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Collagen Fibrillogenesis

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https://www.readbyqxmd.com/read/28910556/probing-the-influence-of-sibling-proteins-on-collagen-i-fibrillogenesis-and-denaturation
#1
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
https://www.readbyqxmd.com/read/28892611/upconversion-nanoparticles-hyaluronate-rose-bengal-conjugate-complex-for-noninvasive-photochemical-tissue-bonding
#2
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...
September 15, 2017: ACS Nano
https://www.readbyqxmd.com/read/28889194/functions-of-periostin-in-dental-tissues-and-its-role-in-periodontal-tissues-regeneration
#3
REVIEW
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...
September 9, 2017: Cellular and Molecular Life Sciences: CMLS
https://www.readbyqxmd.com/read/28860021/disruption-of-fibronectin-matrix-affects-type-iv-collagen-fibrillin-and-laminin-deposition-into-extracellular-matrix-of-human-trabecular-meshwork-htm-cells
#4
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...
August 30, 2017: Experimental Eye Research
https://www.readbyqxmd.com/read/28859141/asporin-deficient-mice-have-tougher-skin-and-altered-skin-glycosaminoglycan-content-and-structure
#5
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
https://www.readbyqxmd.com/read/28836214/visualizing-in-vitro-type-i-collagen-fibrillogenesis-by-transmission-electron-microscopy
#6
J Robin Harris
Techniques and protocols for the in vitro formation of collagen type I fibrils and the extensive biochemical variation of the fibrillogenesis conditions are presented. In all cases, the incubation and fibrillogenesis product can be readily monitored by transmission electron microscopic study of negatively stained specimens. Representative TEM data is presented and discussed within the context of the products of the fibrillogenesis protocols, from which the extensive biochemical and structural possibilities of this integrated approach can be appreciated...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28827814/fibromodulin-deficiency-reduces-collagen-structural-network-but-not-glycosaminoglycan-content-in-a-syngeneic-model-of-colon-carcinoma
#7
P Olof Olsson, Sebastian Kalamajski, Marco Maccarana, Åke Oldberg, Kristofer Rubin
Tumor barrier function in carcinoma represents a major challenge to treatment and is therefore an attractive target for increasing drug delivery. Variables related to tumor barrier include aberrant blood vessels, high interstitial fluid pressure, and the composition and structure of the extracellular matrix. One of the proteins associated with dense extracellular matrices is fibromodulin, a collagen fibrillogenesis modulator expressed in tumor stroma but scarce in normal loose connective tissues. Here, we investigated the effects of fibromodulin on stroma ECM in a syngeneic murine colon carcinoma model...
2017: PloS One
https://www.readbyqxmd.com/read/28794454/lumican-delays-melanoma-growth-in-mice-and-drives-tumor-molecular-assembly-as-well-as-response-to-matrix-targeted-tax2-therapeutic-peptide
#8
Albin Jeanne, Valérie Untereiner, Corinne Perreau, Isabelle Proult, Cyril Gobinet, Camille Boulagnon-Rombi, Christine Terryn, Laurent Martiny, Stéphane Brézillon, Stéphane Dedieu
Lumican is a small leucine-rich proteoglycan (SLRP) being known as a key regulator of collagen fibrillogenesis. However, little attention has been given so far in studying its influence on tumor-associated matrix architecture. Here, we investigate the role of host lumican on tumor matrix organization as well as on disease progression considering an immunocompetent model of melanoma implanted in Lum (-/-) vs. wild type syngeneic mice. Conjointly, lumican impact on tumor response to matrix-targeted therapy was evaluated considering a previously validated peptide, namely TAX2, that targets matricellular thrombospondin-1...
August 9, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28790175/antibody-mediated-blockade-of-jmjd6-interaction-with-collagen-i-exerts-antifibrotic-and-antimetastatic-activities
#9
Silvia Miotti, Alessandro Gulino, Renata Ferri, Mariella Parenza, Agnieszka Chronowska, Daniele Lecis, Sabina Sangaletti, Elda Tagliabue, Claudio Tripodo, Mario P Colombo
JMJD6 is known to localize in the nucleus exerting histone arginine demethylase and lysyl hydroxylase activities. A novel localization of JMJD6 in the extracellular matrix, resulting from its secretion as a soluble protein, was unveiled by a new anti-JMJD6 mAb called P4E11 which was developed to identify new targets in the stroma. Recombinant JMJD6 binds with collagen type I (Coll-I), and distinct JMJD6 peptides interfere with collagen fibrillogenesis, collagen-fibronectin interaction, and adhesion of human tumor cells to the collagen substrate...
August 8, 2017: FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology
https://www.readbyqxmd.com/read/28704418/the-coll%C3%AE-gen-iii-fibril-has-a-flexi-rod-structure-of-flexible-sequences-interspersed-with-rigid-bioactive-domains-including-two-with-hemostatic-roles
#10
J Des Parkin, James D San Antonio, Anton V Persikov, Hayat Dagher, Raymond Dalgleish, Shane T Jensen, Xavier Jeunemaitre, Judy Savige
Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I, with cell interaction domains, fibrillogenesis and enzyme cleavage domains, several major ligand-binding regions, and intermolecular crosslink sites at the same sites. These similarities allow heterotypic fibril formation with, and substitution by, collagen I in embryonic development and wound healing...
2017: PloS One
https://www.readbyqxmd.com/read/28629861/flavonoids-determine-the-rate-of-fibrillogenesis-and-structure-of-collagen-type-i-fibrils-in-vitro
#11
Yuri A Kim, Yury S Tarahovsky, Sergei G Gaidin, Elena A Yagolnik, Eugeny N Muzafarov
Collagen fibrils are produced from collagen monomers not only in vivo, but also in vitro. The ability to have an influence on the structure and properties of fibrils may find medical application and can be useful for controlling the formation of collagen gels and sheets in tissue engineering. Here we investigated the influence of flavonoids, distinguished by the number of hydroxyl groups in the B-ring, on the formation of collagen fibrils. A correlation was found between the number of hydroxyl groups, lipophilicity of molecules and their ability to influence the fibril formation...
November 2017: International Journal of Biological Macromolecules
https://www.readbyqxmd.com/read/28566802/are-genes-encoding-proteoglycans-really-associated-with-the-risk-of-anterior-cruciate-ligament-rupture
#12
P Cięszczyk, K Willard, P Gronek, P Zmijewski, G Trybek, J Gronek, M Weber-Rajek, P Stastny, M Petr, E Lulińska-Kuklik, K Ficek, E Kemeryte-Riaubiene, E Maculewicz, A V September
Proteoglycans are considered integral structural components of tendon and ligament and have been implicated in the resistance of compressive forces, collagen fibrillogenesis, matrix remodelling and cell signalling. Several sequence variants within genes encoding proteoglycans were recently implicated in modulating anterior cruciate ligament ruptures (ACLR). This study aimed to test the previously implicated variants in proteoglycan and vascular epithelial growth factor encoding genes with risk of ACLR in a population from Poland...
June 2017: Biology of Sport
https://www.readbyqxmd.com/read/28562432/a-two-phase-pilot-study-to-evaluate-the-safety-and-tolerability-of-an-in-situ-polymerizing-collagen
#13
Christopher Inglefield, Rebecca Rone-McCrate, Robert Brooks, Jiaxun Zhu, Sheila Grant, Dale P DeVore
BACKGROUND: Demand for collagen-based fillers has declined primarily because of limited long-term clinical benefit and the introduction of hyaluronic acid compositions. In situ polymerizing collagen is a noncrosslinked solution of porcine collagen containing a collagenase shield that undergoes fibrillogenesis on injected into tissues forming a natural matrix. OBJECTIVE: Conduct a prospective, single-center, dual-phase open-label study in 8 subjects to evaluate the safety, tolerability, and efficacy of the porcine collagen composition...
September 2017: Dermatologic Surgery: Official Publication for American Society for Dermatologic Surgery [et Al.]
https://www.readbyqxmd.com/read/28508516/fell-muir-lecture-collagen-fibril-formation-in-vitro-and-in-vivo
#14
REVIEW
Karl E Kadler
It is a great honour to be awarded the Fell Muir Prize for 2016 by the British Society of Matrix Biology. As recipient of the prize, I am taking the opportunity to write a minireview on collagen fibrillogenesis, which has been the focus of my research for 33 years. This is the process by which triple helical collagen molecules assemble into centimetre-long fibrils in the extracellular matrix of animals. The fibrils appeared a billion years ago at the dawn of multicellular animal life as the primary scaffold for tissue morphogenesis...
February 2017: International Journal of Experimental Pathology
https://www.readbyqxmd.com/read/28469139/in-vitro-fibrillogenesis-of-tropocollagen-type-iii-in-collagen-type-i-affects-its-relative-fibrillar-topology-and-mechanics
#15
Meisam Asgari, Neda Latifi, Hossein K Heris, Hojatollah Vali, Luc Mongeau
Tropocollagen types I and III were simultaneously fibrilized in vitro, and the differences between the geometric and mechanical properties of the heterotypic fibrils with different mixing ratios of tropocollagen III to I were investigated. Transmission electron microscopy was used to confirm the simultaneous presence of both tropocollagen types within the heterotypic fibrils. The incorporation of collagen III in I caused the fibrils to be thinner with a shorter D-banding than pure collagen I. Hertzian contact model was used to obtain the elastic moduli from atomic force microscope indentation testing using a force volume analysis...
May 3, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28463693/natural-healing-inspired-collagen-targeting-surgical-protein-glue-for-accelerated-scarless-skin-regeneration
#16
Eun Young Jeon, Bong-Hyuk Choi, Dooyup Jung, Byeong Hee Hwang, Hyung Joon Cha
Skin scarring after deep dermal injuries is a major clinical problem due to the current therapies limited to established scars with poor understanding of healing mechanisms. From investigation of aberrations within the extracellular matrix involved in pathophysiologic scarring, it was revealed that one of the main factors responsible for impaired healing is abnormal collagen reorganization. Here, inspired by the fundamental roles of decorin, a collagen-targeting proteoglycan, in collagen remodeling, we created a scar-preventive collagen-targeting glue consisting of a newly designed collagen-binding mussel adhesive protein and a specific glycosaminoglycan...
July 2017: Biomaterials
https://www.readbyqxmd.com/read/28422173/critical-involvement-of-zeb2-in-collagen-fibrillogenesis-the-molecular-similarity-between-mowat-wilson-syndrome-and-ehlers-danlos-syndrome
#17
Mika Teraishi, Mikiro Takaishi, Kimiko Nakajima, Mitsunori Ikeda, Yujiro Higashi, Shinji Shimoda, Yoshinobu Asada, Atsushi Hijikata, Osamu Ohara, Yoko Hiraki, Seiji Mizuno, Toshiyuki Fukada, Takahisa Furukawa, Nobuaki Wakamatsu, Shigetoshi Sano
Mowat-Wilson syndrome (MOWS) is a congenital disease caused by de novo heterozygous loss of function mutations or deletions of the ZEB2 gene. MOWS patients show multiple anomalies including intellectual disability, a distinctive facial appearance, microcephaly, congenital heart defects and Hirschsprung disease. However, the skin manifestation(s) of patients with MOWS has not been documented in detail. Here, we recognized that MOWS patients exhibit many Ehlers-Danlos syndrome (EDS)-like symptoms, such as skin hyperextensibility, atrophic scars and joint hypermobility...
April 19, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28412645/a-hidden-structural-vulnerability-in-the-thrombospondin-2-deficient-aorta-increases-the-propensity-to-intramural-delamination
#18
C Bellini, N J Kristofik, M R Bersi, T R Kyriakides, J D Humphrey
Mice lacking thrombospondin-2 (TSP2) represent an animal model of impaired collagen fibrillogenesis. Collagen constitutes ~1/3 of the wall of the normal murine descending thoracic aorta (DTA) and is thought to confer mechanical strength at high pressures. Microstructural analysis of the DTA from TSP2-null mice revealed irregular and disorganized collagen fibrils in the adventitia and at the interface between the media and adventitia. Yet, biaxial mechanical tests performed under physiologic loading conditions showed that most mechanical metrics, including stress and stiffness, were not different between mutant and control DTAs at 20- and 40-weeks of age, thus suggesting that the absence of TSP2 is well compensated under normal conditions...
March 9, 2017: Journal of the Mechanical Behavior of Biomedical Materials
https://www.readbyqxmd.com/read/28411451/anisotropic-tough-double-network-hydrogel-from-fish-collagen-and-its-spontaneous-in%C3%A2-vivo-bonding-to-bone
#19
Md Tariful Islam Mredha, Nobuto Kitamura, Takayuki Nonoyama, Susumu Wada, Keiko Goto, Xi Zhang, Tasuku Nakajima, Takayuki Kurokawa, Yasuaki Takagi, Kazunori Yasuda, Jian Ping Gong
Soft supporting tissues in the human body, such as cartilages and ligaments, are tough materials and firmly fixed to bones. These soft tissues, once injured, cannot regenerate spontaneously in vivo. Developing tough and biocompatible hydrogels as artificial soft supporting tissues would substantially improve outcomes after soft tissue injury. Collagen is the main rigid component in soft connective tissues which is organized in various hierarchical arrays. We have successfully developed a novel class of collagen fibril-based tough hydrogels based on the double network (DN) concept using swim bladder collagen (SBC) extracted from Bester sturgeon fish...
July 2017: Biomaterials
https://www.readbyqxmd.com/read/28387435/collagen-v-haploinsufficiency-in-a-murine-model-of-classic-ehlers-danlos-syndrome-is-associated-with-deficient-structural-and-mechanical-healing-in-tendons
#20
Jessica M Johnston, Brianne K Connizzo, Snehal S Shetye, Kelsey A Robinson, Julianne Huegel, Ashley B Rodriguez, Mei Sun, Sheila M Adams, David E Birk, Louis J Soslowsky
Classic Ehlers-Danlos syndrome (EDS) patients suffer from connective tissue hyperelasticity, joint instability, skin hyperextensibility, tissue fragility, and poor wound healing due to heterozygous mutations in COL5a1 or COL5a2 genes. This study investigated the roles of collagen V in establishing structure and function in uninjured patellar tendons as well as in the injury response using a Col5a1(+/-) mouse, a model for classic EDS. These analyses were done comparing tendons from a classic EDS model (Col5a1(+/-) ) with wild-type controls...
April 7, 2017: Journal of Orthopaedic Research: Official Publication of the Orthopaedic Research Society
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