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

PLoS ONE ◽  
2010 ◽  
Vol 5 (4) ◽  
pp. e10305 ◽  
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

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.

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 Interleukin-1 α modulates collagen gene expression in cultured synovial cells

1988 ◽  
Vol 252 (1) ◽  
pp. 247-255 ◽  
Author(s):  
A Mauviel ◽  
L Teyton ◽  
R Bhatnagar ◽  
H Penfornis ◽  
M Laurent ◽  
...  
Keyword(s):  
Steady State ◽  
Type I Collagen ◽  
Interleukin 1 ◽  
Blot Hybridization ◽  
Mrna Level ◽  
Type Iii Collagen ◽  
Type I ◽  
Synovial Cells ◽  
Collagen Production ◽  
Type Iii

The effects of porcine interleukin-1 (IL-1) alpha on collagen production were studied in cultured human rheumatoid synovial cells. Addition of 0.05-5 ng of IL-1/ml into the cultures resulted in a dose-dependent decreased rate of collagen released into the medium over 24 h. To determine whether this inhibition was due to secondary action of prostaglandin E2 (PGE2) secreted in response to IL-1, cultures were incubated in presence of various inhibitors of arachidonate metabolism. Depending on the cell strains, these inhibitors were able to suppress or diminish the effect of IL-1, suggesting that PGE2 is involved in the mechanism. Depression of collagen production caused by IL-1 mainly affected type I collagen and therefore led to a change in the type I/type III collagen ratio in the extracellular medium. Steady-state levels of mRNA for types I and III procollagens were estimated by dot-blot hybridization and compared with the amounts of respective collagens produced in the same cultures. IL-1 generally increased procollagen type I mRNA, but to a variable extent, as did indomethacin (Indo). Depending on the cell strain, the combination of indo and IL-1 could elevate the mRNA level of type I procollagen compared with Indo alone. These results did not correlate with the production rate of collagen in the medium, which was diminished by exposure to IL-1. The level of mRNA for collagen type III was not greatly changed by incubation with IL-1, and a better correlation was generally observed with the amount of type III collagen found in the medium. These data suggest that an additional control mechanism at translational or post-translational level must exist, counterbalancing the stimulatory effect of IL-1 on collagen mRNA transcription. It is likely that IL-1 could modulate the production of collagen in synovial cells by an interplay of different mechanisms, some of them limiting the effect of primary elevation of the steady-state mRNA level.

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.

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