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

Deadline for manuscript submissions: closed (30 June 2022) | Viewed by 9551

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Dr. Burkhard Poeggeler

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Department of Physiology, Johann-Friedrich-Blumenbach-Institute for Zoology and Anthropology, Faculty of Biology Georg August University Göttingen, Göttingen and Goettingen Research Campus, Göttingen, Am Türmchen 3, D-33332 Gütersloh, Germany
Interests: aging; amino acids; antioxidants; inflammaging; melatonin; product development; tryptophan
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Dear Colleagues,

Collagen is the most abundant protein in the body and this key molecule acts as a decisive element of the skin, connective tissue, joints, interstitium, glymphatic system and cardiovascular system. The endogenous intracellular, intercellular and extracellular matrices as well as the glycocalyx acting as the pericellular matrix are largely formed by collagen and attached matrix elements such as glycoproteins, lipoproteins and glycolipids. Endothelial function and neurovascular coupling are ensured by collagen fibers that enable vasoconstriction and vasodilation. For instance, the globular collagen fibers mediate entrainment by the exposome by translating the night shift and drift of the Schumann resonance into the nocturnal shifting and dipping of blood pressure that enables regenerative slow-wave sleep by synchronizing endogenous temperature-dependent brain activity. Collagen carbamylation or glycosylation and oxidation lead to the formation of defect fibers with misfolded proteins and high molecular collagen fragments. Thus, the continuous repair and regeneration of endogenous collagen is needed. Collagen peptides, vitamins such as vitamin C and trace elements such as zinc can promote endogenous collagen synthesis that declines with age and restore the proper structure and function of these decisive proteins. The constriction and dilation of collagen by water release and absorption brings about a tension of 120 MPa, which is 300 times more than the actin–myosin system can generate in terms of force. Consequently, collagen can develop enormous power and decisively determine the skin, connective tissue and myoskeletal and vascular elasticity and strength.

This Special Issue invites papers on all topics related to collagen and the collagen connection, which are essential elements of all living organisms.

Dr. Burkhard Poeggeler
Guest Editor

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Keywords

collagen
collagen fibers
collagen peptides
vitamins
matrix elements
glycoproteins
lipoproteins
glycolipids

Published Papers (5 papers)

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Research

Open AccessArticle

Role of Citrullinated Collagen in Autoimmune Arthritis

Virginia Woo-Rasberry

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Int. J. Mol. Sci. 2022, 23(17), 9833; https://doi.org/10.3390/ijms23179833 - 30 Aug 2022

Cited by 1 | Viewed by 1336

Abstract

Citrullination of proteins plays an important role in protein function and it has recently become clear that citrullinated proteins play a role in immune responses. In this study we examined how citrullinated collagen, an extracellular matrix protein, affects T-cell function during the development of autoimmune arthritis. Using an HLA-DR1 transgenic mouse model of rheumatoid arthritis, mice were treated intraperitoneally with either native type I collagen (CI), citrullinated CI (cit-CI), or phosphate buffered saline (PBS) prior to induction of autoimmune arthritis. While the mice given native CI had significantly less severe arthritis than controls administered PBS, mice receiving cit-CI had no decrease in the severity of autoimmune arthritis. Using Jurkat cells expressing the inhibitory receptor leukocyte-associated immunoglobulin-like receptor-1 (LAIR-1), Western blot analysis indicated that while CI and cit-CI bound to LAIR-1 with similar affinity, only CI induced phosphorylation of the LAIR ITIM tyrosines; cit-CI was ineffective. These data suggest that cit-CI acts as an antagonist of LAIR-1 signaling, and that the severity of autoimmune arthritis can effectively be altered by targeting T cells with citrullinated collagen. Full article

(This article belongs to the Special Issue The Collagen Connection)

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Open AccessCommunication

Irradiated Triple-Negative Breast Cancer Co-Culture Produces a Less Oncogenic Extracellular Matrix

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Int. J. Mol. Sci. 2022, 23(15), 8265; https://doi.org/10.3390/ijms23158265 - 27 Jul 2022

Cited by 3 | Viewed by 1305

Abstract

Triple-negative breast cancer is the most common and most deadly cancer among women. Radiation is a mainstay of treatment, administered after surgery, and used in the hope that any remaining cancer cells will be destroyed. While the cancer cell response is normally the focus of radiation therapy, little is known about the tumor microenvironment response after irradiation. It is widely reported that increased collagen expression and deposition are associated with cancer progression and poor prognosis in breast cancer patients. Aside from the classical fibrotic response, ratios of collagen isoforms have not been studied in a radiated tumor microenvironment. Here, we created one healthy co-culture of stromal fibroblasts and adipose-derived stem cells, and one triple-negative breast cancer co-culture, made of stromal fibroblasts, adipose derived stem cells, and triple-negative breast cancer cells. After irradiation, growth and decellularization of co-cultures, we reseeded the breast cancer cells for 24 h and analyzed the samples using mass spectrometry. Proteomic analysis revealed that collagen VI, a highly oncogenic collagen isoform linked to breast cancer, was decreased in the irradiated cancer co-culture. This indicates that the anti-cancer impact of radiation may be not only cell ablative, but also influential in creating a less oncogenic microenvironment. Full article

(This article belongs to the Special Issue The Collagen Connection)

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Open AccessArticle

Collagen Mimetic Peptides Promote Adherence and Migration of ARPE-19 Cells While Reducing Inflammatory and Oxidative Stress

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Int. J. Mol. Sci. 2022, 23(13), 7004; https://doi.org/10.3390/ijms23137004 - 23 Jun 2022

Viewed by 1792

Abstract

Epithelial cells of multiple types produce and interact with the extracellular matrix to maintain structural integrity and promote healthy function within diverse endogenous tissues. Collagen is a critical component of the matrix, and challenges to collagen’s stability in aging, disease, and injury influence survival of adherent epithelial cells. The retinal pigment epithelium (RPE) is important for maintaining proper function of the light-sensitive photoreceptors in the neural retina, in part through synergy with the collagen-rich Bruch’s membrane that promotes RPE adherence. Degradation of Bruch’s is associated with RPE degeneration, which is implicated early in age-related macular degeneration, a leading cause of irreversible vision loss worldwide. Collagen mimetic peptides (CMPs) effectively repair damage to collagen helices, which are present in all collagens. Our previous work indicates that in doing so, CMPs promote survival and integrity of affected cells and tissues in models of ocular injury and disease, including wounding of corneal epithelial cells. Here, we show that CMPs increase adherence and migration of the ARPE-19 line of human RPE cells challenged by digestion of their collagen substrate. Application of CMPs also reduced both ARPE-19 secretion of pro-inflammatory cytokines (interleukins 6 and 8) and production of reactive oxygen species. Taken together, these results suggest that repairing collagen damaged by aging or other pathogenic processes in the posterior eye could improve RPE adherence and survival and, in doing so, reduce the inflammatory and oxidative stress that perpetuates the cycle of destruction at the root of age-related diseases of the outer retina. Full article

(This article belongs to the Special Issue The Collagen Connection)

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Open AccessArticle

Increased Collagen Crosslinking in Stiff Clubfoot Tissue: Implications for the Improvement of Therapeutic Strategies

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Int. J. Mol. Sci. 2021, 22(21), 11903; https://doi.org/10.3390/ijms222111903 - 02 Nov 2021

Cited by 5 | Viewed by 1711

Abstract

Congenital clubfoot is a complex musculoskeletal deformity, in which a stiff, contracted tissue forms in the medial part of the foot. Fibrotic changes are associated with increased collagen deposition and lysyl oxidase (LOX)-mediated crosslinking, which impair collagen degradation and increase the tissue stiffness. First, we studied collagen deposition, as well as the expression of collagen and the amount of pyridinoline and deoxypyridinoline crosslinks in the tissue of relapsed clubfoot by immunohistochemistry, real-time PCR, and enzyme-linked immunosorbent assay (ELISA). We then isolated fibroblast-like cells from the contracted tissue to study the potential inhibition of these processes in vitro. We assessed the effects of a LOX inhibitor, β-aminopropionitrile (BAPN), on the cells by a hydroxyproline assay, ELISA, and Second Harmonic Generation imaging. We also evaluated the cell-mediated contraction of extracellular matrix in 3D cell-populated collagen gels. For the first time, we have confirmed significantly increased crosslinking and excessive collagen type I deposition in the clubfoot-contracted tissue. We successfully reduced these processes in vitro in a dose-dependent manner with 10–40 µg/mL of BAPN, and we observed an increasing trend in the inhibition of the cell-mediated contraction of collagen gels. The in vitro inhibitory effects indicate that BAPN has good potential for the treatment of relapsed and resistant clubfeet. Full article

(This article belongs to the Special Issue The Collagen Connection)

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Open AccessArticle

Vitamin B Mitigates Thoracic Aortic Dilation in Marfan Syndrome Mice by Restoring the Canonical TGF-β Pathway

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Int. J. Mol. Sci. 2021, 22(21), 11737; https://doi.org/10.3390/ijms222111737 - 29 Oct 2021

Cited by 5 | Viewed by 2440

Abstract

Thoracic aortic aneurysm (TAA) formation is a multifactorial process that results in diverse clinical manifestations and drug responses. Identifying the critical factors and their functions in Marfan syndrome (MFS) pathogenesis is important for exploring personalized medicine for MFS. Methylenetetrahydrofolate reductase (MTHFR), methionine synthase (MTR), and methionine synthase reductase (MTRR) polymorphisms have been correlated with TAA severity in MFS patients. However, the detailed relationship between the folate-methionine cycle and MFS pathogenesis remains unclear. Fbn1^C1039G/+ mice were reported to be a disease model of MFS. To study the role of the folate-methionine cycle in MFS, Fbn1^C1039G/+ mice were treated orally with methionine or vitamin B mixture (VITB), including vitamins B6, B9, and B12, for 20 weeks. VITB reduced the heart rate and circumference of the ascending aorta in Fbn1^C1039G/+ mice. Our data showed that the Mtr and Smad4 genes were suppressed in Fbn1^C1039G/+ mice, while VITB treatment restored the expression of these genes to normal levels. Additionally, VITB restored canonical transforming-growth factor β (TGF-β) signaling and promoted Loxl1-mediated collagen maturation in aortic media. This study provides a potential method to attenuate the pathogenesis of MFS that may have a synergistic effect with drug treatments for MFS patients. Full article

(This article belongs to the Special Issue The Collagen Connection)

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