Tolerizing DNA vaccines encoding key autoantigens are one of emerging strategies for the treatment of rheumatoid arthritis (RA). Among these vaccines, the most representative is pcDNA-CCOL2A1, an antigen-specific DNA vaccine encoding chicken type Ⅱ collagen (CCⅡ) with significant therapeutic and prophylactic efficacy in collagen-induced arthritis (CIA) rat models. We compared the in situ expression levels of CCOL2A1-mRNA and CCⅡ protein and the protective efficacies against CIA after a single dose (300 μg/kg) of this vaccine via intramuscular (IM), subcutaneous (SC) and intravenous (IV) vaccinations. The IM vaccination routes resulted in good protective efficacies in terms of decreasing CIA incidence and severity and significantly improved radiographic and histopathologic findings and scores of joints.
Furthermore, IM, SC, and IV vaccinations markedly decreased serum levels of anti-type Ⅱ collagen (CⅡ) IgG antibodies, but only IM vaccination significantly reduced serum levels of rheumatoid factor (RF) and anti-cyclic citrullinated peptide (anti-CCP) antibody. The vaccine exhibited a continuous CCOL2A1-mRNA expression in the tail and abdominal subcutaneous tissue injection sites, but no CCOL2A1-mRNA signal was observed in muscle. Strikingly, CCⅡ protein expression levels at the three injection sites were comparable with minimal variation. IM administration may be considered the preferred route for RA treatment in clinical practice.
A Double-Blind, Randomized, Placebo-Controlled Trial to Evaluate the Efficacy of a Hydrolyzed Chicken Collagen Type II Supplement in Alleviating Joint Discomfort
Joint pain and disease affects more than one in four adults in the United States. We conducted a double-blind, randomized, placebo-controlled trial to investigate the efficacy of a hydrolyzed chicken collagen type II (HCII) supplement in reducing joint-related discomfort such as pain and stiffness, and in improving mobility. We enrolled adults aged 40-65 (65.5% were women) who had joint discomfort, but had no co-morbidities, and who were not taking pain medications. The participants were randomized to receive either the HCII supplement (n = 47) or a placebo (n = 43) for eight weeks.
At the baseline, and at week 4 and week 8, we administered the Western Ontario and McMaster Universities Arthritis Index (WOMAC) survey with three additional wrist-related questions and the Visual Analog Scale for assessments of joint-related symptoms. In the WOMAC stiffness and physical activity domains and in the overall WOMAC score, the HCII group had a significant reduction in joint-related discomforts compared with the placebo group. For example, at week 4, the HCII group had a 36.9% reduction in the overall WOMAC score, compared with a 14.3% reduction in the placebo group (p = 0.027). This HCII product is effective in reducing joint pain and stiffness and in improving joint function among otherwise healthy adults.
Characteristics of Reconstituted Collagen Fibers from Chicken Keel Cartilage Depends on Salt Type for Removal of Proteoglycans
- The aim of the presented research was to obtain reconstituted atelocollagen fibers after extraction from poultry cartilage using the pepsin-acidic method in order to remove telopeptides from the tropocollagen. Firstly, we examined the extraction of collagen from the cartilage extracellular matrix (ECM) after proteoglycans (PG) had been removed by the action of salts, i.e., NaCl or chaotropic MgCl2. Additionally, the effects of the salt type used for PG and hyaluronic acid removal on the properties of self-assembled fibers in solutions at pH 7.4 and freeze-dried matrices were investigated.
- The basic features of the obtained fibers were characterized, including thermal properties using scanning calorimetry, rheological properties using dynamic oscillatory rheometry, and the structure by scanning electron microscopy. The fibers obtained after PG removal with both analyzed types of salts had similar thermal denaturation characteristics.
- However, the fibers after PG removal with NaCl, in contrast to those obtained after MgCl2 treatment, showed different rheological properties during gelatinization and smaller diameter size. Moreover, the degree of fibrillogenesis of collagens after NaCl treatment was complete compared to that with MgCl2, which was only partial (70%). The structures of fibers after lyophilization were fundamentally different. The matrices obtained after NaCl pretreatment form regular scaffolds in contrast to the thin, surface structures of the cartilage matrix after proteoglycans removal using MgCl2.
Ultrasound as an alternative method to increase the extraction yield from chicken mecanically separated meatresidue collagen
The residue from chicken mechanically separated meat (MSM) is a potential source for the extraction of collagen. However, this process requires the removal of many covalent crosslinks, which makes it quite complex. Ultrasound has been successfully used to extract collagen; it reduces the process time and increases the yield. However, information regarding the effects of this treatment on the structural and functional properties of proteins is still very limited.
Therefore, the aims of the present study were to obtain collagen from chicken MSM residue and to test the effects of pre-treatment with ultrasonic probe and enzymatic extraction with pepsin in its yield, as well as to evaluate the properties of extracted collagen using gel electrophoresis, Fourier-transform infrared spectroscopy, solubility, and differential scanning calorimetry. Both the ultrasound and the enzymatic extraction had a positive effect on the extraction yield of collagen from chicken MSM residue without affecting its integrity.
Using ultrasound led to an increase of up to 40% in yield when compared to treatments without ultrasound application. Five extraction treatments were considered. The extracted collagen exhibited high thermal stability (43.9-47.0 °C) and mainly type I structure. The use of ultrasound as pre-treatment, together with enzymatic extraction with pepsin, were effective in increasing the extraction yield of collagen from chicken MSM residue, as well as preserving the triple helical structure of the native collagen.
Chicken Collagen I Antibody |
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| GWB-66EC61 | GenWay Biotech | 0.5 ml | Ask for price |
Chicken Collagen I Antibody |
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| GWB-6FE450 | GenWay Biotech | 0.5 ml | Ask for price |
Chicken Collagen III Antibody |
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| GWB-F00D8E | GenWay Biotech | 0.5 ml | Ask for price |
Collagen Type I, chicken |
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| MBS397115-01mL | MyBiosource | 0.1mL | 630 EUR |
Collagen Type I, chicken |
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| MBS397115-5x01mL | MyBiosource | 5x0.1mL | 2680 EUR |
Collagen Type II, chicken |
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| MBS397124-01mL | MyBiosource | 0.1mL | 630 EUR |
Collagen Type II, chicken |
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| MBS397124-5x01mL | MyBiosource | 5x0.1mL | 2680 EUR |
Collagen Type V, chicken |
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| MBS397138-05mL | MyBiosource | 0.5mL | 1080 EUR |
Collagen Type V, chicken |
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| MBS397138-5x05mL | MyBiosource | 5x0.5mL | 4790 EUR |
Collagen Type IX, chicken |
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| MBS397141-05mL | MyBiosource | 0.5mL | 1080 EUR |
Collagen Type IX, chicken |
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| MBS397141-5x05mL | MyBiosource | 5x0.5mL | 4790 EUR |
Native Chicken Collagen Type II |
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| NATE-1165 | Creative BioMart | 1 kg | 263.2 EUR |
Chicken Collagen type I alpha 2,COL1A2/Collagen I ELISA Kit |
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| YLA0139CH-48T | Shanghai YL Biotech | 48T | Ask for price |
Chicken Collagen type I alpha 2,COL1A2/Collagen I ELISA Kit |
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| YLA0139CH-96T | Shanghai YL Biotech | 96T | Ask for price |
Chicken Collagen type I alpha 2, COL1A2/Collagen I ELISA Kit |
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| MBS1601848-10x96StripWells | MyBiosource | 10x96-Strip-Wells | 4470 EUR |
Chicken Collagen type I alpha 2, COL1A2/Collagen I ELISA Kit |
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| MBS1601848-48StripWells | MyBiosource | 48-Strip-Wells | 415 EUR |
Chicken Collagen type I alpha 2, COL1A2/Collagen I ELISA Kit |
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| MBS1601848-5x96StripWells | MyBiosource | 5x96-Strip-Wells | 2270 EUR |
Chicken Collagen type I alpha 2, COL1A2/Collagen I ELISA Kit |
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| MBS1601848-96StripWells | MyBiosource | 96-Strip-Wells | 540 EUR |
Chicken Collagen VI(COL6) ELISA Kit |
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| NSL0931Ch | Sunlong | 1026 T | 528 EUR |
Chicken Collagen VI (COL6) Elisa Kit |
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| MBS261315-10x96StripWells | MyBiosource | 10x96-Strip-Wells | 3545 EUR |
Chicken Collagen VI (COL6) Elisa Kit |
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| MBS261315-48StripWells | MyBiosource | 48-Strip-Wells | 310 EUR |
Chicken Collagen VI (COL6) Elisa Kit |
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| MBS261315-5x96StripWells | MyBiosource | 5x96-Strip-Wells | 1940 EUR |
Chicken Collagen VI (COL6) Elisa Kit |
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| MBS261315-96StripWells | MyBiosource | 96-Strip-Wells | 475 EUR |
Chicken collagen V (COL5) ELISA Kit |
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| MBS2605612-10x96StripWells | MyBiosource | 10x96-Strip-Wells | 3545 EUR |
Chicken collagen V (COL5) ELISA Kit |
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| MBS2605612-48StripWells | MyBiosource | 48-Strip-Wells | 310 EUR |
Chicken collagen V (COL5) ELISA Kit |
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| MBS2605612-5x96StripWells | MyBiosource | 5x96-Strip-Wells | 1940 EUR |
Collagen Hydrolysate Prepared from Chicken By-Product as a Functional Polymer in Cosmetic Formulation
Chicken stomachs can be processed into collagen hydrolysate usable in cosmetic products. The aim of the study was to verify the effects of a carbopol gel formulation enriched with 1.0% (w/w) chicken hydrolysate on the properties of the skin in the periorbital area after regular application twice a day for eight weeks in volunteers ageed 50 ± 9 years. Skin hydration, transepidermal water loss (TEWL), skin elasticity and skin relief were evaluated. Overall, skin hydration increased by 11.82% and 9.45%, TEWL decreased by 25.70% and 17.80% (always reported for the right and left area). Generally, there was an increase in skin elasticity, a decrease in skin roughness, as the resonance times decreased by 85%.
The average reduction of wrinkles was 35.40% on the right and 41.20% on the left. For all results, it can be seen that the longer the cosmetic gel formulation is applied, the better the results. Due to the positive effect on the quality and functionality of the skin, it is possible to apply the cosmetic gel formulation in the periorbital area. The advantage of the product with chicken collagen hydrolysate is also the biocompatibility with the skin and the biodegradability of the formulation.