Marine Collagen Substrates for 2D and 3D Ovarian Cancer Cell Systems.

Francesca Paradiso,R Steven Conlan,Frank Barry,Francesca Taraballi,Joan Fitzgerald,Deyarina Gonzalez,Lewis Francis,Seydou Yao

doi:10.3389/fbioe.2019.00343

Abstract

A fundamental structural component of extracellular matrix in all connective and interstitial tissue, collagen is the most abundant protein in the human body. To date, mammalian collagens sources represent the golden standard for multiple biomedical applications, while marine-derived collagens have largely been used in industry (food, pharmaceutical, and cosmetic), with little use in research and clinical applications. Herein we demonstrate the effective use Rhizostoma pulmo jellyfish collagen, a source of biocompatible, sustainable collagen for 2D and 3D cell culture, addressing the global drive for technological developments that result in the replacement of animals and their derived products in research. Jellyfish collagen harbors similar structural features mammalian collagen type I, despite differing slightly in amino acid content. Jellyfish collagen supports ovarian cancer (OvCa) cell line proliferation, cellular morphology and expression of epithelial to mesenchymal transition markers, supporting the use of R. pulmo as a non-mammalian collagen cell culture substrate. Furthermore, R. pulmo collagen is effective in 3D device fabrication such as sponges where it mimics tissue architecture complexity. OvCa cells migrated and differentiated within the R. pulmo collagen 3D scaffolds confirming its suitability for advanced cell culturing applications, providing an excellent alternative to mammalian collagen sources for the culture of human cells.

Highlights

Collagens represent 30% of total protein mass in mammals, providing a fundamental structural component of extracellular matrix (ECM) in all connective and interstitial tissue (Gelse et al, 2003)
The basic structure of collagen type I is composed of three polypeptide α-chains, termed the coil, which are wound around each other
Mammalian integrin collagen receptor motifs found in collagens, such as GPO (GlycineProline-Hydroxyproline) (Heino, 2007) and RGD (ArginineGlycine-Aspartic acid), have been suggested as a mechanism by which mammalian cells anchor to collagens in mammals and other vertebrates (Leitinger, 2011)

Summary

Introduction

Collagens represent 30% of total protein mass in mammals, providing a fundamental structural component of extracellular matrix (ECM) in all connective and interstitial tissue (Gelse et al, 2003). The triple helix is composed of three polypeptide α chains, composed of the peptide triplet repeat Gly-X-Y (X = proline, Y = hydroxyproline), conserved structural features which are crucial in mediating the spectrum of collagen functions (Gelse et al, 2003). Marine Collagen for Cell Culture mammals skin, porcine/bovine/ovine tendon tissue and rat tail, while bovine, porcine and chicken cartilage tissues provide a good source for collagen type II. The ability of these collagen sources to be fabricated into varying scaffold forms such as hydrogels, sponges, fibers, films, and hollow spheres provide tools for mimicking complex biological and mechanical features of native tissue (Sorushanova et al, 2019). Bioinspired collagen-based in vitro culture methods provide a base for ECM substitutes in pathologic models for drug screening (Sorushanova et al, 2019)

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