In situ localization of lectin-binding glycoconjugates in the matrix of growth-plate cartilage

1986 ◽  
Vol 176 (1) ◽  
pp. 65-82 ◽  
Author(s):  
Cornelia E. Farnum ◽  
Norman J. Wilsman
Keyword(s):  
Growth Plate ◽  
Lectin Binding ◽  
Growth Plate Cartilage ◽  
The Matrix

scholarly journals Lectin-binding histochemistry of non-decalcified growth plate cartilage: a postembedment method for light microscopy of epon-embedded tissue.

1984 ◽  
Vol 32 (6) ◽  
pp. 593-607 ◽  
Author(s):  
C E Farnum ◽  
N J Wilsman
Keyword(s):  
Growth Plate ◽  
Morphological Analysis ◽  
Lectin Binding ◽  
Direct Methods ◽  
Miniature Swine ◽  
Double Labeling ◽  
Indirect Methods ◽  
Growth Plate Cartilage ◽  
Disease States ◽  
Intracellular Binding

A postembedment method for the localization of lectin-binding glycoconjugates was developed using Epon-embedded growth plate cartilage from Yucatan miniature swine. By testing a variety of etching, blocking, and incubation procedures, a standard protocol was developed for 1 micron thick sections that allowed visualization of both intracellular and extracellular glycoconjugates with affinity for wheat germ agglutinin and concanavalin A. Both fluorescent and peroxidase techniques were used, and comparisons were made between direct methods and indirect methods using the biotin-avidin bridging system. Differential extracellular lectin binding allowed visualization of interterritorial , territorial, and pericellular matrices. Double labeling experiments showed the precision with which intracellular binding could be localized to specific cytoplasmic compartments, with resolution of binding to the Golgi apparatus, endoplasmic reticulum, and nuclear membrane at the light microscopic level. This method allows the localization of both intracellular and extracellular lectin-binding glycoconjugates using fixation and embedment procedures that are compatible with simultaneous ultrastructural analysis. As such it should have applicability both to the morphological analysis of growth plate organization during normal endochondral ossification, as well as to the diagnostic pathology of matrix abnormalities in disease states of growing cartilage.

scholarly journals Preclinical Studies on Mesenchymal Stem Cell-Based Therapy for Growth Plate Cartilage Injury Repair

2011 ◽  
Vol 2011 ◽  
pp. 1-10 ◽  
Author(s):  
Rosa Chung ◽  
Bruce K. Foster ◽  
Cory J. Xian
Keyword(s):  
Stem Cell ◽  
Mesenchymal Stem Cell ◽  
Growth Plate ◽  
Disease Transmission ◽  
Ex Vivo ◽  
Large Animal ◽  
Growth Plate Cartilage ◽  
Large Animal Models ◽  
Cell Based Therapy

In the last two decades, there has been a strong interest in searching for biological treatments for regeneration of injured growth plate cartilage and prevention of its bony repair. Various means have been tried, including implantation of chondrocytes, mesenchymal stem cell (MSC), together with exogenous growth factor and scaffolds, and gene therapy. However, with the lack of success with chondrocytes, more research has focussed on MSC-based treatments. In addition to circumvent limitations with MSC-based treatments (including cell harvest-associated morbidity, difficulties/time/cost involved in MSC isolation andex vivoexpansion, and potential disease transmission), mobilising endogenous MSCs to the growth plate injury site and enhancingin situregeneration mechanisms would represent an alternative attractive approach. Further studies are required to investigate the potential particularly in large animal models or clinical setting of theex vivoMSC approach and the feasibility of the endogenous MSCin situapproach in growth plate regeneration.

Quantification and immunolocalisation of porcine articular and growth plate cartilage collagens

1993 ◽  
Vol 105 (4) ◽  
pp. 975-984 ◽  
Author(s):  
R.J. Wardale ◽  
V.C. Duance
Keyword(s):  
Articular Cartilage ◽  
Growth Plate ◽  
Type I Collagen ◽  
Articular Surface ◽  
Dry Weight ◽  
Type I ◽  
Collagen Types ◽  
Growth Plate Cartilage ◽  
The Matrix ◽  
Cross Links

The collagens of growth plate and articular cartilage from 5–6 month old commercial pigs were characterised. Growth plate cartilage was found to contain less total collagen than articular cartilage as a proportion of the dry weight. Collagen types I, II, VI, IX and XI are present in both growth plate and articular cartilage whereas type X is found exclusively in growth plate cartilage. Types III and V collagen could not be detected in either cartilage. Type I collagen makes up at least 10% of the collagenous component of both cartilages. There are significant differences in the ratios of the quantifiable collagen types between growth plate and articular cartilage. Collagen types I, II, and XI were less readily extracted from growth plate than from articular cartilage following pepsin treatment, although growth plate cartilage contains less of the mature collagen cross-links, hydroxylysyl-pyridinoline and lysyl-pyridinoline. Both cartilages contain significant amounts of the divalent reducible collagen cross-links, hydroxylysyl-ketonorleucine and dehydro-hydroxylysinonorleucine. Immunofluorescent localisation indicated that type I collagen is located predominantly at the surface of articular cartilage but is distributed throughout the matrix in growth plate. Types II and XI are located in the matrix of both cartilages whereas type IX is predominantly pericellular in the calcifying region of articular cartilage and the hypertrophic region of the growth plate. Collagen type VI is located primarily as a diffuse area at the articular surface.

In Situ Levels of Intracellular Ca2+ and pH in Avian Growth Plate Cartilage

1997 ◽  
Vol 335 ◽  
pp. 310-324 ◽  
Author(s):  
Licia N.Y. Wu ◽  
Melissa G. Wuthier ◽  
Brian R. Genge ◽  
Roy E. Wuthier
Keyword(s):  
Growth Plate ◽  
Growth Plate Cartilage

Effects of the FGF2 aptamer on growth plate cartilage development of achondroplasia patient-specific iPS cells in a xenograft model

2019 ◽  
Author(s):  
Takeshi Kimura ◽  
Kie Yasuda ◽  
Yukako Nakano ◽  
Shinji Takeyari ◽  
Yasuji Kitabatake ◽  
...  
Keyword(s):  
Growth Plate ◽  
Xenograft Model ◽  
Ips Cells ◽  
Patient Specific ◽  
Growth Plate Cartilage ◽  
Cartilage Development

scholarly journals Supramolecular ionic polymer/carbon nanotube composite hydrogels with enhanced electromechanical performance

2020 ◽  
Vol 9 (1) ◽  
pp. 478-488 ◽  
Author(s):  
Yun-Fei Zhang ◽  
Fei-Peng Du ◽  
Ling Chen ◽  
Ka-Wai Yeung ◽  
Yuqing Dong ◽  
...  
Keyword(s):  
Carbon Nanotube ◽  
Ion Mobility ◽  
Artificial Muscles ◽  
Ionic Polymer ◽  
Composite Hydrogels ◽  
The Matrix ◽  
Electromechanical Performance ◽  
Carbon Nanotube Composite ◽  
Robotic Devices

AbstractElectroactive hydrogels have received increasing attention due to the possibility of being used in biomimetics, such as for soft robotics and artificial muscles. However, the applications are hindered by the poor mechanical properties and slow response time. To address these issues, in this study, supramolecular ionic polymer–carbon nanotube (SIPC) composite hydrogels were fabricated via in situ free radical polymerization. The polymer matrix consisted of carbon nanotubes (CNTs), styrene sulfonic sodium (SSNa), β-cyclodextrin (β-CD)-grafted acrylamide, and ferrocene (Fc)-grafted acrylamide, with the incorporation of SSNa serving as the ionic source. On applying an external voltage, the ions accumulate on one side of the matrix, leading to localized swelling and bending of the structure. Therefore, a controllable and reversible actuation can be achieved by changing the applied voltage. The tensile strength of the SIPC was improved by over 300%, from 12 to 49 kPa, due to the reinforcement effect of the CNTs and the supramolecular host–guest interactions between the β-CD and Fc moieties. The inclusion of CNTs not only improved the tensile properties but also enhanced the ion mobility, which lead to a faster electromechanical response. The presented electro-responsive composite hydrogel shows a high potential for the development of robotic devices and soft smart components for sensing and actuating applications.

scholarly journals In situ structure and organization of the influenza C virus surface glycoprotein

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Steinar Halldorsson ◽  
Kasim Sader ◽  
Jack Turner ◽  
Lesley J. Calder ◽  
Peter B. Rosenthal
Keyword(s):  
Membrane Fusion ◽  
Hexagonal Lattice ◽  
Surface Glycoprotein ◽  
Structural Basis ◽  
Virus Surface ◽  
The Matrix ◽  
Influenza C Virus ◽  
Subtomogram Averaging ◽  
Electron Cryotomography

AbstractThe lipid-enveloped influenza C virus contains a single surface glycoprotein, the haemagglutinin-esterase-fusion (HEF) protein, that mediates receptor binding, receptor destruction, and membrane fusion at the low pH of the endosome. Here we apply electron cryotomography and subtomogram averaging to describe the structural basis for hexagonal lattice formation by HEF on the viral surface. The conformation of the glycoprotein in situ is distinct from the structure of the isolated trimeric ectodomain, showing that a splaying of the membrane distal domains is required to mediate contacts that form the lattice. The splaying of these domains is also coupled to changes in the structure of the stem region which is involved in membrane fusion, thereby linking HEF’s membrane fusion conformation with its assembly on the virus surface. The glycoprotein lattice can form independent of other virion components but we show a major role for the matrix layer in particle formation.

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