Dissolving microneedle-encapsulated drug-loaded nanoparticles and recombinant humanized collagen type III for the treatment of chronic wound via anti-inflammation and enhanced cell proliferation and angiogenesis

Nanoscale ◽  
2022 ◽  
Author(s):  
Lin-yu Long ◽  
Wenqi Liu ◽  
Li Li ◽  
Cheng Hu ◽  
Shuyi He ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Hyaluronic Acid ◽  
Glycolic Acid ◽  
Chronic Wounds ◽  
Collagen Type ◽  
Chronic Wound ◽  
Plga Nanoparticles ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Anti Inflammation

The first recombinant humanized collagen type III (rhCol III) and naproxen (Nap) loaded poly(lactic-co-glycolic acid) (PLGA) nanoparticles incorporated hyaluronic acid (HA) microneedle (MN) was fabricated for diabetic chronic wounds therapy.

scholarly journals Data mining-based study of collagen type III alpha 1 (COL3A1) prognostic value and immune exploration in pan-cancer

Bioengineered ◽  
2021 ◽  
Vol 12 (1) ◽  
pp. 3634-3646
Author(s):  
Hanyu Zhang ◽  
Cheng Ding ◽  
Yatong Li ◽  
Cheng Xing ◽  
Shunda Wang ◽  
...  
Keyword(s):  
Data Mining ◽  
Prognostic Value ◽  
Collagen Type ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Pan Cancer

scholarly journals Prognostic value of blood-based fibrosis biomarkers in patients with metastatic colorectal cancer receiving chemotherapy and bevacizumab

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Neel I. Nissen ◽  
Stephanie Kehlet ◽  
Mogens K. Boisen ◽  
Maria Liljefors ◽  
Christina Jensen ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Metastatic Colorectal Cancer ◽  
Collagen Type ◽  
Performance Status ◽  
Drug Uptake ◽  
Collagen Type Iii ◽  
Serum Samples ◽  
Type Iii ◽  
Poor Treatment ◽  
And Performance

AbstractA desmoplastic colorectal cancer stroma, characterized by excess turnover of the cancer-associated fibroblast derived collagens type III and VI, can lead to reduced drug-uptake and poor treatment response. We investigated the association between biomarkers of collagen type III and VI and overall survival (OS) in patients with metastatic colorectal cancer (mCRC). Serum samples were collected from 252 patients with mCRC prior to treatment with bevacizumab and chemotherapy. Serum concentrations of biomarkers reflecting formation of collagen type III (PRO-C3) and VI (PRO-C6) and degradation of collagen type VI (C6M and C6Mα3) were determined by ELISA. The biomarkers were evaluated for associations with OS, individually, combined, and after adjusting for carcinoembryonic antigen (CEA), lactate dehydrogenase (LDH) and performance status (PS). High baseline levels (> median) of each collagen biomarker were significantly associated with shorter OS (PRO-C3: HR = 2.0, 95%CI = 1.54–2.63; PRO-C6: HR = 1.6, 95%CI = 1.24–2.11; C6M: HR = 1.4, 95%CI = 1.05–1.78; C6Mα3: HR = 1.6, 95%CI = 1.16–2.07). PRO-C3 and PRO-C6 remained significant after adjustment for CEA, LDH and PS. Weak correlations were seen between the collagen biomarkers (r = 0.03–0.59) and combining all improved prognostic capacity (HR = 3.6, 95%CI = 2.30–5.76). Collagen biomarkers were predictive of shorter OS in patients with mCRC. This supports that collagen- and CAF biology is important in CRC.

Two Brothers in One Chinese Family With Collagen Type III Glomerulopathy

2007 ◽  
Vol 50 (6) ◽  
pp. 1037-1042 ◽  
Author(s):  
Nan Chen ◽  
Xiaoxia Pan ◽  
Yaowen Xu ◽  
Zhaohui Wang ◽  
Hao Shi ◽  
...  
Keyword(s):  
Collagen Type ◽  
Chinese Family ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Collagen Type Iii Glomerulopathy

Histologic Characterization of Rat Vocal Fold Scarring

2005 ◽  
Vol 114 (3) ◽  
pp. 183-191 ◽  
Author(s):  
Tomoko Tateya ◽  
Jin Ho Sohn ◽  
Ichiro Tateya ◽  
Diane M. Bless
Keyword(s):  
Hyaluronic Acid ◽  
Vocal Fold ◽  
Type I Collagen ◽  
Collagen Type ◽  
Control Level ◽  
Vocal Folds ◽  
Collagen Type I ◽  
Type I ◽  
Type Iii ◽  
Blue Stain

This study aimed to clarify the characteristics of rat vocal fold scarring by examining the alteration of key components in the extracellular matrix: hyaluronic acid, collagen, and fibronectin. Under monitoring with a 1.9-mm-diameter telescope, unilateral vocal fold stripping was performed, and larynges were harvested at 2, 4, 8, and 12 weeks after operation. The vocal folds were histologically analyzed with Alcian blue stain, trichrome stain, and immunofluorescence of collagen type I, collagen type III, and fibronectin. The scarred vocal folds showed less hyaluronic acid and more collagen types I and III than did the controls at all time points. Type III was stable for 12 weeks, while type I declined until 8 weeks and thereafter remained unchanged. Fibronectin increased for 4 weeks and then decreased; it was close to the control level at 8 and 12 weeks. These results suggest that the tissue remodeling process in scarred vocal folds slows down around 2 months after wounding.

scholarly journals Measurement of matrix metalloproteinase 9-mediated Collagen type III degradation fragment as a marker of skin fibrosis

2011 ◽  
Vol 11 (1) ◽  
Author(s):  
Efstathios Vassiliadis ◽  
Sanne Skovgård Veidal ◽  
Natasha Barascuk ◽  
Jhinuk Basu Mullick ◽  
Rikke Elgaard Clausen ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Collagen Type ◽  
Matrix Metalloproteinase 9 ◽  
Skin Fibrosis ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Metalloproteinase 9

scholarly journals Correction: Microenvironment-responsive multifunctional hydrogels with spatiotemporal sequential release of tailored recombinant human collagen type III for the rapid repair of infected chronic diabetic wounds

2022 ◽  
Author(s):  
Cheng Hu ◽  
Wenqi Liu ◽  
Linyu Long ◽  
Zhicun Wang ◽  
Yihui Yuan ◽  
...  
Keyword(s):  
Collagen Type ◽  
Collagen Type Iii ◽  
Rapid Repair ◽  
Type Iii ◽  
Sequential Release ◽  
Human Collagen ◽  
Diabetic Wounds

Correction for ‘Microenvironment-responsive multifunctional hydrogels with spatiotemporal sequential release of tailored recombinant human collagen type III for the rapid repair of infected chronic diabetic wounds’ by Cheng Hu et al., J. Mater. Chem. B, 2021, 9, 9684–9699, DOI: 10.1039/D1TB02170B.

scholarly journals High-Resolution Bioprinting of Recombinant Human Collagen Type III

Polymers ◽  
2021 ◽  
Vol 13 (17) ◽  
pp. 2973
Author(s):  
Rory Gibney ◽  
Jennifer Patterson ◽  
Eleonora Ferraris
Keyword(s):  
Tissue Engineering ◽  
High Resolution ◽  
Collagen Type ◽  
Thin Layers ◽  
Corneal Tissue ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Pure Collagen ◽  
Human Collagen ◽  
Visible Wavelengths

The development of commercial collagen inks for extrusion-based bioprinting has increased the amount of research on pure collagen bioprinting, i.e., collagen inks not mixed with gelatin, alginate, or other more common biomaterial inks. New printing techniques have also improved the resolution achievable with pure collagen bioprinting. However, the resultant collagen constructs still appear too weak to replicate dense collagenous tissues, such as the cornea. This work aims to demonstrate the first reported case of bioprinted recombinant collagen films with suitable optical and mechanical properties for corneal tissue engineering. The printing technology used, aerosol jet® printing (AJP), is a high-resolution printing method normally used to deposit conductive inks for electronic printing. In this work, AJP was employed to deposit recombinant human collagen type III (RHCIII) in overlapping continuous lines of 60 µm to form thin layers. Layers were repeated up to 764 times to result in a construct that was considered a few hundred microns thick when swollen. Samples were subsequently neutralised and crosslinked using EDC:NHS crosslinking. Nanoindentation and absorbance measurements were conducted, and the results show that the AJP-deposited RHCIII samples possess suitable mechanical and optical properties for corneal tissue engineering: an average effective elastic modulus of 506 ± 173 kPa and transparency ≥87% at all visible wavelengths. Circular dichroism showed that there was some loss of helicity of the collagen due to aerosolisation. SDS-PAGE and pepsin digestion were used to show that while some collagen is degraded due to aerosolisation, it remains an inaccessible substrate for pepsin cleavage.

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