Recently it has been reported that the molecular size of decorin dermatan sulfate (DS) was increased in healing skin after hapten application and that the elongated DS was distributed in enlarged interfibrillar space among thin collagen fibrils in situ. Here we show that such modulation of the length of decorin DS is temporary. Although the size of decorin DS was evidently increased on day 15, it decreased to almost normal size on day 35 when the altered disaccharide composition of DS was also recovered. Electron microscopic observation revealed that elongated decorin DS was localized among thin collagen fibrils packed loosely in hapten-treated skin on day 15. In contrast, decorin DS of normal size was distributed among thick collagen fibrils packed tightly on day 35. These results suggest that size control of decorin DS plays important roles in organization of collagen fibrils into bundles by regulating interfibrillar space in healing skin, particularly in maturation of collagen fibrils through shortening of decorin DS in later stages of healing.
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http://dx.doi.org/10.1016/s0923-1811(02)00023-3 | DOI Listing |
Sci Rep
December 2024
Department of Chemistry and Biochemistry, Northern Arizona University, Flagstaff, AZ, USA.
Idiopathic pulmonary fibrosis (IPF) is a fatal disease defined by a progressive decline in lung function due to scarring and accumulation of extracellular matrix (ECM) proteins. The SOCS (Suppressor Of Cytokine Signaling) domain is a 40 amino acid conserved domain known to form a functional ubiquitin ligase complex targeting the Von Hippel Lindau (VHL) protein for proteasomal degradation. Here we show that the SOCS conserved domain operates as a molecular tool, to disrupt collagen and fibronectin fibrils in the ECM associated with fibrotic lung myofibroblasts.
View Article and Find Full Text PDFPurpose: Using a thin semitendinosus tendon as an autograft is a risk factor for poor clinical outcomes after anterior cruciate ligament reconstruction. Preoperative evaluation of the cross-sectional area of the semitendinosus tendon using magnetic resonance imaging is useful. However, studies comparing the cross-sectional area of the semitendinosus tendon on magnetic resonance imaging and the collagen fibril diameter of the semitendinosus tendon are lacking.
View Article and Find Full Text PDFBiomimetics (Basel)
December 2024
Center for Advanced Eye Care, Vero Beach, FL 32960, USA.
We have compared the biomechanical properties of human and porcine corneas using vibrational optical coherence tomography (VOCT). The elastic modulus of the cornea has been previously reported in the literature to vary from about several kPa to more than several GPa based on the results of different techniques. In addition, the formation of corneal cones near the central cornea in keratoconus has been observed in the clinic.
View Article and Find Full Text PDFBiomech Model Mechanobiol
December 2024
Department of Biomedical Engineering, Virginia Commonwealth University, 401 W. Main St., Richmond, VA, 23284, USA.
Embryonic development, wound healing, and organogenesis all require assembly of the extracellular matrix protein fibronectin (FN) into insoluble, viscoelastic fibrils. FN fibrils mediate cell migration, force generation, angiogenic sprouting, and collagen deposition. While the critical role of FN fibrils has long been appreciated, we still have an extremely poor understanding of their mechanical properties and how these mechanical properties facilitate cellular responses.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Department of Civil Engineering, National Taiwan University, Taipei 106, Taiwan; Department of Biomedical Engineering, National Taiwan University, Taipei 106, Taiwan. Electronic address:
Collagen plays a crucial role in human bodies and has a significant presence in connective tissues. As such, the impact of collagen mutations can be devastating. Osteogenesis imperfecta (OI), a rare genetic disease affecting 1 in every 15,000 to 20,000 people, is one such example characterized by brittle bones.
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