Dataset Information

Investigations of Processing-Induced Structural Changes in Horse Type-I Collagen at Sub and Supramolecular Levels.

ABSTRACT: The aim of this work is to evaluate the effects of different extraction and material processing protocols on the collagen structure and hierarchical organization of equine tendons. Wide and Small Angle X-ray Scattering investigations on raw powders and thin films revealed that not only the extraction and purification treatments, but also the processing conditions may affect the extent of the protein crystalline domain and induce a nanoscale "shield effect." This is due to the supramolecular fiber organization, which protects the atomic scale structure from the modifications that occur during fabrication protocols. Moreover, X-ray analyses and Fourier Transform Infrared spectroscopy performed on the biomaterial sheds light on the relationship between processing conditions, triple helical content and the organization in atomic and nanoscale domains. It was found that the mechanical homogenization of the slurry in acidic solution is a treatment that ensures a high content of super-organization of collagen into triple helices and a lower crystalline domain in the material. Finally, mechanical tensile tests were carried out, proving that the acidic solution is the condition which most enhances both mechanical stiffness and supramolecular fiber organization of the films.

SUBMITTER: Terzi A

PROVIDER: S-EPMC6736615 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

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Investigations of Processing-Induced Structural Changes in Horse Type-I Collagen at Sub and Supramolecular Levels.

Terzi Alberta A Gallo Nunzia N Bettini Simona S Sibillano Teresa T Altamura Davide D Campa Lorena L Natali Maria Lucia ML Salvatore Luca L Madaghiele Marta M De Caro Liberato L Valli Ludovico L Sannino Alessandro A Giannini Cinzia C

Frontiers in bioengineering and biotechnology 20190826

The aim of this work is to evaluate the effects of different extraction and material processing protocols on the collagen structure and hierarchical organization of equine tendons. Wide and Small Angle X-ray Scattering investigations on raw powders and thin films revealed that not only the extraction and purification treatments, but also the processing conditions may affect the extent of the protein crystalline domain and induce a nanoscale "shield effect." This is due to the supramolecular fibe ...[more]

PMID: 31552231

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Project description:Invasive growth of epithelial cancers is a complex multi-step process which involves dissolution of the basement membrane. Type IV collagen is a major component in most basement membranes. Type VII collagen is related to anchoring fibrils and is found primarily in the basement membrane zone of stratified epithelia. Immunohistochemical studies have previously reported changes in steady-state levels of different alpha(IV) chains in several epithelial cancer types. In the present study we aimed to quantitatively determine the mRNA levels of type IV collagen (alpha1/alpha 4/alpha 6) and type VII collagen (alpha1) during colorectal cancer carcinogenesis.Using quantitative RT-PCR, we have determined the mRNA levels for alpha1(IV), alpha 4(IV), alpha 6(IV), and alpha1(VII) in colorectal cancer tissue (n = 33), adenomas (n = 29) and in normal tissue from the same individuals. In addition, corresponding tissue was examined from healthy volunteers (n = 20). mRNA levels were normalized to beta-actin. Immunohistochemical analysis of the distributions of type IV and type VII collagens were performed on normal and affected tissues from colorectal cancer patients.The alpha1(IV) and alpha1(VII) mRNA levels were statistically significantly higher in colorectal cancer tissue (p < 0.001) as compared to corresponding tissue from healthy controls. This is an early event as tissue from adenomas also displayed a higher level. There were small changes in the levels of alpha 4(IV). The level of alpha 6(IV) was 5-fold lower in colorectal cancer tissue as compared to healthy individuals (p < 0.01). The localisation of type IV and type VII collagen was visualized by immunohistochemical staining.Our results suggest that the down-regulation of alpha 6(IV) mRNA coincides with the acquisition of invasive growth properties, whereas alpha1(IV) and alpha1(VII) mRNAs were up-regulated already in dysplastic tissue. There are no differences in collagen expression between tissues from healthy individuals and normal tissues from affected individuals.

Dataset Information

Investigations of Processing-Induced Structural Changes in Horse Type-I Collagen at Sub and Supramolecular Levels.

Publications

Investigations of Processing-Induced Structural Changes in Horse Type-I Collagen at Sub and Supramolecular Levels.

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