scholarly journals Comparison of the solophenyl-red polarization method and the immunohistochemical analysis for collagen type III

1992 ◽  
Vol 105 (1) ◽  
pp. 27-29 ◽  
Author(s):  
P. Betz ◽  
A. Nerlich ◽  
J. Wilske ◽  
I. Wiest ◽  
R. Penning ◽  
...  
Keyword(s):  
Collagen Type ◽  
Immunohistochemical Analysis ◽  
Collagen Type Iii ◽  
Polarization Method ◽  
Type Iii

scholarly journals The immunohistochemical analysis of fibronectin, collagen type III, laminin, and cytokeratin 5 in putrified skin

1993 ◽  
Vol 61 (1) ◽  
pp. 35-42 ◽  
Author(s):  
P. Betz ◽  
A. Nerlich ◽  
J. Wilske ◽  
J. Tübel ◽  
R. Penning ◽  
...  
Keyword(s):  
Collagen Type ◽  
Immunohistochemical Analysis ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Cytokeratin 5

scholarly journals Targeting Collagen Type III in Proteinuric Kidney Disease: Informing Drug Potential Using the Jaccard–Tanimoto Index

Processes ◽  
2020 ◽  
Vol 8 (8) ◽  
pp. 996
Author(s):  
Michelle Liu ◽  
Anoushka Dalvi ◽  
Sony Dalapati ◽  
Natalia Prakash ◽  
Zhijian Hu ◽  
...  
Keyword(s):  
Kidney Disease ◽  
Collagen Type ◽  
Mrna Level ◽  
Immunohistochemical Analysis ◽  
Fold Increase ◽  
Collagen Type Iii ◽  
Type Iii ◽  
Polarized Microscopy ◽  
Picrosirius Red ◽  
Bowman's Capsule

Collagenofibrotic glomerulopathy, a collagen type III kidney disease, is associated with proteinuria and accumulation ofcollagen type III in the glomerulus specifically the mesangium and/or capillary walls. The puromcyin aminonucleoside (PAN) nephropathy model was evaluated to examine the relation between COL3A1 mRNA and proteinuria. In Wistar rats administered PAN, a robust increase in proteinuria was accompanied by glomerular hypertrophy and expansion of both the Bowman’s capsule and Bowman’s space. An ~4-fold increase in renal COL3A1 mRNA was observed in the PAN cohort with urine protein exhibiting a direct (r = 0.8) and significant correlation with kidney COL3A1 mRNA level. Both Picrosirius red polarized microscopy and immunohistochemical analysis showed localization of collagen type III to the glomerular mesangium. Gene ontology-driven transcriptomic analysis reveals a robust COL3A1 network in the glomerular compartment.

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

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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