scholarly journals Fiber Metabolism, Procollagen and Collagen Type III Immunoreactivity in Broiler Pectoralis Major Affected by Muscle Abnormalities

Animals ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 1081 ◽  
Author(s):  
Maurizio Mazzoni ◽  
Francesca Soglia ◽  
Massimiliano Petracci ◽  
Federico Sirri ◽  
Giulia Lattanzio ◽  
...  
Keyword(s):  
Positive Reaction ◽  
Collagen Type ◽  
Pectoralis Major Muscle ◽  
Live Weight ◽  
Pectoralis Major ◽  
Collagen Type Iii ◽  
Cross Sectional ◽  
Type Iii ◽  
Glycerophosphate Dehydrogenase ◽  
Wooden Breast

The present study aimed to evaluate the muscle fiber metabolism and assess the presence and distribution of both procollagen and collagen type III in pectoralis major muscles affected by white striping (WS), wooden breast (WB), and spaghetti meat (SM), as well as in those with macroscopically normal appearance (NORM). For this purpose, 20 pectoralis major muscles (five per group) were selected from the same flock of fast-growing broilers (Ross 308, males, 45-days-old, 3.0 kg live weight) and were used for histochemical (nicotinamide adenine dinucleotide tetrazolium reductase (NADH-TR) and alpha-glycerophosphate dehydrogenase (α-GPD)) and immunohistochemical (procollagen and collagen type III) analyses. When compared to NORM, we found an increased proportion (p < 0.001) of fibers positively stained to NADH-TR in myopathic muscles along with a relevant decrease (p < 0.001) in the percentage of those exhibiting a positive reaction to α-GPD. In addition, an increased proportion of fibers exhibiting a positive reaction to both stainings was observed in SM, in comparison with NORM (14.3 vs. 7.2%; p < 0.001). After reacting to NADH-TR, SM exhibited the lowest (p < 0.001) cross-sectional area (CSA) of the fibers (−12% with respect to NORM). On the other hand, after reacting to α-GPD, the CSA of WS was found to be significantly larger (+10%) in comparison with NORM (7480 vs. 6776 µm2; p < 0.05). A profound modification of the connective tissue architecture involving a different presence and distribution of procollagen and collagen type III was observed. Intriguingly, an altered metabolism and differences in the presence and distribution of procollagen and collagen type III were even observed in pectoralis major muscle classified as NORM.

Serum Insulin-Like Growth Factor-I and Pro-Collagen Type III N-Terminal Peptide in Adolescent Elite Athletes: Implications for the Detection of Growth Hormone Abuse in Sport

2010 ◽  
Vol 95 (6) ◽  
pp. 2969-2976 ◽  
Author(s):  
Nishan Guha ◽  
Ioulietta Erotokritou-Mulligan ◽  
Caroline Burford ◽  
Gail Strobridge ◽  
Joanna Brigg ◽  
...  
Keyword(s):  
Collagen Type ◽  
Elite Athletes ◽  
Serum Insulin ◽  
Collagen Type Iii ◽  
Adolescent Athletes ◽  
Cross Sectional ◽  
Type Iii ◽  
Factor I ◽  
Igf I ◽  
Positive Results

Abstract Context: A method based on two GH-dependent markers, IGF-I and pro-collagen type III N-terminal peptide (P-III-P), has been devised to detect exogenously administered GH. Because previous studies on the detection of GH abuse involved predominantly adult athletes, the method must be validated in adolescent athletes. Objective: The aim of the study was to examine serum IGF-I and P-III-P concentrations in elite adolescent athletes and to determine whether the method developed in adults is appropriate to detect GH abuse in this population. Design and Setting: We conducted a cross-sectional observational study at national sporting organization training events. Subjects: A total of 157 (85 males, 72 females) elite athletes between 12 and 20 yr of age participated in the study. Intervention: Serum IGF-I and P-III-P were each measured by two commercially available immunoassays. GH-2000 discriminant function scores were calculated. Results: Both IGF-I and P-III-P rose to a peak during adolescence, which was earlier in girls than in boys. All GH-2000 scores lay below the proposed cutoff limit of 3.7 (although some scores were close to this value), indicating that none of these athletes would be accused of GH doping if the GH-2000 discriminant formulae were used. The results between the two immunoassays for IGF-I and P-III-P were closely aligned. Conclusions: The GH-2000 score rises in early adolescence, reaches a peak in athletes aged 13–16 yr, and then falls. We have found no evidence that the proposed GH-2000 score developed in adults would lead to an unacceptable rate of false-positive results in adolescent athletes, but caution may be required around the time of peak growth velocity.

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.

Alpha 1 Integrin and Collagen Type III in C2C12 Cell Lines

2000 ◽  
Vol 6 (S2) ◽  
pp. 962-963
Author(s):  
C. DiLullo ◽  
J. Malsbury ◽  
P. M. Mattioli
Keyword(s):  
Cell Line ◽  
Cell Lines ◽  
Muscle Development ◽  
Collagen Type ◽  
C2c12 Cell ◽  
C2c12 Cells ◽  
Collagen Type Iii ◽  
Skeletal Myocytes ◽  
Type Iii ◽  
Specific Proteins

In nascent cultured primary chick skeletal myocytes, a l integrin is observed to have a punctate distribution. As early as day 3 in culture, however, it can be found to reorganize into periodic doublet bands. Subsequent to a l integrin reorganization, collagen type III has been found to colocalize with these periodic α l integrin bands. The coordinated appearance of these two proteins is suggestive of a possible regulatory role for one or both proteins in muscle development.To ascertain whether this same αl integrin/collagen type III reorganization occurs in muscle cell lines, differentiating myocytes from the C2C12 cell line were examined for the temporal appearance and localization of both proteins. Cultured C2C12 cells were immunofluorescently labeled with antibodies to al integrin, collagen type III and other muscle specific proteins on days 1, 3, 6, 9 and 11 after growth medium was replaced with differentiation medium.

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