword(s):  
Hartmann’S Procedure ◽  
Type Iii Collagen ◽  
Type I ◽  
Fecal Stream ◽  
Type Iii ◽  
Hartmann's Procedure ◽  
Tissue Contents

Change in phenotype in long-term cultures of a clonal rat bone cell line: switch to the synthesis of α1 (I)-trimer collagen

1984 ◽  
Vol 62 (6) ◽  
pp. 462-469 ◽  
Author(s):  
Hardy Limeback ◽  
Kichibee Otsuka ◽  
Kam-Ling Yao ◽  
Jane E. Aubin ◽  
Jaro Sodek
Keyword(s):  
Collagen Synthesis ◽  
Type I Collagen ◽  
Bone Cell ◽  
Detectable Effect ◽  
Prostaglandin E ◽  
Intracellular Camp ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Type V

A number of bone cell clones isolated from rat calvaria have been maintained in culture for more than 3 years. Several of these clones have undergone dramatic changes in phenotype. One of these clones, RGB 2.2, was observed originally to have a fibroblastic morphology in culture and to respond to parathyroid hormone (PTH), but not prostaglandin E2 (PGE2), with an increase in intracellular cAMP. Throughout several passages in early subcultures, these cells synthesized mostly type I collagen, with small amounts of type III and type V collagens. Whereas PTH had no detectable effect on collagen synthesis, PGE2 decreased the amount of total cell layer collagen, with the greatest effect on type III collagen, while increasing the proportion of type V collagen. Subsequent studies on these cells during 3 years in culture have indicated changes in their phenotype including a progressive change in morphology to a more cuboidal shape and a change in collagen synthesis, the cells producing large amounts of the "embryonic" collagen, α1(I) trimer. The reason(s) for the change in collagen expression is unknown, but may be the result of a change in which gene(s) is being expressed.

scholarly journals PERITONEAL ADHESIONS TYPE I, III AND TOTAL COLLAGEN ON POLYPROPYLENE AND COATED POLYPROPYLENE MESHES: EXPERIMENTAL STUDY IN RATS

2017 ◽  
Vol 30 (2) ◽  
pp. 77-82 ◽  
Author(s):  
Lucas Félix ROSSI ◽  
Manoel Roberto Maciel TRINDADE ◽  
Armando José D`ACAMPORA ◽  
Luise MEURER
Keyword(s):  
Type I Collagen ◽  
Cell Types ◽  
Type Iii Collagen ◽  
Type I ◽  
Abdominal Adhesions ◽  
Peritoneal Adhesions ◽  
Type Iii ◽  
Total Collagen

ABSTRACT Background: Hernia correction is a routinely performed treatment in surgical practice. The improvement of the operative technique and available materials certainly has been a great benefit to the quality of surgical results. The insertion of prostheses for hernia correction is well-founded in the literature, and has become the standard of treatment when this type of disease is discussed. Aim: To evaluate two available prostheses: the polypropylene and polypropylene coated ones in an experimental model. Methods: Seven prostheses of each kind were inserted into Wistar rats (Ratus norvegicus albinus) in the anterior abdominal wall of the animal in direct contact with the viscera. After 90 days follow-up were analyzed the intra-abdominal adhesions, and also performed immunohistochemical evaluation and videomorphometry of the total, type I and type III collagen. Histological analysis was also performed with hematoxylin-eosin to evaluate cell types present in each mesh. Results: At 90 days the adhesions were not different among the groups (p=0.335). Total collagen likewise was not statistically different (p=0.810). Statistically there was more type III collagen in the coated polypropylene group (p=0.039) while type I was not different among the prostheses (p=0.050). The lymphocytes were statistically more present in the polypropylene group (p=0.041). Conclusion: The coated prosthesis was not different from the polypropylene one regarding the adhesion. Total and type I collagen were not different among the groups, while type III collagen was more present on the coated mesh. There was a greater number of lymphocytes on the polypropylene mesh.

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