The difference between residual monomer dentin bonding HEMA and UDMA with acetone and ethanol solvent after binding to type I collagen

Background: In caries and non-caries lesions involving dentine, it is necessary to provide dentine-bonding material to help improve retention between the composite resin and the tooth surface. Composite resin attachment to dentine is influenced by bonding polymerization reactions. In several studies, researchers found that polymerized monomers will experience volume shrinkage because not all will fully polymerize but, rather, become residual monomers that can cause post-operative pain. Purpose: This study aimed to identify the difference in the amount of residual monomers between HEMA- and UDMA-based dentin bonding materials with acetone and ethanol solvents after binding to type I collagen. Methods: Four groups featured in this study: HEMA with acetone solvent and type I collagen , HEMA with ethanol solvent and type I collagen , UDMA with acetone solvent and type I collagen and UDMA with ethanol solvent and type I collagen . All groups were checked by high performance liquid chromatography (HPLC) to quantify the remaining amount of monomers. Results: The percentage of residual monomers of dentine bonding HEMA with acetone solvent and type I collagen was 10.69%, HEMA with ethanol solvent and type I collagen was 13.93%, UDMA with acetone solvent and type I collagen was 2.89% and UDMA with ethanol solvent and type I collagen was 7.48%. Conclusion: HEMA with ethanol solvent has the highest number of residual monomers, while UDMA with acetone solvent has the lowest.

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Contractile properties of EDL and soleus muscles of myostatin-deficient mice

Journal of Applied Physiology ◽

10.1152/japplphysiol.00126.2006 ◽

2006 ◽

Vol 101 (3) ◽

pp. 898-905 ◽

Cited By ~ 95

Author(s):

Christopher L. Mendias ◽

James E. Marcin ◽

Daniel R. Calerdon ◽

John A. Faulkner

Keyword(s):

Type I Collagen ◽

Contractile Properties ◽

Negative Regulator ◽

Type I ◽

Lengthening Contractions ◽

Tetanic Force ◽

The Difference ◽

The Impact ◽

Deficient Mice

Myostatin is a negative regulator of muscle mass. The impact of myostatin deficiency on the contractile properties of healthy muscles has not been determined. We hypothesized that myostatin deficiency would increase the maximum tetanic force (Po), but decrease the specific Po(sPo) of muscles and increase the susceptibility to contraction-induced injury. The in vitro contractile properties of extensor digitorum longus (EDL) and soleus muscles from wild-type ( MSTN+/+), heterozygous-null ( MSTN+/−), and homozygous-null ( MSTN−/−) adult male mice were determined. For EDL muscles, the Poof both MSTN+/−and MSTN−/−mice were greater than the Poof MSTN+/+mice. For soleus muscles, the Poof MSTN−/−mice was greater than that of MSTN+/+mice. The sPoof EDL muscles of MSTN−/−mice was less than that of MSTN+/+mice. For soleus muscles, however, no difference in sPowas observed. Following two lengthening contractions, EDL muscles from MSTN−/−mice had a greater force deficit than that of MSTN+/+or MSTN+/−mice, whereas no differences were observed for the force deficits of soleus muscles. Myostatin-deficient EDL muscles had less hydroxyproline, and myostatin directly increased type I collagen mRNA expression and protein content. The difference in the response of EDL and soleus muscles to myostatin may arise from differences in the levels of a myostatin receptor, activin type IIB. Compared with the soleus, the amount of activin type IIB receptor was approximately twofold greater in EDL muscles. The results support a significant role for myostatin not only in the mass of muscles but also in the contractility and the composition of the extracellular matrix of muscles.

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Reduced Antigenicity of Type I Collagen and Proteoglycans in Sclerotic Dentin

Journal of Dental Research ◽

10.1177/154405910608500204 ◽

2006 ◽

Vol 85 (2) ◽

pp. 133-137 ◽

Cited By ~ 25

Author(s):

P. Suppa ◽

A. Ruggeri ◽

F.R. Tay ◽

C. Prati ◽

M. Biasotto ◽

...

Keyword(s):

High Resolution ◽

Type I Collagen ◽

Organic Matrix ◽

Collagen Fibrils ◽

Type I ◽

Secondary Antibodies ◽

Caries Lesions ◽

Carious Teeth ◽

Double Immunolabeling

Antigenic alterations to the dentin organic matrix may be detected by an immunohistochemical approach. We hypothesized that alterations in the antigenicity of type I collagen and proteoglycans occur in sclerotic dentin under caries lesions. Transverse sections were prepared from carious teeth in the sclerotic zone and normal hard dentin. A double-immunolabeling technique was performed on these sections, with anti-type I collagen and anti-chondroitin 4/6 sulfate monoclonal primary antibodies. We used gold-conjugated secondary antibodies to visualize the distribution of intact collagen fibrils and proteoglycans by high-resolution SEM. For sclerotic dentin, labeling densities were 19.57 ± 3.01/μm2 for collagen and 9.84 ± 2.62/μm2 for proteoglycans. For normal hard dentin, values were 35.20 ± 2.73/μm2 and 17.03 ± 1.98/μm2, respectively. Distribution of intact collagen fibrils and proteoglycans in sclerotic dentin was significantly lower than in normal hard dentin. Reductions in antigenicity from the organic matrix of sclerotic dentin under caries lesions raise concern about the potential of intrafibrillar remineralization.

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Isolation and characterisation of collagen from elk antler velvet

Animal Production Science ◽

10.1071/an13281 ◽

2014 ◽

Vol 54 (8) ◽

pp. 1095

Author(s):

Do Hun Lee ◽

Heeok Hong ◽

Gaurav Lodhi ◽

Sun Hee Cheong ◽

Pyo Jam Park ◽

...

Keyword(s):

Cervus Elaphus ◽

Acid Content ◽

High Performance ◽

Type I Collagen ◽

Peptide Mapping ◽

Total Yield ◽

Type I ◽

Soluble Collagen ◽

Electrophoretic Patterns ◽

Imino Acid

Collagen was extracted from the antler velvet of elk (Cervus elaphus). Two types of collagen were prepared namely, acetic acid-soluble collagen and pepsin-soluble collagen. The electrophoretic patterns of both of the collagens showed that they were heterotrimeric, i.e. they consisted of α1α2α3. The total yield of the collagen obtained from the elk antler velvet was 12.1%. Amino acid analysis of the collagen by high-performance liquid chromatography showed that imino acid content such as that of proline and hydroxyproline was high, which might contribute to better visco-elastic properties. The peptide mapping of the collagens showed their similarity with porcine Type I collagen, thereby suggesting that the primary structure of both collagens is identical to that of porcine skin Type I collagen. The thermal denaturation temperature was 37°C, which is comparable to porcine Type I collagen and may also be as a result of high imino acid content.

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AFM Imaging of Water, Cells and Tissues

MRS Proceedings ◽

10.1557/proc-874-l4.1 ◽

2005 ◽

Vol 874 ◽

Author(s):

Xiaodong Li

Keyword(s):

Type I Collagen ◽

Calibration Method ◽

Phase Imaging ◽

Type I ◽

Contact Mode ◽

Tapping Mode ◽

Afm Imaging ◽

The Difference ◽

Afm Cantilever ◽

Pit Cell

AbstractThis paper presents the results of several AFM case studies of water, tumor cells, pit cells, and type-I collagen samples. The AFM imaging procedures, surface structural characterization capabilities such as contact mode, tapping mode, and friction mode are discussed. The difference in surface morphology between the pit cell submerged in liquid and the cell in air was observed. The AFM tapping mode phase imaging technique was used to study the crosslinks in the type-I collagen. The calibration method for accurately measuring the AFM cantilever spring constant with the help of a nanoindenter is also presented.

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Antioxidant and Anti-Inflammatory Properties of Anthocyanins Extracted from Oryza sativa L. in Primary Dermal Fibroblasts

Oxidative Medicine and Cellular Longevity ◽

10.1155/2019/2089817 ◽

2019 ◽

Vol 2019 ◽

pp. 1-18 ◽

Cited By ~ 5

Author(s):

Pakhawadee Palungwachira ◽

Salunya Tancharoen ◽

Chareerut Phruksaniyom ◽

Sirinapha Klungsaeng ◽

Ratchaporn Srichan ◽

...

Keyword(s):

Wound Healing ◽

Oryza Sativa ◽

Group Treatment ◽

High Performance ◽

Type I Collagen ◽

Oryza Sativa L ◽

Antioxidant Properties ◽

Dermal Fibroblasts ◽

Type I ◽

Anti Inflammatory

Flavonoids are naturally active substances that form a large class of phenolic compounds abundant in certain foods. Black rice (Oryza sativa L.) contains high levels of anthocyanin polyphenols, which have beneficial effects on health owing to their antioxidant properties. The breakdown of collagenous networks with aging or skin deterioration results in the impairment of wound healing in the skin. Accordingly, reviving stagnant collagen synthesis can help maintain dermal homeostasis during wound healing. This study presents an assessment of the cellular activity of anthocyanins (ANT) extracted from Oryza sativa L., providing information necessary for the development of new products that support natural healing processes. The relative composition of ANT from Oryza sativa L. was determined by high-performance liquid chromatography/diode array detection. ANT promoted the migration of rat dermal fibroblasts (RDFs) and demonstrated antioxidant properties. ANT increased the mRNA expression of collagen type I alpha 2 (COL1A2) and upregulated type I collagen protein levels in H2O2-stimulated RDFs without cytotoxicity. Compared with the untreated group, treatment of RDFs with ANT in the presence of H2O2 led to the activation of signaling pathways, including the extracellular signal-regulated protein kinases 1 and 2 (ERK1/2) and Akt, whereas it significantly (p<0.001) inhibited the phosphorylation of IκBα and suppressed the activation of the nuclear factor-kappa B (NF-κB) subunits, p50 and p65, which are transcription factors responsible for inflammation. Taken together, our findings suggest that ANT from Oryza sativa L. have anti-inflammatory properties and antiaging potential by modulating type I collagen gene expression and suppressing H2O2-induced NF-κB activation in skin fibroblasts.

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A Multicenter Study to Evaluate Harmonization of Assays for C-Terminal Telopeptides of Type I Collagen (ß-CTX): A Report from the IFCC-IOF Committee for Bone Metabolism (C-BM)

Calcified Tissue International ◽

10.1007/s00223-021-00816-5 ◽

2021 ◽

Author(s):

E. Cavalier ◽

◽

R. Eastell ◽

N. R. Jørgensen ◽

K. Makris ◽

...

Keyword(s):

Multicenter Study ◽

Evaluation Method ◽

Type I Collagen ◽

Clinical Laboratory ◽

Type I ◽

Regression Equations ◽

Long Term Storage ◽

Comparison Results ◽

The Difference ◽

Routine Clinical Laboratory

Abstract Background Biochemical bone turnover markers are useful tools to assess bone remodeling. C-terminal telopeptide of type I collagen (ß-CTX) has been recommended as a reference marker for bone resorption in research studies. Methods We describe the results of a multicenter study for routine clinical laboratory assays for ß-CTX in serum and plasma. Four centers (Athens GR, Copenhagen DK, Liege BE and Sheffield UK) collected serum and plasma (EDTA) samples from 796 patients presenting to osteoporosis clinics. Specimens were analyzed in duplicate with each of the available routine clinical laboratory methods according to the manufacturers’ instructions. Passing-Bablok regressions, Bland–Altman plots, V-shape evaluation method, and Concordance correlation coefficient for ß-CTX values between serum and plasma specimens and between methods were used to determine the agreement between results. A generalized linear model was employed to identify possible variables that affected the relationship between the methods. Two pools of serum were finally prepared and sent to the four centers to be measured in 5-plicates on 5 consecutive days with the different methods. Results We identified significant variations between methods and between centers although comparison results were generally more consistent in plasma compared to serum. We developed univariate linear regression equations to predict Roche Elecsys®, IDS-iSYS, or IDS ELISA ß-CTX results from any other assay and a multivariable model including the site of analysis, the age, and weight of the patient. The coefficients of determination (R2) increased from approximately 0.80 in the univariate model to approximately 0.90 in the multivariable one, with the site of analysis being the major contributing factor. Results observed on the pools also suggest that long-term storage could explain the difference observed with the different methods on serum. Conclusion Our results show large within- and between-assay variation for ß-CTX measurement, particularly in serum. Stability of the analyte could be one of the explanations. More studies should be undertaken to overcome this problem. Until harmonization is achieved, we recommend measuring ß-CTX by the same assay on EDTA plasma, especially for research purposes in large pharmacological trials where samples can be stored for long periods before they are assayed.

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Effects of Type I Collagen Degradation on the Durability of Three Adhesive Systems in the Early Phase of Dentin Bonding

PLoS ONE ◽

10.1371/journal.pone.0116790 ◽

2015 ◽

Vol 10 (2) ◽

pp. e0116790 ◽

Cited By ~ 5

Author(s):

Lin Hu ◽

Yu-hong Xiao ◽

Ming Fang ◽

Yu Gao ◽

Li Huang ◽

...

Keyword(s):

Early Phase ◽

Type I Collagen ◽

Collagen Degradation ◽

Type I ◽

Adhesive Systems ◽

Dentin Bonding

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Collagen fibrillogenesis in vitro: interaction of types I and V collagen

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100142670 ◽

1986 ◽

Vol 44 ◽

pp. 210-211

Author(s):

Arthur J. Wasserman ◽

Kathy C. Kloos ◽

David E. Birk

Keyword(s):

Type I Collagen ◽

Corneal Stroma ◽

Minor Component ◽

Homogeneous Distribution ◽

Type I ◽

Type V Collagen ◽

Fibril Morphology ◽

Type V ◽

In Vitro Interaction

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.

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Total etch dentin bonding systems: scanning electron microscopy of the resin-dentin hybrid layer

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100130092 ◽

1992 ◽

Vol 50 (2) ◽

pp. 1092-1093

Author(s):

Jorge Perdigao

Keyword(s):

Composite Resin ◽

Mechanical Interlocking ◽

Hybrid Layer ◽

Agent Based ◽

Dentin Bonding ◽

Acid Agent ◽

Bond Strengths ◽

Main Component ◽

Bonding Systems ◽

New Generation

In 1955, Buonocore introduced the etching of enamel with phosphoric acid. Bonding to enamel was created by mechanical interlocking of resin tags with enamel prisms. Enamel is an inert tissue whose main component is hydroxyapatite (98% by weight). Conversely, dentin is a wet living tissue crossed by tubules containing cellular extensions of the dental pulp. Dentin consists of 18% of organic material, primarily collagen. Several generations of dentin bonding systems (DBS) have been studied in the last 20 years. The dentin bond strengths associated with these DBS have been constantly lower than the enamel bond strengths. Recently, a new generation of DBS has been described. They are applied in three steps: an acid agent on enamel and dentin (total etch technique), two mixed primers and a bonding agent based on a methacrylate resin. They are supposed to bond composite resin to wet dentin through dentin organic component, forming a peculiar blended structure that is part tooth and part resin: the hybrid layer.

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