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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: closed (30 April 2023) | Viewed by 12981

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Dr. Shunji Hattori

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Nippi Research Institute of Biomatrix, 520-11 Kuwabara, Toride 302-0017, Japan
Interests: collagen; cells
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

In recent years, environmental issues have been attracting considerable attention on a global scale. In the microscopic world of living organisms, it is the extracellular matrix that provides the environment for cellular activities. Among the many extracellular matrix proteins, collagen is the most abundant, and various types of collagen support organs and tissues of the body such as fibers and basement membranes. In addition, collagen has been shown to function as a cell adhesion protein and a reservoir for various liquid factors. Collagen is expected to be applied to 3D culture substrates for organoids and regenerative medicine. Furthermore, it is becoming clear that collagen peptides, which are degraded products of collagen, are taken into the body and work to control cell functions. In this Special Issue, we would like to introduce review articles and recent original papers that serve as a platform to gain a comprehensive understanding of the diversity of collagen—a macromolecule with a supramolecular structure and microscopic functions—and to explore new ways to utilize collagen.

Dr. Shunji Hattori
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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Keywords

collagen
regenerative medicine
cell adhesion
collagen peptide

Published Papers (6 papers)

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Research

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11 pages, 2055 KiB

Open AccessArticle

Local Net Charge State of Collagen Triple Helix Is a Determinant of FKBP22 Binding to Collagen III

by Yoshihiro Ishikawa, Arkadiusz Bonna, Douglas B. Gould and Richard W. Farndale

Int. J. Mol. Sci. 2023, 24(20), 15156; https://doi.org/10.3390/ijms242015156 - 13 Oct 2023

Viewed by 1239

Abstract

Mutations in the FKBP14 gene encoding the endoplasmic reticulum resident collagen-related proline isomerase FK506 binding protein 22 kDa (FKBP22) result in kyphoscoliotic Ehlers–Danlos Syndrome (EDS), which is characterized by a broad phenotypic outcome. A plausible explanation for this outcome is that FKBP22 participates in the biosynthesis of subsets of collagen types: FKBP22 selectively binds to collagens III, IV, VI, and X, but not to collagens I, II, V, and XI. However, these binding mechanisms have never been explored, and they may underpin EDS subtype heterogeneity. Here, we used collagen Toolkit peptide libraries to investigate binding specificity. We observed that FKBP22 binding was distributed along the collagen helix. Further, it (1) was higher on collagen III than collagen II peptides and it (2) was correlated with a positive peptide charge. These findings begin to elucidate the mechanism by which FKBP22 interacts with collagen. Full article

(This article belongs to the Special Issue Updates & New Concepts in Collagen)

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18 pages, 8069 KiB

Open AccessArticle

The Role of Integrin Receptor’s α and β Subunits of Mouse Mesenchymal Stem Cells on the Interaction of Marine-Derived Blacktip Reef Shark (Carcharhinus melanopterus) Skin Collagen

by Baolin Ge, Mingjun Wei, Bin Bao, Zhilin Pan, Jeevithan Elango and Wenhui Wu

Int. J. Mol. Sci. 2023, 24(11), 9110; https://doi.org/10.3390/ijms24119110 - 23 May 2023

Cited by 1 | Viewed by 1597

Abstract

Marine collagen (MC) has recently attracted more attention in tissue engineering as a biomaterial substitute due to its significant role in cellular signaling mechanisms, especially in mesenchymal stem cells (MSCs). However, the actual signaling mechanism of MC in MSC growth, which is highly influenced by their molecular pattern, is poorly understood. Hence, we investigated the integrin receptors (α₁β₁, α₂β₁, α₁₀β₁, and α₁₁β₁) binding mechanism and proliferation of MCs (blacktip reef shark collagen (BSC) and blue shark collagen (SC)) compared to bovine collagen (BC) on MSCs behavior through functionalized collagen molecule probing for the first time. The results showed that BSC and SC had higher proliferation rates and accelerated scratch wound healing by increasing migratory rates of MSCs. Cell adhesion and spreading results demonstrated that MC had a better capacity to anchor MSCs and maintain cell morphology than controls. Living cell observations showed that BSC was gradually assembled by cells into the ECM network within 24 h. Interestingly, qRT-PCR and ELISA revealed that the proliferative effect of MC was triggered by interacting with specific integrin receptors such as α₂β₁, α₁₀β₁, and α₁₁β₁ of MSCs. Accordingly, BSC accelerated MSCs’ growth, adhesion, shape, and spreading by interacting with specific integrin subunits (α₂ and β₁) and thereby triggering further signaling cascade mechanisms. Full article

(This article belongs to the Special Issue Updates & New Concepts in Collagen)

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14 pages, 2265 KiB

Open AccessArticle

Collagen V α1 Chain Decrease in Papillary Dermis from Early Systemic Sclerosis: A New Proposal in Cutaneous Fibrosis Molecular Structure

by Jymenez de Morais, Ana Paula P. Velosa, Priscila C. Andrade, Denise Frediani, Solange Carrasco, Zelita A. de Jesus Queiroz, Patrícia Martin, Renata F. Saito, Vitória Elias, Cláudia Goldenstein-Schainberg, Roger Chammas, Percival D. Sampaio-Barros, Vera L. Capelozzi and Walcy R. Teodoro

Int. J. Mol. Sci. 2022, 23(20), 12654; https://doi.org/10.3390/ijms232012654 - 21 Oct 2022

Viewed by 1402

Abstract

Cutaneous fibrosis is one of the main features of systemic sclerosis (SSc). Recent findings correlated abnormal collagen V (Col V) deposition in dermis with skin thickening and disease activity in SSc. Considering that Col V is an important regulator of collagen fibrillogenesis, understanding the role of Col V in the first two years of the skin fibrosis in SSc (early SSc) can help to determine new targets for future treatments. In this study, we analyzed the morphological, ultrastructural and molecular features of α1(V) and α2(V) chains and the expression of their coding genes COL5A1 and COL5A2 in collagen fibrillogenesis in early-SSc. Skin biopsies were obtained from seven consecutive treatment-naïve patients with SSc-related fibrosis and four healthy controls. Our data showed increased α1(V) and α2(V) chain expression in the reticular dermis of early-SSc patients; however, immunofluorescence and ultrastructural immunogold staining determined a significant decreased expression of the α1(V) chain along the dermoepidermal junction in the papillary dermis from early-SSc-patients in relation to the control (12.77 ± 1.34 vs. 66.84 ± 3.36; p < 0.0001). The immunoblot confirmed the decreased expression of the α1(V) chain by the cutaneous fibroblasts of early-SSc, despite the increased COL5A1 and COL5A2 gene expression. In contrast, the α2(V) chain was overexpressed in the small vessels (63.18 ± 3.56 vs. 12.16 ± 0.81; p < 0.0001) and capillaries (60.88 ± 5.82 vs. 15.11 ± 3.80; p < 0.0001) in the reticular dermis of early-SSc patients. Furthermore, COLVA2 siRNA in SSc cutaneous fibroblasts resulted in a decreased α1(V) chain expression. These results highlight an intense decrease in the α1(V) chain along the dermoepidermal junction, suggesting an altered molecular histoarchitecture in the SSc papillary dermis, with a possible decrease in the expression of the α1(V)3 homotrimeric isoform, which could interfere with the thickening and cutaneous fibrosis related to SSc. Full article

(This article belongs to the Special Issue Updates & New Concepts in Collagen)

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Review

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33 pages, 5095 KiB

Open AccessReview

Reviewing the Regulators of COL1A1

by Hanne Devos, Jerome Zoidakis, Maria G. Roubelakis, Agnieszka Latosinska and Antonia Vlahou

Int. J. Mol. Sci. 2023, 24(12), 10004; https://doi.org/10.3390/ijms241210004 - 11 Jun 2023

Cited by 9 | Viewed by 2677

Abstract

The collagen family contains 28 proteins, predominantly expressed in the extracellular matrix (ECM) and characterized by a triple-helix structure. Collagens undergo several maturation steps, including post-translational modifications (PTMs) and cross-linking. These proteins are associated with multiple diseases, the most pronounced of which are fibrosis and bone diseases. This review focuses on the most abundant ECM protein highly implicated in disease, type I collagen (collagen I), in particular on its predominant chain collagen type I alpha 1 (COLα1 (I)). An overview of the regulators of COLα1 (I) and COLα1 (I) interactors is presented. Manuscripts were retrieved searching PubMed, using specific keywords related to COLα1 (I). COL1A1 regulators at the epigenetic, transcriptional, post-transcriptional and post-translational levels include DNA Methyl Transferases (DNMTs), Tumour Growth Factor β (TGFβ), Terminal Nucleotidyltransferase 5A (TENT5A) and Bone Morphogenic Protein 1 (BMP1), respectively. COLα1 (I) interacts with a variety of cell receptors including integrinβ, Endo180 and Discoidin Domain Receptors (DDRs). Collectively, even though multiple factors have been identified in association to COLα1 (I) function, the implicated pathways frequently remain unclear, underscoring the need for a more spherical analysis considering all molecular levels simultaneously. Full article

(This article belongs to the Special Issue Updates & New Concepts in Collagen)

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21 pages, 1583 KiB

Open AccessReview

by Ziwei Ouyang, Lei Dong, Feng Yao, Ke Wang, Yong Chen, Shufang Li, Renpeng Zhou, Yingjie Zhao and Wei Hu

Int. J. Mol. Sci. 2023, 24(12), 9841; https://doi.org/10.3390/ijms24129841 - 7 Jun 2023

Cited by 11 | Viewed by 3238

Abstract

Collagens serve essential mechanical functions throughout the body, particularly in the connective tissues. In articular cartilage, collagens provide most of the biomechanical properties of the extracellular matrix essential for its function. Collagen plays a very important role in maintaining the mechanical properties of articular cartilage and the stability of the ECM. Noteworthily, many pathogenic factors in the course of osteoarthritis and rheumatoid arthritis, such as mechanical injury, inflammation, and senescence, are involved in the irreversible degradation of collagen, leading to the progressive destruction of cartilage. The degradation of collagen can generate new biochemical markers with the ability to monitor disease progression and facilitate drug development. In addition, collagen can also be used as a biomaterial with excellent properties such as low immunogenicity, biodegradability, biocompatibility, and hydrophilicity. This review not only provides a systematic description of collagen and analyzes the structural characteristics of articular cartilage and the mechanisms of cartilage damage in disease states but also provides a detailed characterization of the biomarkers of collagen production and the role of collagen in cartilage repair, providing ideas and techniques for clinical diagnosis and treatment. Full article

(This article belongs to the Special Issue Updates & New Concepts in Collagen)

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14 pages, 574 KiB

Open AccessReview

Epithelial–Mesenchymal Transition Induced in Cancer Cells by Adhesion to Type I Collagen

by Hitomi Fujisaki and Sugiko Futaki

Int. J. Mol. Sci. 2023, 24(1), 198; https://doi.org/10.3390/ijms24010198 - 22 Dec 2022

Cited by 2 | Viewed by 1646

Abstract

The epithelial–mesenchymal transition (EMT) is an important biological process that is physiologically observed during development, wound healing, and cancer invasion. During EMT induction, cancer cells lose their epithelial properties owing to various tumor microenvironmental factors and begin to exhibit mesenchymal properties, such as loss of apical–basal polarity, weakened intercellular adhesion, and promotion of single cell migration. Several factors, including growth factor stimulation and adhesion to type I collagen (Col-I), induce EMT in cancer cells. Cells adhere to Col-I via specific receptors and induce EMT by activating outside-in signals. In vivo, Col-I molecules often form fibrils, which then assemble into supramolecular structures (gel form). Col-I also self-assembles in vitro under physiological conditions. Notably, Col-I can be used as a culture substrate in both gel and non-gel forms, and the gel formation state of Col-I affects cell fate. Although EMT can be induced in both forms of Col-I, the effects of gel formation on EMT induction remain unclear and somewhat inconsistent. Therefore, this study reviews the relationship between Col-I gel-forming states and EMT induction in cancer cells. Full article

(This article belongs to the Special Issue Updates & New Concepts in Collagen)

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