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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Macromolecules".

Deadline for manuscript submissions: closed (30 January 2024) | Viewed by 9124

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Special Issue Editor

Dr. Blerida Banushi

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Genetics and Genomic (GGM) Department, University College London, London WC1N 1EH, UK
Interests: mental health; breathwork; meditation; psychedelic therapies
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Collagens are the most abundant family of proteins in mammals. With 28 known types, collagens are present at diverse locations and possess varying functions. They represent the major component of the extracellular matrix that gives structural integrity to the cell and are involved in cell signalling and processes such as adhesion and migration.

Abnormalities affecting collagen homeostasis have been associated with many connective tissue disorders and various diseases such as cancer and autoimmune diseases.

Despite the extensive research on collagen over the past 100 years, our knowledge of the most abundant protein of the human body remains very limited.

This open access Special Issue will provide up-to-date research and review articles on our advanced knowledge of collagen proteins.

Topics include, but are not limited to:

the complexity of collagen synthesis, processing, degradation, and turnover
collagen homeostasis in health, aging, and disease
intracellular and extracellular post-translational modifications of collagens
advances in techniques for the analysis of collagen structure and function

Dr. Blerida Banushi
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.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

collagen
extracellular matrix
connective tissue
collagen homeostasis
collagen modifications
collagen structure
collagen biosynthesis
collagen diseases
cancer
aging

Published Papers (6 papers)

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Research

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12 pages, 1981 KiB

Open AccessCommunication

Collagen Mimetic Peptides Promote Repair of MMP-1-Damaged Collagen in the Rodent Sclera and Optic Nerve Head

by Ghazi O. Bou Ghanem, Dmitry Koktysh, Robert O. Baratta, Brian J. Del Buono, Eric Schlumpf, Lauren K. Wareham and David J. Calkins

Int. J. Mol. Sci. 2023, 24(23), 17031; https://doi.org/10.3390/ijms242317031 - 1 Dec 2023

Viewed by 945

Abstract

The structural and biomechanical properties of collagen-rich ocular tissues, such as the sclera, are integral to ocular function. The degradation of collagen in such tissues is associated with debilitating ophthalmic diseases such as glaucoma and myopia, which often lead to visual impairment. Collagen mimetic peptides (CMPs) have emerged as an effective treatment to repair damaged collagen in tissues of the optic projection, such as the retina and optic nerve. In this study, we used atomic force microscopy (AFM) to assess the potential of CMPs in restoring tissue stiffness in the optic nerve head (ONH), including the peripapillary sclera (PPS) and the glial lamina. Using rat ONH tissue sections, we induced collagen damage with MMP-1, followed by treatment with CMP-3 or vehicle. MMP-1 significantly reduced the Young’s modulus of both the PPS and the glial lamina, indicating tissue softening. Subsequent CMP-3 treatment partially restored tissue stiffness in both the PPS and the glial lamina. Immunohistochemical analyses revealed reduced collagen fragmentation after MMP-1 digestion in CMP-3-treated tissues compared to vehicle controls. In summary, these results demonstrate the potential of CMPs to restore collagen stiffness and structure in ONH tissues following enzymatic damage. CMPs may offer a promising therapeutic avenue for preserving vision in ocular disorders involving collagen remodeling and degradation. Full article

(This article belongs to the Special Issue Recent Advances in Collagen Proteins)

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21 pages, 5316 KiB

Open AccessArticle

THBS1-Mediated Degradation of Collagen via the PI3K/AKT Pathway Facilitates the Metastasis and Poor Prognosis of OSCC

by Zhihao Wen, Yuxiao Zhang, Xiangyao Wang, Yaxin Wu, Jing Mao, Qilin Li and Shiqiang Gong

Int. J. Mol. Sci. 2023, 24(17), 13312; https://doi.org/10.3390/ijms241713312 - 28 Aug 2023

Cited by 7 | Viewed by 1286

Abstract

Oral squamous cell carcinoma (OSCC) is a prevalent form of malignant tumor, characterized by a persistently high incidence and mortality rate. The extracellular matrix (ECM) plays a crucial role in the initiation, progression, and diverse biological behaviors of OSCC, facilitated by mechanisms such as providing structural support, promoting cell migration and invasion, regulating cell morphology, and modulating signal transduction. This study investigated the involvement of ECM-related genes, particularly THBS1, in the prognosis and cellular behavior of OSCC. The analysis of ECM-related gene data from OSCC samples identified 165 differentially expressed genes forming two clusters with distinct prognostic outcomes. Seventeen ECM-related genes showed a significant correlation with survival. Experimental methods were employed to demonstrate the impact of THBS1 on proliferation, migration, invasion, and ECM degradation in OSCC cells. A risk-prediction model utilizing four differentially prognostic genes demonstrated significant predictive value in overall survival. THBS1 exhibited enrichment of the PI3K/AKT pathway, indicating its potential role in modulating OSCC. In conclusion, this study observed and verified that ECM-related genes, particularly THBS1, have the potential to influence the prognosis, biological behavior, and immunotherapy of OSCC. These findings hold significant implications for enhancing survival outcomes and providing guidance for precise treatment of OSCC. Full article

(This article belongs to the Special Issue Recent Advances in Collagen Proteins)

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14 pages, 4097 KiB

Open AccessArticle

Preparation and Characterization of a Photo-Crosslinked Methacryloyl-Collagen Composite Film to Promote Corneal Nerve Regeneration via Surface Grafting of Taurine Molecules

by Yang Liu, Chuanlei Zhang, Yanhui Kong, Huiyu Liu, Cheng Chen, Wenyu Gao, Xiaowei Xi, Hui Yang and Linhong Deng

Int. J. Mol. Sci. 2023, 24(14), 11248; https://doi.org/10.3390/ijms241411248 - 8 Jul 2023

Viewed by 1178

Abstract

Blindness is frequently caused by corneal abnormalities, and corneal transplantation is the most effective treatment method. It is extremely important to develop high-quality artificial corneas because there are not enough donor corneas accessible for cornea transplantation. One of the most-often utilized materials is collagen, which is the primary component of natural cornea. Collagen-based corneal repair materials have good physicochemical properties and excellent biocompatibility, but how to promote the regeneration of the corneal nerve after keratoplasty is still a big challenge. In this research, in order to promote the growth of nerve cells on a collagen (Col) substrate, a novel collagen-based material was synthesized starting from the functionalization of collagen with unsaturated methacryloyl groups that three-dimensionally photopolymerize to a 3D network of chemically crosslinked collagen (ColMA), onto which taurine molecules were eventually grafted (ColMA-Tr). The physicochemical properties and biocompatibility of the Col, ColMA and ColMA-Tr films were evaluated. By analyzing the results, we found that all the three samples had good moisture retention and aq high covalent attachment of methacryloyl groups followed by their photopolymerization improved the mechanical properties of the ColMA and ColMA-Tr. Most importantly, compared with ColMA, the taurine-modified collagen-MA film significantly promoted the growth of nerve cells and corneal epithelial cells on its surface. Our preliminary results suggest that this novel ColMA-Tr film may have potential use in cornea tissue engineering in the future. Full article

(This article belongs to the Special Issue Recent Advances in Collagen Proteins)

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22 pages, 7910 KiB

Open AccessArticle

Identification of Regulatory Molecular “Hot Spots” for LH/PLOD Collagen Glycosyltransferase Activity

by Daiana Mattoteia, Antonella Chiapparino, Marco Fumagalli, Matteo De Marco, Francesca De Giorgi, Lisa Negro, Alberta Pinnola, Silvia Faravelli, Tony Roscioli, Luigi Scietti and Federico Forneris

Int. J. Mol. Sci. 2023, 24(13), 11213; https://doi.org/10.3390/ijms241311213 - 7 Jul 2023

Cited by 1 | Viewed by 1741

Abstract

Hydroxylysine glycosylations are post-translational modifications (PTMs) essential for the maturation and homeostasis of fibrillar and non-fibrillar collagen molecules. The multifunctional collagen lysyl hydroxylase 3 (LH3/PLOD3) and the collagen galactosyltransferase GLT25D1 are the human enzymes that have been identified as being responsible for the glycosylation of collagen lysines, although a precise description of the contribution of each enzyme to these essential PTMs has not yet been provided in the literature. LH3/PLOD3 is thought to be capable of performing two chemically distinct collagen glycosyltransferase reactions using the same catalytic site: an inverting beta-1,O-galactosylation of hydroxylysines (Gal-T) and a retaining alpha-1,2-glucosylation of galactosyl hydroxylysines (Glc-T). In this work, we have combined indirect luminescence-based assays with direct mass spectrometry-based assays and molecular structure studies to demonstrate that LH3/PLOD3 only has Glc-T activity and that GLT25D1 only has Gal-T activity. Structure-guided mutagenesis confirmed that the Glc-T activity is defined by key residues in the first-shell environment of the glycosyltransferase catalytic site as well as by long-range contributions from residues within the same glycosyltransferase (GT) domain. By solving the molecular structures and characterizing the interactions and solving the molecular structures of human LH3/PLOD3 in complex with different UDP-sugar analogs, we show how these studies could provide insights for LH3/PLOD3 glycosyltransferase inhibitor development. Collectively, our data provide new tools for the direct investigation of collagen hydroxylysine PTMs and a comprehensive overview of the complex network of shapes, charges, and interactions that enable LH3/PLOD3 glycosyltransferase activities, expanding the molecular framework and facilitating an improved understanding and manipulation of glycosyltransferase functions in biomedical applications. Full article

(This article belongs to the Special Issue Recent Advances in Collagen Proteins)

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Review

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14 pages, 1072 KiB

Open AccessReview

Features of Congenital Arthrogryposis Due to Abnormalities in Collagen Homeostasis, a Scoping Review

by Sarah MacKenzie Picker, George Parker and Paul Gissen

Int. J. Mol. Sci. 2023, 24(17), 13545; https://doi.org/10.3390/ijms241713545 - 31 Aug 2023

Viewed by 1045

Abstract

Congenital arthrogryposis (CA) refers to the presence of multiple contractures at birth. It is a feature of several inherited syndromes, notable amongst them are disorders of collagen formation. This review aims to characterize disorders that directly or indirectly impact collagen structure and function leading to CA in search for common phenotypic or pathophysiological features, possible genotype–phenotype correlation, and potential novel treatment approaches based on a better understanding of the underlying pathomechanism. Nine genes, corresponding to five clinical phenotypes, were identified after a literature search. The most notable trend was the extreme phenotype variability. Clinical features across all syndromes ranged from subtle with minimal congenital contractures, to severe with multiple congenital contractures and extra-articular features including skin, respiratory, or other manifestations. Five of the identified genes were involved in the function of the Lysyl Hydroxylase 2 or 3 enzymes, which enable the hydroxylation and/or glycosylation of lysyl residues to allow the formation of the collagen superstructure. Whilst current treatment approaches are post-natal surgical correction, there are also potential in-utero therapies being developed. Cyclosporin A showed promise in treating collagen VI disorders although there is an associated risk of immunosuppression. The treatments that could be in the clinical trials soon are the splice correction therapies in collagen VI-related disorders. Full article

(This article belongs to the Special Issue Recent Advances in Collagen Proteins)

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21 pages, 1585 KiB

Open AccessReview

Significance of Type II Collagen Posttranslational Modifications: From Autoantigenesis to Improved Diagnosis and Treatment of Rheumatoid Arthritis

by Tsvetelina Batsalova and Balik Dzhambazov

Int. J. Mol. Sci. 2023, 24(12), 9884; https://doi.org/10.3390/ijms24129884 - 8 Jun 2023

Cited by 3 | Viewed by 1882

Abstract

Collagen type II (COL2), the main structural protein of hyaline cartilage, is considerably affected by autoimmune responses associated with the pathogenesis of rheumatoid arthritis (RA). Posttranslational modifications (PTMs) play a significant role in the formation of the COL2 molecule and supramolecular fibril organization, and thus, support COL2 function, which is crucial for normal cartilage structure and physiology. Conversely, the specific PTMs of the protein (carbamylation, glycosylation, citrullination, oxidative modifications and others) have been implicated in RA autoimmunity. The discovery of the anti-citrullinated protein response in RA, which includes anti-citrullinated COL2 reactivity, has led to the development of improved diagnostic assays and classification criteria for the disease. The induction of immunological tolerance using modified COL2 peptides has been highlighted as a potentially effective strategy for RA therapy. Therefore, the aim of this review is to summarize the recent knowledge on COL2 posttranslational modifications with relevance to RA pathophysiology, diagnosis and treatment. The significance of COL2 PTMs as a source of neo-antigens that activate immunity leading to or sustaining RA autoimmunity is discussed. Full article

(This article belongs to the Special Issue Recent Advances in Collagen Proteins)

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