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Collagen Fibrillogenesis

Sanne D'hondt, Brecht Guillemyn, Delfien Syx, Sofie Symoens, Riet De Rycke, Leen Vanhoutte, Wendy Toussaint, Bart N Lambrecht, Anne De Paepe, Douglas R Keene, Yoshihiro Ishikawa, Hans Peter Bächinger, Sophie Janssens, Mathieu J M Bertrand, Fransiska Malfait
Type III collagen is a major fibrillar collagen consisting of three identical α1 (III)-chains that is particularly present in tissues exhibiting elastic properties, such as the skin and the arterial wall. Heterozygous mutations in the COL3A1 gene result in vascular Ehlers-Danlos syndrome (vEDS), a severe, life-threatening disorder, characterized by thin, translucent skin and propensity to arterial, intestinal and uterine rupture. Most human vEDS cases result from a missense mutation substituting a crucial glycine residue in the triple helical domain of the α1 (III)-chains...
March 15, 2018: Matrix Biology: Journal of the International Society for Matrix Biology
Karen L Posey, Francoise Coustry, Jacqueline T Hecht
Cartilage oligomeric matrix protein (COMP) is a large pentameric glycoprotein that interacts with multiple extracellular matrix proteins in cartilage and other tissues. While, COMP is known to play a role in collagen secretion and fibrillogenesis, chondrocyte proliferation and mechanical strength of tendons, the complete range of COMP functions remains to be defined. COMPopathies describe pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (MED), two skeletal dysplasias caused by autosomal dominant COMP mutations...
March 9, 2018: Matrix Biology: Journal of the International Society for Matrix Biology
Konstantina Karamanou, Gwenn Perrot, Francois-Xavier Maquart, Stéphane Brézillon
Wound healing, a complex physiological process, is responsible for tissue repair after exposure to destructive stimuli, without resulting in complete functional regeneration. Injuries can be stromal or epithelial, and most cases of wound repair have been studied in the skin and cornea. Lumican, a small leucine-rich proteoglycan, is expressed in the extracellular matrices of several tissues, such as the cornea, cartilage, and skin. This molecule has been shown to regulate collagen fibrillogenesis, keratinocyte phenotypes, and corneal transparency modulation...
March 1, 2018: Advanced Drug Delivery Reviews
Reza Nadafi, Jasper J Koning, Henrike Veninga, Xanthi N Stachtea, Tanja Konijn, Antonie Zwiers, Anders Malmström, Joke M M den Haan, Reina E Mebius, Marco Maccarana, Rogier M Reijmers
For full activation of naïve adaptive lymphocytes in skin-draining lymph nodes (LNs), presentation of peptide:MHC complexes by LN-resident and skin-derived dendritic cells (DCs) that encountered antigens (Ags) is an absolute prerequisite. To get to the nearest draining LN upon intradermal immunization, DCs need to migrate from the infection site to the afferent lymphatics, which can only be reached by traversing a collagen-dense network located in the dermis of the skin through the activity of proteolytic enzymes...
2018: Frontiers in Immunology
Marissa A Ruehle, Laxminarayanan Krishnan, Steven A LaBelle, Nick J Willett, Jeffrey A Weiss, Robert E Guldberg
Angiogenesis is a critical component during wound healing, and the process is sensitive to mechanical stimuli. Current in vitro culture environments used to investigate three-dimensional microvascular growth often lack dimensional stability and the ability to withstand compression. We investigated the ability of decorin, a proteoglycan known to modulate collagen fibrillogenesis, incorporated into a collagen hydrogel to increase construct dimensional stability while maintaining vascular growth. Decorin did not affect microvascular growth parameters, while increasing the compressive modulus of collagen gels and significantly reducing the contraction of 3% collagen gels after 16 days in culture...
September 2017: MRS Communications
Wen Zhang, Yan Ge, Qian Cheng, Qi Zhang, Lin Fang, Junnian Zheng
Decorin (DCN), an extracellular matrix (ECM) protein, belongs to the small leucine-rich proteoglycan family. As a pluripotent molecule, DCN regulates the bioactivities of cell growth factors and participates in ECM assembly. Accumulating evidence has shown that DCN acts as a ligand of various cytokines and growth factors by directly or indirectly interacting with the corresponding signalling molecules involved in cell growth, differentiation, proliferation, adhesion and metastasis and that DCN especially plays vital roles in cancer cell proliferation, spread, pro-inflammatory processes and anti-fibrillogenesis...
January 12, 2018: Oncotarget
Tomoyuki Nakamura
Cyclical inflation of the lungs depends on the elasticity of lung parenchymal tissues, a mechanical property that is largely determined by elastic fibers and collagen fibers contained therein. Breakdown of elastic fibers in lungs and lack of the ability to repair damaged elastic fibers causes emphysema, and excessive collagen fibrillogenesis in lung parenchyma is critical for the pathogenesis of lung fibrosis. Recent studies revealed that fibulin-3, 4, and 5, which are matricellular proteins collectively termed "short fibulins" or "elastic fibulins", play crucial roles in the assembly of elastic fibers...
February 2, 2018: Matrix Biology: Journal of the International Society for Matrix Biology
Wei Long Ng, Min Hao Goh, Wai Yee Yeong, May Win Naing
Native tissues and/or organs possess complex hierarchical porous structures that confer highly-specific cellular functions. Despite advances in fabrication processes, it is still very challenging to emulate the hierarchical porous collagen architecture found in most native tissues. Hence, the ability to recreate such hierarchical porous structures would result in biomimetic tissue-engineered constructs. Here, a single-step drop-on-demand (DOD) bioprinting strategy is proposed to fabricate hierarchical porous collagen-based hydrogels...
January 31, 2018: Biomaterials Science
Seungkuk Ahn, Keel Yong Lee, Kevin Kit Parker, Kwanwoo Shin
The extracellular matrix (ECM) consists of polymerized protein monomers that form a unique fibrous network providing stability and structural support to surrounding cells. We harnessed the fibrillogenesis mechanisms of naturally occurring ECM proteins to produce artificial fibers with a heterogeneous protein makeup. Using ECM proteins as fibril building blocks, we created uniquely structured multi-component ECM fibers. Sequential incubation of fibronectin (FN) and laminin (LAM) resulted in self-assembly into locally stacked fibers...
January 30, 2018: Scientific Reports
Neda Latifi, Meisam Asgari, Hojatollah Vali, Luc Mongeau
While collagen type I (Col-I) is commonly used as a structural component of biomaterials, collagen type III (Col-III), another fibril forming collagen ubiquitous in many soft tissues, has not previously been used. In the present study, the novel concept of an injectable hydrogel with semi-interpenetrating polymeric networks of heterotypic collagen fibrils, with tissue-specific Col-III to Col-I ratios, in a glycol-chitosan matrix was investigated. Col-III was introduced as a component of the novel hydrogel, inspired by its co-presence with Col-I in many soft tissues, its influence on the Col-I fibrillogenesis in terms of diameter and mechanics, and its established role in regulating scar formation...
January 18, 2018: Scientific Reports
Zhong Zheng, Aaron W James, Chenshuang Li, Wenlu Jiang, Joyce Z Wang, Grace X Chang, Kevin S Lee, Feng Chen, Emily A Berthiaume, Yao Chen, Hsin Chuan Pan, Eric C Chen, Weiming Li, Zhihe Zhao, Xinli Zhang, Kang Ting, Chia Soo
Blocking transforming growth factor (TGF)β1 signal transduction has been a central strategy for scar reduction; however, this approach appears to be minimally effective. Here, we show that fibromodulin (FMOD), a 59-kD small leucine-rich proteoglycan critical for normal collagen fibrillogenesis, significantly reduces scar formation while simultaneously increasing scar strength in both adult rodent models and porcine wounds, which simulate human cutaneous scar repair. Mechanistically, FMOD uncouples pro-migration/contraction cellular signals from pro-fibrotic signaling by selectively enhancing SMAD3-mediated signal transduction, while reducing AP-1-mediated TGFβ1 auto-induction and fibrotic extracellular matrix accumulation...
2017: Signal Transduction and Targeted Therapy
Yue Shen, Valerio Russo, Matthew R Zeglinski, Stephanie L Sellers, Zhengguo Wu, Cameron Oram, Stephanie Santacruz, Yulia Merkulova, Christopher Turner, Keerit Tauh, Hongyan Zhao, Tatjana Bozin, Lubos Bohunek, Haishan Zeng, Michael A Seidman, R Chris Bleackley, Bruce M McManus, Erkki Ruoslahti, Tero A H Järvinen, David J Granville
Decorin (DCN) is a small-leucine rich proteoglycan that mediates collagen fibrillogenesis, organization, and tensile strength. Adventitial DCN is reduced in abdominal aortic aneurysm (AAA) resulting in vessel wall instability thereby predisposing the vessel to rupture. Recombinant DCN fusion protein CAR-DCN was engineered with an extended C-terminus comprised of CAR homing peptide that recognizes inflamed blood vessels and penetrates deep into the vessel wall. In the present study, the role of systemically-administered CAR-DCN in AAA progression and rupture was assessed in a murine model...
November 20, 2017: Scientific Reports
Khanh-Hoa Tran-Ba, Daniel J Lee, Jieling Zhu, Keewook Paeng, Laura J Kaufman
Fibrillar type I collagen-based hydrogels are commonly used in tissue engineering and as matrices for biophysical studies. Mechanical and structural properties of these gels are known to be governed by the conditions under which fibrillogenesis occurs, exhibiting variation as a function of protein concentration, temperature, pH, and ionic strength. Deeper understanding of how macroscopic structure affects viscoelastic properties of collagen gels over the course of fibrillogenesis provides fundamental insight into biopolymer gel properties and promises enhanced control over the properties of such gels...
October 17, 2017: Biophysical Journal
Mario Raspanti, Marcella Reguzzoni, Marina Protasoni, Petra Basso
For many decades the fibrillar collagens have been the subject of a remarkable body of ultrastructural research. The vast majority of the studies, however, were carried out on tendon or on tendon-derived material. For many reasons this reflects an obvious choice but at the same time it also is an unfortunate circumstance, because this flooding of tendon-related data can easily encourage the false confidence that all connective tissues are similar. The reality is quite the opposite, and a different fibrillar structure has been long time observed on collagen fibrils from different tissues, the most notable example being offered by corneal fibrils...
October 10, 2017: International Journal of Biological Macromolecules
Jolanta Fertala, Freddy Romero, Ross Summer, Andrzej Fertala
Regardless of the cause of organ fibrosis, its main unwanted consequence is the formation of collagen fibril-rich deposits that hamper the structure and function of affected tissues. Although many strategies have been proposed for the treatment of fibrotic diseases, no therapy has been developed, which can effectively block the formation of collagen fibril deposits. With this in mind, we recently developed an antibody-based therapy to block key interactions that drive collagen molecules into fibrils. In this study, we analyzed target specificity, which is a main parameter that defines the safe use of all antibody-based therapies in humans...
October 2017: Monoclonal Antibodies in Immunodiagnosis and Immunotherapy
Chengyu Jiang, Kevin Zurick, Chunlin Qin, Matthew T Bernards
Bone tissue is comprised of collagen, non-collagenous proteins, and hydroxyapatite and the SIBLING (small integrin binding, N-linked glycoprotein) family of proteins is the primary group of non-collagenous proteins. By replicating the native interactions between collagen and the SIBLING family of proteins at the interface of an implant, it is believed that a bone scaffold will more easily integrate with the surrounding tissue. In this work bone sialoprotein (BSP), osteopontin (OPN), dentin sialoprotein (DSP), dentin phosphoprotein (DPP), C-terminal fragment of dentin matrix protein 1 (DMP1-C) and proteoglycan versions of DSP (DSP-PG) and DMP1 (DMP1-PG) were tested individually to determine their roles in collagen fibrillogenesis and the prevention of denaturation...
September 14, 2017: Connective Tissue Research
Seulgi Han, Byung Woo Hwang, Eun Young Jeon, Dooyup Jung, Geon Hui Lee, Do Hee Keum, Ki Su Kim, Seok Hyun Yun, Hyung Joon Cha, Sei Kwang Hahn
The recent progress in photonic nanomaterials has contributed greatly to the development of photomedicines. However, the finite depth of light penetration is still a serious limitation, constraining their clinical applications. Here, we developed a poly(allylamine) (PAAm)-modified upconversion nanoparticle/hyaluronate-rose bengal (UCNP/PAAm/HA-RB) conjugate complex for photochemical bonding of deep tissue with near-infrared (NIR) light illumination. Compared to the conventional invasive treatment via suturing and stapling, the UCNP/PAAm/HA-RB conjugate complex could be noninvasively delivered into the deep tissue and accelerate the tissue bonding upon NIR light illumination...
October 24, 2017: ACS Nano
Juan Du, Minqi Li
The goal of periodontal regenerative therapy is to predictably restore the tooth's supporting periodontal tissues and form a new connective tissue attachment of periodontal ligament (PDL) fibers and new alveolar bone. Periostin is a matricellular protein so named for its expression primarily in the periosteum and PDL of adult mice. Its biological functions have been widely studied in areas such as cardiovascular physiology and oncology. Despite being initially identified in the dental tissues and bone, investigations of Periostin functions in PDL and alveolar-bone-related physiopathology are less abundant...
December 2017: Cellular and Molecular Life Sciences: CMLS
Mark S Filla, Kaylee D Dimeo, Tiegang Tong, Donna M Peters
Fibronectin fibrils are a major component of the extracellular matrix (ECM) of the trabecular meshwork (TM). They are a key mediator of the formation of the ECM which controls aqueous humor outflow and contributes to the pathogenesis of glaucoma. The purpose of this work was to determine if a fibronectin-binding peptide called FUD, derived from the Streptococcus pyogenes Functional Upstream Domain of the F1 adhesin protein, could be used to control fibronectin fibrillogenesis and hence ECM formation under conditions where its expression was induced by treatment with the glucocorticoid dexamethasone...
December 2017: Experimental Eye Research
Marco Maccarana, René B Svensson, Anki Knutsson, Antonis Giannopoulos, Mea Pelkonen, MaryAnn Weis, David Eyre, Matthew Warman, Sebastian Kalamajski
The main structural component of connective tissues is fibrillar, cross-linked collagen whose fibrillogenesis can be modulated by Small Leucine-Rich Proteins/Proteoglycans (SLRPs). Not all SLRPs' effects on collagen and extracellular matrix in vivo have been elucidated; one of the less investigated SLRPs is asporin. Here we describe the successful generation of an Aspn-/- mouse model and the investigation of the Aspn-/- skin phenotype. Functionally, Aspn-/- mice had an increased skin mechanical toughness, although there were no structural changes present on histology or immunohistochemistry...
2017: PloS One
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