Editorial

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5 pages, 214 KiB

Open AccessEditorial

by Ngan F. Huang, Tatiana S. Zaitseva and Michael V. Paukshto

Bioengineering 2023, 10(1), 90; https://doi.org/10.3390/bioengineering10010090 - 10 Jan 2023

Cited by 1 | Viewed by 2012

Extracellular matrix proteins (ECMs) provide structural support and dynamic signaling cues that regulate cell behavior and tissue morphogenesis [...] Full article

(This article belongs to the Special Issue Biomedical Applications of Collagen)

Review

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15 pages, 868 KiB

Open AccessEditor’s ChoiceReview

Collagen in Wound Healing

by Shomita S. Mathew-Steiner, Sashwati Roy and Chandan K. Sen

Bioengineering 2021, 8(5), 63; https://doi.org/10.3390/bioengineering8050063 - 11 May 2021

Cited by 287 | Viewed by 22192

Abstract

Normal wound healing progresses through inflammatory, proliferative and remodeling phases in response to tissue injury. Collagen, a key component of the extracellular matrix, plays critical roles in the regulation of the phases of wound healing either in its native, fibrillar conformation or as [...] Read more.

Normal wound healing progresses through inflammatory, proliferative and remodeling phases in response to tissue injury. Collagen, a key component of the extracellular matrix, plays critical roles in the regulation of the phases of wound healing either in its native, fibrillar conformation or as soluble components in the wound milieu. Impairments in any of these phases stall the wound in a chronic, non-healing state that typically requires some form of intervention to guide the process back to completion. Key factors in the hostile environment of a chronic wound are persistent inflammation, increased destruction of ECM components caused by elevated metalloproteinases and other enzymes and improper activation of soluble mediators of the wound healing process. Collagen, being central in the regulation of several of these processes, has been utilized as an adjunct wound therapy to promote healing. In this work the significance of collagen in different biological processes relevant to wound healing are reviewed and a summary of the current literature on the use of collagen-based products in wound care is provided. Full article

(This article belongs to the Special Issue Biomedical Applications of Collagen)

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16 pages, 1404 KiB

Open AccessEditor’s ChoiceReview

Collagen-Based Electrospun Materials for Tissue Engineering: A Systematic Review

by Britani N. Blackstone, Summer C. Gallentine and Heather M. Powell

Bioengineering 2021, 8(3), 39; https://doi.org/10.3390/bioengineering8030039 - 18 Mar 2021

Cited by 37 | Viewed by 6257

Abstract

Collagen is a key component of the extracellular matrix (ECM) in organs and tissues throughout the body and is used for many tissue engineering applications. Electrospinning of collagen can produce scaffolds in a wide variety of shapes, fiber diameters and porosities to match [...] Read more.

Collagen is a key component of the extracellular matrix (ECM) in organs and tissues throughout the body and is used for many tissue engineering applications. Electrospinning of collagen can produce scaffolds in a wide variety of shapes, fiber diameters and porosities to match that of the native ECM. This systematic review aims to pool data from available manuscripts on electrospun collagen and tissue engineering to provide insight into the connection between source material, solvent, crosslinking method and functional outcomes. D-banding was most often observed in electrospun collagen formed using collagen type I isolated from calfskin, often isolated within the laboratory, with short solution solubilization times. All physical and chemical methods of crosslinking utilized imparted resistance to degradation and increased strength. Cytotoxicity was observed at high concentrations of crosslinking agents and when abbreviated rinsing protocols were utilized. Collagen and collagen-based scaffolds were capable of forming engineered tissues in vitro and in vivo with high similarity to the native structures. Full article

(This article belongs to the Special Issue Biomedical Applications of Collagen)

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19 pages, 1971 KiB

Open AccessReview

Navigating the Collagen Jungle: The Biomedical Potential of Fiber Organization in Cancer

by Jonathan N. Ouellette, Cole R. Drifka, Kelli B. Pointer, Yuming Liu, Tyler J Lieberthal, W John Kao, John S. Kuo, Agnes G. Loeffler and Kevin W. Eliceiri

Bioengineering 2021, 8(2), 17; https://doi.org/10.3390/bioengineering8020017 - 21 Jan 2021

Cited by 37 | Viewed by 7057

Abstract

Recent research has highlighted the importance of key tumor microenvironment features, notably the collagen-rich extracellular matrix (ECM) in characterizing tumor invasion and progression. This led to great interest from both basic researchers and clinicians, including pathologists, to include collagen fiber evaluation as part [...] Read more.

Recent research has highlighted the importance of key tumor microenvironment features, notably the collagen-rich extracellular matrix (ECM) in characterizing tumor invasion and progression. This led to great interest from both basic researchers and clinicians, including pathologists, to include collagen fiber evaluation as part of the investigation of cancer development and progression. Fibrillar collagen is the most abundant in the normal extracellular matrix, and was revealed to be upregulated in many cancers. Recent studies suggested an emerging theme across multiple cancer types in which specific collagen fiber organization patterns differ between benign and malignant tissue and also appear to be associated with disease stage, prognosis, treatment response, and other clinical features. There is great potential for developing image-based collagen fiber biomarkers for clinical applications, but its adoption in standard clinical practice is dependent on further translational and clinical evaluations. Here, we offer a comprehensive review of the current literature of fibrillar collagen structure and organization as a candidate cancer biomarker, and new perspectives on the challenges and next steps for researchers and clinicians seeking to exploit this information in biomedical research and clinical workflows. Full article

(This article belongs to the Special Issue Biomedical Applications of Collagen)

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13 pages, 313 KiB

Open AccessReview

Role of Collagen in Airway Mechanics

by Lumei Liu, Brooke Stephens, Maxwell Bergman, Anne May and Tendy Chiang

Bioengineering 2021, 8(1), 13; https://doi.org/10.3390/bioengineering8010013 - 16 Jan 2021

Cited by 35 | Viewed by 4021

Abstract

Collagen is the most abundant airway extracellular matrix component and is the primary determinant of mechanical airway properties. Abnormal airway collagen deposition is associated with the pathogenesis and progression of airway disease. Thus, understanding how collagen affects healthy airway tissue mechanics is essential. [...] Read more.

Collagen is the most abundant airway extracellular matrix component and is the primary determinant of mechanical airway properties. Abnormal airway collagen deposition is associated with the pathogenesis and progression of airway disease. Thus, understanding how collagen affects healthy airway tissue mechanics is essential. The impact of abnormal collagen deposition and tissue stiffness has been an area of interest in pulmonary diseases such as cystic fibrosis, asthma, and chronic obstructive pulmonary disease. In this review, we discuss (1) the role of collagen in airway mechanics, (2) macro- and micro-scale approaches to quantify airway mechanics, and (3) pathologic changes associated with collagen deposition in airway diseases. These studies provide important insights into the role of collagen in airway mechanics. We summarize their achievements and seek to provide biomechanical clues for targeted therapies and regenerative medicine to treat airway pathology and address airway defects. Full article

(This article belongs to the Special Issue Biomedical Applications of Collagen)

12 pages, 289 KiB

Open AccessReview

The Role of Collagen-Based Biomaterials in Chronic Wound Healing and Sports Medicine Applications

by David A. Yeung and Natalie H. Kelly

Bioengineering 2021, 8(1), 8; https://doi.org/10.3390/bioengineering8010008 - 08 Jan 2021

Cited by 32 | Viewed by 6775

Abstract

Advancements in tissue engineering have taken aim at treating tissue types that have difficulty healing naturally. In order to achieve improved healing conditions, the balance of exogenous matrix, cells, and different factors must be carefully controlled. This review seeks to explore the aspects [...] Read more.

Advancements in tissue engineering have taken aim at treating tissue types that have difficulty healing naturally. In order to achieve improved healing conditions, the balance of exogenous matrix, cells, and different factors must be carefully controlled. This review seeks to explore the aspects of tissue engineering in specific tissue types treated in sports medicine and advanced wound management from the perspective of the matrix component. While the predominant material to be discussed is collagen I, it would be remiss not to mention its relation to the other contributing factors to tissue engineered healing. The main categories of materials summarized here are (1) reconstituted collagen scaffolds, (2) decellularized matrix tissue, and (3) non-decellularized tissue. These three groups are ordered by their increase in additional components beyond simply collagen. Full article

(This article belongs to the Special Issue Biomedical Applications of Collagen)

24 pages, 3948 KiB

Open AccessEditor’s ChoiceReview

Collagen Mimetic Peptides

by Yujia Xu and Michele Kirchner

Bioengineering 2021, 8(1), 5; https://doi.org/10.3390/bioengineering8010005 - 05 Jan 2021

Cited by 29 | Viewed by 9085

Abstract

Since their first synthesis in the late 1960s, collagen mimetic peptides (CMPs) have been used as a molecular tool to study collagen, and as an approach to develop novel collagen mimetic biomaterials. Collagen, a major extracellular matrix (ECM) protein, plays vital roles in [...] Read more.

Since their first synthesis in the late 1960s, collagen mimetic peptides (CMPs) have been used as a molecular tool to study collagen, and as an approach to develop novel collagen mimetic biomaterials. Collagen, a major extracellular matrix (ECM) protein, plays vital roles in many physiological and pathogenic processes. Applications of CMPs have advanced our understanding of the structure and molecular properties of a collagen triple helix—the building block of collagen—and the interactions of collagen with important molecular ligands. The accumulating knowledge is also paving the way for developing novel CMPs for biomedical applications. Indeed, for the past 50 years, CMP research has been a fast-growing, far-reaching interdisciplinary field. The major development and achievement of CMPs were documented in a few detailed reviews around 2010. Here, we provided a brief overview of what we have learned about CMPs—their potential and their limitations. We focused on more recent developments in producing heterotrimeric CMPs, and CMPs that can form collagen-like higher order molecular assemblies. We also expanded the traditional view of CMPs to include larger designed peptides produced using recombinant systems. Studies using recombinant peptides have provided new insights on collagens and promoted progress in the development of collagen mimetic fibrillar self-assemblies. Full article

(This article belongs to the Special Issue Biomedical Applications of Collagen)

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23 pages, 13871 KiB

Open AccessEditor’s ChoiceReview

Collagen Structure-Function Mapping Informs Applications for Regenerative Medicine

by James D. San Antonio, Olena Jacenko, Andrzej Fertala and Joseph P.R.O. Orgel

Bioengineering 2021, 8(1), 3; https://doi.org/10.3390/bioengineering8010003 - 29 Dec 2020

Cited by 41 | Viewed by 7564

Abstract

Type I collagen, the predominant protein of vertebrates, assembles into fibrils that orchestrate the form and function of bone, tendon, skin, and other tissues. Collagen plays roles in hemostasis, wound healing, angiogenesis, and biomineralization, and its dysfunction contributes to fibrosis, atherosclerosis, cancer metastasis, [...] Read more.

Type I collagen, the predominant protein of vertebrates, assembles into fibrils that orchestrate the form and function of bone, tendon, skin, and other tissues. Collagen plays roles in hemostasis, wound healing, angiogenesis, and biomineralization, and its dysfunction contributes to fibrosis, atherosclerosis, cancer metastasis, and brittle bone disease. To elucidate the type I collagen structure-function relationship, we constructed a type I collagen fibril interactome, including its functional sites and disease-associated mutations. When projected onto an X-ray diffraction model of the native collagen microfibril, data revealed a matrix interaction domain that assumes structural roles including collagen assembly, crosslinking, proteoglycan (PG) binding, and mineralization, and the cell interaction domain supporting dynamic aspects of collagen biology such as hemostasis, tissue remodeling, and cell adhesion. Our type III collagen interactome corroborates this model. We propose that in quiescent tissues, the fibril projects a structural face; however, tissue injury releases blood into the collagenous stroma, triggering exposure of the fibrils’ cell and ligand binding sites crucial for tissue remodeling and regeneration. Applications of our research include discovery of anti-fibrotic antibodies and elucidating their interactions with collagen, and using insights from our angiogenesis studies and collagen structure-function model to inform the design of super-angiogenic collagens and collagen mimetics. Full article

(This article belongs to the Special Issue Biomedical Applications of Collagen)

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20 pages, 1884 KiB

Open AccessReview

Engineered Collagen Matrices

by Vaidehi A. Patil and Kristyn S. Masters

Bioengineering 2020, 7(4), 163; https://doi.org/10.3390/bioengineering7040163 - 16 Dec 2020

Cited by 31 | Viewed by 5098

Abstract

Collagen is the most abundant protein in mammals, accounting for approximately one-third of the total protein in the human body. Thus, it is a logical choice for the creation of biomimetic environments, and there is a long history of using collagen matrices for [...] Read more.

Collagen is the most abundant protein in mammals, accounting for approximately one-third of the total protein in the human body. Thus, it is a logical choice for the creation of biomimetic environments, and there is a long history of using collagen matrices for various tissue engineering applications. However, from a biomaterial perspective, the use of collagen-only scaffolds is associated with many challenges. Namely, the mechanical properties of collagen matrices can be difficult to tune across a wide range of values, and collagen itself is not highly amenable to direct chemical modification without affecting its architecture or bioactivity. Thus, many approaches have been pursued to design scaffold environments that display critical features of collagen but enable improved tunability of physical and biological characteristics. This paper provides a brief overview of approaches that have been employed to create such engineered collagen matrices. Specifically, these approaches include blending of collagen with other natural or synthetic polymers, chemical modifications of denatured collagen, de novo creation of collagen-mimetic chains, and reductionist methods to incorporate collagen moieties into other materials. These advancements in the creation of tunable, engineered collagen matrices will continue to enable the interrogation of novel and increasingly complex biological questions. Full article

(This article belongs to the Special Issue Biomedical Applications of Collagen)

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24 pages, 1079 KiB

Open AccessReview

Best of Both Hydrogel Worlds: Harnessing Bioactivity and Tunability by Incorporating Glycosaminoglycans in Collagen Hydrogels

by Tanaya Walimbe and Alyssa Panitch

Bioengineering 2020, 7(4), 156; https://doi.org/10.3390/bioengineering7040156 - 02 Dec 2020

Cited by 24 | Viewed by 7719

Abstract

Collagen, the most abundant protein in mammals, has garnered the interest of scientists for over 50 years. Its ubiquitous presence in all body tissues combined with its excellent biocompatibility has led scientists to study its potential as a biomaterial for a wide variety [...] Read more.

Collagen, the most abundant protein in mammals, has garnered the interest of scientists for over 50 years. Its ubiquitous presence in all body tissues combined with its excellent biocompatibility has led scientists to study its potential as a biomaterial for a wide variety of biomedical applications with a high degree of success and widespread clinical approval. More recently, in order to increase their tunability and applicability, collagen hydrogels have frequently been co-polymerized with other natural and synthetic polymers. Of special significance is the use of bioactive glycosaminoglycans—the carbohydrate-rich polymers of the ECM responsible for regulating tissue homeostasis and cell signaling. This review covers the recent advances in the development of collagen-based hydrogels and collagen-glycosaminoglycan blend hydrogels for biomedical research. We discuss the formulations and shortcomings of using collagen in isolation, and the advantages of incorporating glycosaminoglycans (GAGs) in the hydrogels. We further elaborate on modifications used on these biopolymers for tunability and discuss tissue specific applications. The information presented herein will demonstrate the versatility and highly translational value of using collagen blended with GAGs as hydrogels for biomedical engineering applications. Full article

(This article belongs to the Special Issue Biomedical Applications of Collagen)

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26 pages, 2017 KiB

Open AccessReview

Three Decades of Research on Recombinant Collagens: Reinventing the Wheel or Developing New Biomedical Products?

by Andrzej Fertala

Bioengineering 2020, 7(4), 155; https://doi.org/10.3390/bioengineering7040155 - 02 Dec 2020

Cited by 38 | Viewed by 6631

Abstract

Collagens provide the building blocks for diverse tissues and organs. Furthermore, these proteins act as signaling molecules that control cell behavior during organ development, growth, and repair. Their long half-life, mechanical strength, ability to assemble into fibrils and networks, biocompatibility, and abundance from [...] Read more.

Collagens provide the building blocks for diverse tissues and organs. Furthermore, these proteins act as signaling molecules that control cell behavior during organ development, growth, and repair. Their long half-life, mechanical strength, ability to assemble into fibrils and networks, biocompatibility, and abundance from readily available discarded animal tissues make collagens an attractive material in biomedicine, drug and food industries, and cosmetic products. About three decades ago, pioneering experiments led to recombinant human collagens’ expression, thereby initiating studies on the potential use of these proteins as substitutes for the animal-derived collagens. Since then, scientists have utilized various systems to produce native-like recombinant collagens and their fragments. They also tested these collagens as materials to repair tissues, deliver drugs, and serve as therapeutics. Although many tests demonstrated that recombinant collagens perform as well as their native counterparts, the recombinant collagen technology has not yet been adopted by the biomedical, pharmaceutical, or food industry. This paper highlights recent technologies to produce and utilize recombinant collagens, and it contemplates their prospects and limitations. Full article

(This article belongs to the Special Issue Biomedical Applications of Collagen)

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