Different protective efficacies of a novel antigen-specific DNA vaccine encoding chicken type Ⅱ collagen via intramuscular, subcutaneous, and intravenous vaccination against experimental rheumatoid arthritis

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.

Native Chicken Collagen Type II

NATE-1165 Creative Enzymes 1kg 453.6 EUR

Chicken Collagen type I alpha 2,COL1A2/Collagen I ELISA Kit

YLA0139CH-48T Shanghai YL Biotech 48T 540 EUR

Chicken Collagen type I alpha 2,COL1A2/Collagen I ELISA Kit

YLA0139CH-96T Shanghai YL Biotech 96T 645 EUR

Rabbit Anti Chicken Collagen I Polyclonal Antibody

CPBT-67349RC Creative Diagnostics 0.5 ml 1033.2 EUR

Chicken Collagen alpha-1 (XII) chain (COL12A1)

1-CSB-EP005719CH Cusabio
  • 733.20 EUR
  • 370.80 EUR
  • 2192.40 EUR
  • 1126.80 EUR
  • 1461.60 EUR
  • 476.40 EUR
  • 100ug
  • 10ug
  • 1MG
  • 200ug
  • 500ug
  • 50ug

Chicken Collagen alpha-1 (XII) chain (COL12A1)

1-CSB-YP005719CH Cusabio
  • 814.80 EUR
  • 402.00 EUR
  • 2606.40 EUR
  • 1261.20 EUR
  • 1730.40 EUR
  • 522.00 EUR
  • 100ug
  • 10ug
  • 1MG
  • 200ug
  • 500ug
  • 50ug

Chicken Collagen Type VI (COL6) ELISA Kit

abx356088-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Type IV (COL4) ELISA Kit

abx356980-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Type III (COL3) ELISA Kit

abx357046-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Type I Alpha 2 (COL1a2) Protein

20-abx652987 Abbexa
  • 777.60 EUR
  • 326.40 EUR
  • 2397.60 EUR
  • 927.60 EUR
  • 560.40 EUR
  • 100 ug
  • 10 ug
  • 1 mg
  • 200 ug
  • 50 ug

Chicken COL1A1/ Collagen alpha-1(I) chain ELISA Kit

E0015Ch Sunlong 1 Kit 860.4 EUR

Chicken Collagen Alpha-1(XIV) Chain (COL14A1) ELISA Kit

abx355559-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Type VI Alpha 1 (COL6A1) ELISA Kit

abx355575-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Type VIII Alpha 1 (COL8A1) ELISA Kit

abx355580-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Type XIII Alpha 1 (COL13A1) ELISA Kit

abx355680-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Alpha-1(XVII) Chain (COL17A1) ELISA Kit

abx355724-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Alpha-1(VII) Chain (COL7A1) ELISA Kit

abx355737-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Alpha-1(XV) Chain (COL15A1) ELISA Kit

abx355967-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Type V Alpha 2 (COL5A2) ELISA Kit

abx356092-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Type IX Alpha 3 (COL9A3) ELISA Kit

abx356153-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Type VI Alpha 3 (COL6A3) ELISA Kit

abx356536-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Type XI Alpha 1 (COL11A1) ELISA Kit

abx356581-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Type IV Alpha 1 (COL4A1) ELISA Kit

abx356618-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Alpha-1(X) Chain (COL10A1) ELISA Kit

abx356698-96tests Abbexa 96 tests 990 EUR

Chicken Collagen Type III Alpha 1 (COL3A1) ELISA Kit

abx357002-96tests Abbexa 96 tests 904.8 EUR

Chicken Collagen Type I Alpha 1 (COL1A1) ELISA Kit

abx513352-96tests Abbexa 96 tests 1093.2 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.

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