Applications of Marine Biochemical Pathways to Develop Bioactive and Functional Products
Se-Kwon Kim in Marine Biochemistry, 2023
Collagen is a common fibrous protein found in all connective tissues (i.e., skin, bones, ligaments, tendons, and cartilage). The most abundant, cost-effective, and eco-friendly source of the bioactive compound is available as marine collagen obtained through marine waste streams (Cheung & Li-Chan, 2016; Suleria et al., 2015). Seafood processing by-products contain a rich content of functional molecules, such as proteins, bioactive peptides, collagen, polyunsaturated fatty acids, chitin, and fat-soluble vitamins (Lucarini et al., 2020). Collagen is characterized by a triple-helix structure made by three crosslinked alpha-amino acid chains, consisting of two homologous α1-chains and one α2-chain (Lionetto & Esposito Corcione, 2021). Gelatin is a protein derived from the partial hydrolysis of native collagen followed by thermal treatment. Further enzymatic hydrolysis can be used to extract collagen peptides from gelatin (Lionetto & Esposito Corcione, 2021).
Dentin-Pulp Complex Regeneration
Vincenzo Guarino, Marco Antonio Alvarez-Pérez in Current Advances in Oral and Craniofacial Tissue Engineering, 2020
Collagen is a major protein that can be found in sinew, cartilage, bone and skin. One of the most important advantages of collagen is that it can be processed into a variety of set-ups, as porous sponges, gels and sheets, and can also be crosslinked with chemicals to make it stronger or to alter its degradation rate (Nasir et al. 2006). Collagen sponges have demonstrated to be similar to the structure of an extracellular matrix, they have low immunogenicity and cytotoxicity, and also, the ability of forming several shapes and stimulating the differentiation of osteoblasts (Silver and Pins 1991; Chevallay et al. 2000). Collagen sponge scaffolds and gels have been reported for tooth regeneration; results suggest that not only does collagen retain and support cell proliferation and differentiation, but also help in the production of calcified tissues (Sumita et al. 2006). Seeding Dental Pulp Stem Cells (DPSC) on a collagen scaffold, the collagen scaffold could stimulate a systematized comparable matrix formation similar to that of pulp tissue (Prescott et al. 2008). Collagen scaffold allows easy placement of cells and growth factors. It also allows for substitution by natural tissues after suffering degradation (Sumita et al. 2006; Yamauchi et al. 2011). However, the results are not always consistent; consequently, the characteristics of collagen scaffolds and gels require further investigation before being applied in human trials.
Natural Products and Stem Cells and Their Commercial Aspects in Cosmetics
Heather A.E. Benson, Michael S. Roberts, Vânia Rodrigues Leite-Silva, Kenneth A. Walters in Cosmetic Formulation, 2019
Proteins have been used for cosmetic purposes since ancient times. One such protein, collagen, is found in all multicellular organisms and is the main protein found in skin. Collagen is also present in connective tissues, tendons and bones. With skin aging, the molecular structure of collagen is modified and causes skin to look wrinkled and dry and have reduced elasticity. Several types of collagen are marketed that are extracted from animal waste produced after preparing animals for dietary consumption. Soluble collagen, also known as native collagen, is generally the type used in skin and hair care products. This collagen can be hydrolyzed with free amino acids, resulting in no residue on skin and hair. Collagen is known for its moisturizing properties and can be used in creams to increase the skin penetration of formulation ingredients. However, there is some controversy over the effectiveness of collagen for use in hair products. Collagen can also be hydrolyzed and denatured to obtain gelatin. Elastin is a protein that is often found in the body together with collagen and, as the name implies, elastin contributes to the skin’s elasticity. This protein is used in creams, lotions, shampoos and conditioners, face masks, and other cosmetic formulations. Non-animal–derived options are available for collagen and elastin, including plant and synthetic sources (Corbeil et al., 2000).
Efficacy of endoscopic porcine small intestinal submucosa graft myringoplasty: a retrospective comparative study
Published in Acta Oto-Laryngologica, 2023
Li Jin, Xueying Pan, Tuanfang Yin, Jihao Ren, Wei Liu
The results of the present study demonstrated the success and safety of PSISG for myringoplasty in the repair of TM perforations. The closure rates were 85.2% (23/27), 92.1% (35/38) and 87.9% (29/33) in the PSISG, TF and PC groups respectively, and no significant statistical difference in the closure rates among the three groups (p = .667). A stable TM closure was observed 3 months after the endoscopic PSISG myringoplasty (Figure 2). PSISG is a new graft material derived from porcine acellular small intestine submucosa, which was successfully and safely used as a tissue reinforcement material in several different surgical procedures [15,16]. PSISG is removed all kinds of cells and antigens contained in the tissue, and retained the collagen-rich of 3D fiber framework. The collagen can be used for host cell proliferation, tissue remodeling and vascular regeneration, supporting and strengthening tissue repair [8]. Additionally, it includes fibronectin, glycosaminoglycans, hyaluronate, heparin, chondroitin sulfate, and growth factors [8,17,18], which contribute to the repair and healing of the host tissues. PSISG has been successfully demonstrated effective in the repair of chronic TM perforations in an animal model [6]. Additionally, a randomized controlled study found PSISG was a safe and effective material for TM closure in children via the post-auricular approach [8]. Our study showed that PSISG also an effective graft for endoscopic myringoplasty in adult.
Effects of 8 Weeks of Shilajit Supplementation on Serum Pro-c1α1, a Biomarker of Type 1 Collagen Synthesis: A Randomized Control Trial
Published in Journal of Dietary Supplements, 2022
Tyler J. Neltner, Prakash K. Sahoo, Robert W. Smith, John Paul V. Anders, Jocelyn E. Arnett, Richard J. Schmidt, Glen O. Johnson, Sathish Kumar Natarajan, Terry J. Housh
Collagens are prominent structural proteins in the extracellular matrix of the skin, eyes, bones, ligaments, tendons, and muscles, and accounts for approximately one-third of all protein in the human body (Henriksen and Karsdal 2016; Khatri et al. 2021). Type I collagen is the most abundant collagen subtype in soft tissues and bones (Henriksen and Karsdal 2016; Holm Nielsen et al. 2021) and comprises up to 70% of collagen in the skin, 65-80% of the dry weight of tendons, 95% of bone collagen, and 80% of total bone proteins (Das et al. 2016; Khatri et al. 2021). Type I collagen supports skin structure and firmness, which are factors associated with wrinkles (Proksch et al. 2014), contributes to the tensile strength of the cornea and sclera of the eyes (Ihanamäki et al. 2004), and affects the formation and mechanical properties of bone, such as toughness (Viguet-Carrin et al. 2006; Henriksen and Karsdal 2016). In addition, type 1 collagen enhances cell proliferation and remodeling of the extracellular matrix during tissue repair of ligaments (Martinez et al. 2007; Das et al. 2016), is involved in the transfer of force via the endomysium, perimysium, and epimysium during a muscle contraction, and aids in the prevention of exercise-induced injuries (Lis and Baar 2019).
Functional Characterization of Undenatured Type II Collagen Supplements: Are They Interchangeable?
Published in Journal of Dietary Supplements, 2022
Robert B. Harris, Fernando L. A Fonseca, Matthew H. Sharp, Charlie R. Ottinger
Hydrolyzed collagen or denatured collagen is collagen that has been broken into its peptide components by means of enzymes, heat, or pH (Woo et al. 2017). In contrast, undenatured collagen type II retains its native triple helix conformation. The molecular weight for undenatured collagen is approximately 300 kDa whereas that for collagen hydrolysates ranges from 2 to 9 kDa (Prabhoo and Billa 2018). Not only are the structures different, the two forms are thought to have different modes of action. Hydrolyzed collagen, which is more easily absorbed due to its lower molecular weight, is thought to aid in cartilage regeneration by providing material for the synthesis of collagen in situ (García-Coronado et al. 2019). In contrast, preclinical studies suggest that undenatured collagen influences the humoral and cellular immune response via interactions with gut-associated lymphoid tissues (GALT) in a process known as oral tolerance (Bagchi et al. 2002). Given the differences in physical characteristics, dosage, and mode of action, it seems inappropriate that studies on hydrolyzed collagen and undenatured collagen would be combined in the same meta-analysis (García-Coronado et al. 2019).