Pulsed heat shocks enhance procollagen type I and procollagen type III expression in human dermal fibroblasts

2010 ◽  
Author(s):  
S. D. Dams ◽  
M. de Liefde-van Beest ◽  
A. M. Nuijs ◽  
C. W. J. Oomens ◽  
F. P. T. Baaijens
Keyword(s):  
Dermal Fibroblasts ◽  
Type I ◽  
Human Dermal Fibroblasts ◽  
Type Iii ◽  
Procollagen Type ◽  
Procollagen Type I ◽  
Heat Shocks

scholarly journals Asiaticoside induces cell proliferation and collagen synthesis in human dermal fibroblasts

2015 ◽  
Vol 34 (2) ◽  
pp. 96
Author(s):  
Linda Yuliati ◽  
Etik Mardliyati ◽  
Kusmarinah Bramono ◽  
Hans Joachim Freisleben
Keyword(s):  
Cell Proliferation ◽  
Wound Healing ◽  
Retinoic Acid ◽  
Collagen Synthesis ◽  
Active Agent ◽  
Dermal Fibroblasts ◽  
Type Iii Collagen ◽  
Type I ◽  
Human Dermal Fibroblasts ◽  
Type Iii

Background<br />Asiatiocoside, a saponin component isolated from Centella asiatica can improve wound healing by promoting the proliferation of human dermal fibroblasts (HDF) and synthesis of collagen. The skin-renewing cells and type I and III collagen synthesis decrease with aging, resulting in the reduction of skin elasticity and delayed wound healing. Usage of natural active compounds from plants in wound healing should be evaluated and compared to retinoic acid as an active agent that regulates wound healing. The aim of this study was to compare and evaluate the effect of asiaticoside and retinoic acid to induce greater cell proliferation and type I and III collagen synthesis in human dermal fibroblast.<br /><br />Methods<br />Laboratory experiments were conducted using human dermal fibroblasts (HDF) isolated from human foreskin explants. Seven passages of HDF were treated with asiaticoside and retinoic acid at several doses and incubated for 24 and 48 hours. Cell viability in all groups was tested with the MTT assay to assess HDF proliferation. Type I and III collagen synthesis was examined using the respective ELISA kits. Analysis of variance was performed to compare the treatment groups. <br /><br />Results<br />Asiaticoside had significantly stronger effects on HDF proliferation than retinoic acid (p&lt;0.05). The type III collagen production was significantly greater induction with asiaticoside compared to retinoic acid (p&lt;0.05). <br /><br />Conclusion<br />Asiaticoside induces HDF proliferation and type I and III collagen synthesis in a time- and dose-dependent pattern. Asiaticoside has a similar effect as retinoic acid on type I and type III collagen synthesis.

Procollagen Type I C-terminal propeptide, procollagen Type III N-terminal propeptide, hyaluronic acid, and laminin in the cerebrospinal fluid of rats with communicating hydrocephalus

2013 ◽  
Vol 11 (6) ◽  
pp. 692-696 ◽  
Author(s):  
Hao Xu ◽  
Zhanxiang Wang ◽  
Shaolin Zhang ◽  
Guowei Tan ◽  
Hongwei Zhu
Keyword(s):  
Hyaluronic Acid ◽  
Saline Control ◽  
Control Group ◽  
Communicating Hydrocephalus ◽  
Type I ◽  
Type Iii ◽  
Procollagen Type ◽  
Procollagen Type I ◽  
Group 5 ◽  
Diagnostic Index

Object Fibrosis along the route of CSF flow is indicated by the development of hydrocephalus. The changes of fibrosis index might reflect the level of hydrocephalus and even become a diagnostic index of hydrocephalus. The object of this study was to analyze the levels of procollagen Type I C-terminal propeptide (PICP), procollagen Type III N-terminal propeptide (PIIINP), hyaluronic acid (HA), and laminin (LN) and their significance in the CSF of communicating hydrocephalus rat models. Methods Thirty adult Sprague-Dawley rats were randomly divided into 3 groups: hydrocephalus group (20 rats) with intraventricular kaolin injections, sham control group (5 rats) with saline injections, and normal group (5 rats) without any processing. The levels of PICP, PIIINP, HA, and LN in the CSF were detected using ELISA. Results Levels of PICP, PIIINP, HA, and LN in the hydrocephalus group were significantly higher than those in the saline control group (p < 0.05). It was revealed by correlation analysis that the increase was positively correlated with the severity of ventricular dilation. Conclusions Results indicated that PICP, PIIINP, HA, and LN continue to rise dramatically in experimental hydrocephalus and may serve as the diagnostic index of hydrocephalus.

Pulsed Heat Shocks to Enhance Collagen Production of Human Dermal Fibroblasts in Ex-Vivo Skin

2010 ◽  
Author(s):  
S. D. Dams ◽  
M. de Liefde ◽  
A. M. Nuijs ◽  
C. W. J. Oomens ◽  
F. P. T. Baaijens
Keyword(s):  
Ex Vivo ◽  
Contemporary Literature ◽  
Collagen Matrix ◽  
Dermal Fibroblasts ◽  
Human Dermal Fibroblasts ◽  
Procollagen Type ◽  
Different Temperatures ◽  
Heat Shocks ◽  
Ablative Techniques ◽  
Type 3

Well-known characteristics of aging skin are the development of fine lines and wrinkles, but also changes in skin tone, skin texture, thickness and moisture content [1, 2]. Rejuvenation of the skin aims at reversing the signs of aging and can be established in the epidermis as well as in the dermis. Aged dermis for that matter has a degenerated collagen matrix. To regenerate this matrix, fibroblasts need to be stimulated into synthesizing new collagen. Among the rejuvenation methods used the non-ablative techniques are gaining popularity. These methods produce dermal remodeling without obvious epidermal injury using a thermal approach. The generation of heat would cause collagen injury and contraction followed by collagen synthesis [2, 3]. However, little research on physiological evidence can be found in contemporary literature. In this study, the effects of heat shocks of different temperatures on the expression of procollagen type 1and type 3 of human dermal fibroblasts in ex-vivo skin are investigated.

scholarly journals Mutations in COL1A1 and COL1A2 Genes Associated with Osteogenesis Imperfecta (OI) Types I or III.

2018 ◽  
Vol 65 (1) ◽  
pp. 79-86 ◽  
Author(s):  
Aleksandra Augusciak-Duma ◽  
Joanna Witecka ◽  
Aleksander L. Sieroń ◽  
Magdalena Janeczko ◽  
Jacek J Pietrzyk ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
Collagen Type ◽  
Collagen Type I ◽  
Base Substitution ◽  
Type I ◽  
Intracellular Accumulation ◽  
Single Base ◽  
Type Iii ◽  
Procollagen Type ◽  
Procollagen Type I

Over 85% of osteogenesis imperfecta (OI) cases associates to mutations in procollagen type I genes (COL1A1 or COL1A2), however, no hot spots were linked to particular clinical phenotypes. The 8 patients whom were clinically diagnosed with OI are from Polish population with no ethnic background indicated. Six unpublished mutations were detected in eight patients diagnosed with OI. Genotypes for polymorphisms (Sp1 - rs1800012 and PvuII - rs412777), linked to bone formation and metabolism were also determined. In COL1A1 gene the mutations were found in exons 2, 22, 50 and in introns 13 and 51. In COL1A2 one mutation was identified in exon 22. Mutations of deletion type in COL1A1 that resulted in OI type I an effect neither on collagen type I secretion nor its intracellular accumulation were detected. Also, a single base substitution in I13 (c.904-9 G>T) was associated with OI type I. The OI type III was associated with single base change in I51 of COL1A1, possibly causing an exon skipping. Also, a missense mutation in COL1A2 changing Gly®Cys in the central part of triple helical domain of the collagen type I molecule caused OI type III. It affected secretion of heterotrimeric form of procollagen type I. However, no intracellular accumulation of procollagen chains could be detected. Mutation in COL1A2 affected its incorporation to procollagen type I. The results shall help in genetic counseling of OI patients and provide rational support in making by them and their families conscious, life important decisions.

Heat shocks enhance procollagen type I and III expression in fibroblasts in ex vivo human skin

2011 ◽  
Vol 17 (2) ◽  
pp. 167-180 ◽  
Author(s):  
S. D. Dams ◽  
M. de Liefde-van Beest ◽  
A. M. Nuijs ◽  
C. W. J. Oomens ◽  
F. P. T. Baaijens
Keyword(s):  
Human Skin ◽  
Ex Vivo ◽  
Type I ◽  
Procollagen Type ◽  
Procollagen Type I ◽  
Heat Shocks

Increased serum concentrations of type I procollagen C-terminal propeptide and osteocalcin during a short course of calcitriol administration to adult male volunteers

1991 ◽  
Vol 125 (6) ◽  
pp. 609-613 ◽  
Author(s):  
Jeppe Gram ◽  
Jens Bollerslev ◽  
Henning K. Nielsen ◽  
Peter Junker
Keyword(s):  
Serum Concentration ◽  
Serum Levels ◽  
Bone Collagen ◽  
Type I ◽  
Type Iii ◽  
Procollagen Type ◽  
Short Course ◽  
Procollagen Type I ◽  
Serum Hyaluronan ◽  
Healthy Males

Abstract. To investigate bone collagen metabolism during vitamin D treatment, 15 healthy males (aged 28-45 years, median 34) were treated orally with calcitriol, 2 μg daily for 7 days and followed for a total of 2 weeks. The serum concentration of calcitriol rose markedly (median difference and 95% confidence limits: 49% (5-82), p<0.005) during treatment, whereas serum levels of calcidiol, and calcium remained unchanged. The serum level of procollagen type I C-terminal propeptide rose 15% (7-33, p<0.003), whereas no alterations were observed concerning serum procollagen type III N-terminal propeptide, and serum hyaluronan. The serum concentration of osteocalcin rose concomitantly (26% (12-45), p<0.003). All values returned to baseline levels within seven days after the treatment week. The serum levels of osteocalcin and procollagen type I C-terminal propeptide were positively correlated (rs=0.71, p<0.004) during the study. Serum procollagen type I C-terminal propeptide and serum osteocalcin did not correlate with serum procollagen type III N-terminal propeptide or serum hyaluronan either at baseline or after treatment. It is concluded that a short course of calcitriol administration to healthy males stimulates the biosynthesis of bone-related matrix proteins. By contrast, connective tissue components of predominantly extraosseous origin are not affected.

Expression of TGF-β and procollagen type I and type III in human gastric carcinomas

1989 ◽  
Vol 44 (3) ◽  
pp. 394-398 ◽  
Author(s):  
Kazuhiro Yoshida ◽  
Hiroshi Yokozaki ◽  
Minoru Niimoto ◽  
Hisao Ito ◽  
Masanori Ito ◽  
...  
Keyword(s):  
Type I ◽  
Gastric Carcinomas ◽  
Type Iii ◽  
Procollagen Type ◽  
Procollagen Type I

scholarly journals Non pharmacological high-intensity ultrasound treatment of human dermal fibroblasts to accelerate wound healing

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Jeong Yu Lee ◽  
Dae-Jin Min ◽  
Wanil Kim ◽  
Bum-Ho Bin ◽  
Kyuhan Kim ◽  
...  
Keyword(s):  
Wound Healing ◽  
High Intensity ◽  
Mapk Pathway ◽  
Dermal Fibroblasts ◽  
Ultrasound Treatment ◽  
Type I ◽  
Human Dermal Fibroblasts ◽  
Short Term ◽  
High Intensity Ultrasound ◽  
Extracellular Matrix Components

AbstractInspired by the effectiveness of low-intensity ultrasound on tissue regeneration, we investigated the potential effect of short-term high-intensity ultrasound treatment for acceleration of wound healing in an in vitro wound model and dermal equivalent, both comprising human dermal fibroblasts. Short-term ultrasound of various amplitudes significantly increased the proliferation and migration of fibroblasts and subsequently increased the production of the extracellular matrix components fibronectin and collagen type I, both of which are important for wound healing and are secreted by fibroblasts. In addition, ultrasound treatment increased the contraction of a fibroblast-embedded three-dimensional collagen matrix, and the effect was synergistically increased in the presence of TGF-β. RNA-sequencing and bioinformatics analyses revealed changes in gene expression and p38 and ERK1/2 MAPK pathway activation in the ultrasound-stimulated fibroblasts. Our findings suggest that ultrasound as a mechanical stimulus can activate human dermal fibroblasts. Therefore, the activation of fibroblasts using ultrasound may improve the healing of various types of wounds and increase skin regeneration.

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