Electron microscopy of the collagen fibril

1984 ◽  
pp. 1-33 ◽  
Author(s):  
John A. Chapman ◽  
David J. S. Hulmes
Keyword(s):  
Electron Microscopy ◽  
Collagen Fibril

A Novel, Label-Free Method for Quantifying Collagen Fibril Formation and Degradation Using DIC Microscopy, Electromagnetic Wave Theory, and Image Processing

2009 ◽  
Author(s):  
Brendan P. Flynn ◽  
Amit Bhole ◽  
Charles DiMarzio ◽  
Jeffrey W. Ruberti
Keyword(s):  
Electron Microscopy ◽  
Image Processing ◽  
Electromagnetic Wave ◽  
Collagen Fibril ◽  
Reaction Rate ◽  
Wave Theory ◽  
Label Free ◽  
Averaging Methods ◽  
Rate Kinetics ◽  
Dic Microscopy

Methods to assay fibrillar growth and degradation at sub-light scales include: fluorescence assays using FITC-collagen or FRAP, destructive preparation and measurement using electron microscopy, and light occlusion methods including turbidity and absorption methods. Many of these methods require the outright destruction, or at least modification via labelling, of the sample in question. This requirement can slow experimentation and introduce additional variability or even alter the reaction rate kinetics. The two methods (absorption and turbidity) which are label-free are bulk averaging methods and cannot isolate subsets of fibrils (e.g. fibrils under load).

Collagen Characteristics and Organization during the Progression of Cholesterol-Induced Atherosclerosis in Japanese Quail

2001 ◽  
Vol 226 (4) ◽  
pp. 328-333 ◽  
Author(s):  
Sandra G. Velleman ◽  
Richard J. McCormick ◽  
Daniel Ely ◽  
Bradley B. Jarrold ◽  
Ruthi A. Patterson ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Blood Pressure ◽  
Transmission Electron Microscopy ◽  
Extracellular Matrix ◽  
Systolic Blood Pressure ◽  
Japanese Quail ◽  
Collagen Fibril ◽  
Cholesterol Feeding ◽  
Transmission Electron ◽  
Progression Of Atherosclerosis

This study reports the concentration of collagen and its hydroxypyridinoline crosslinks, collagen fibril organization in the dorsal aortas, and systolic blood pressure during the progression of atherosclerosis in Japanese quail selected for cholesterol-induced atherosclerosis. The quail were placed on either a control or 0.5% cholesterol-added diet at approximately 16 weeks of age. The concentration of total collagen did not change in the control arteries during the course of the study, whereas at 5 and 10 weeks of cholesterol feeding, collagen levels decreased in the cholesterol-fed birds. Hydroxypyridinoline concentration increased during the duration of the study in the cholesterol-fed birds and by 15 and 20 weeks of cholesterol feeding, levels were significantly increased over those observed in the control arteries. Transmission electron microscopy showed changes in the organization of collagen fibrils. Increased systolic blood pressure was noted beginning at 10 weeks of cholesterol feeding, which is suggestive of other systemic changes induced by hypercholesterolemia. These results demonstrated remodeling of the collagen component of the dorsal aorta extracellular matrix during the progression of atherosclerosis and are suggestive of other systemic cardiovascular system changes.

scholarly journals Extracellular compartments in matrix morphogenesis: collagen fibril, bundle, and lamellar formation by corneal fibroblasts.

1984 ◽  
Vol 99 (6) ◽  
pp. 2024-2033 ◽  
Author(s):  
D E Birk ◽  
R L Trelstad
Keyword(s):  
Electron Microscopy ◽  
Cell Surface ◽  
High Voltage ◽  
Collagen Fibril ◽  
Corneal Stroma ◽  
Collagen Fibrils ◽  
High Voltage Electron Microscopy ◽  
Voltage Electron ◽  
High Voltage Electron ◽  
Corneal Fibroblasts

The regulation of collagen fibril, bundle, and lamella formation by the corneal fibroblasts, as well as the organization of these elements into an orthogonal stroma, was studied by transmission electron microscopy and high voltage electron microscopy. Transmission and high voltage electron microscopy of chick embryo corneas each demonstrated a series of unique extracellular compartments. Collagen fibrillogenesis occurred within small surface recesses. These small recesses usually contained between 5 and 12 collagen fibrils with typically mature diameters and constant intrafibrillar spacing. The lateral fusion of the recesses resulted in larger recesses and consequent formation of prominent cell surface foldings. Within these surface foldings, bundles that contained 50-100 collagen fibrils were formed. The surface foldings continued to fuse and the cell surface retracted, forming large surface-associated compartments in which bundles coalesced to form lamellae. High voltage electron microscopy of 0.5 micron sections cut parallel to the corneal surface revealed that the corneal fibroblasts and their processes had two major axes at approximately right angles to one another. The surface compartments involved in the production of the corneal stroma were aligned along the fibroblast axes and the orthogonality of the cell was in register with that of the extracellular matrix. In this manner, corneal fibroblasts formed collagen fibrils, bundles, and lamellae within a controlled environment and thereby determined the architecture of the corneal stroma by the configuration of the cell and its associated compartments.

scholarly journals Electron microscopy shows periodic structure in collagen fibril cross sections.

1981 ◽  
Vol 78 (6) ◽  
pp. 3567-3571 ◽  
Author(s):  
D. J. Hulmes ◽  
J. C. Jesior ◽  
A. Miller ◽  
C. Berthet-Colominas ◽  
C. Wolff
Keyword(s):  
Electron Microscopy ◽  
Periodic Structure ◽  
Cross Sections ◽  
Collagen Fibril

scholarly journals Collagen Fibril Ultrastructure in Mice Lacking Discoidin Domain Receptor 1

2016 ◽  
Vol 22 (3) ◽  
pp. 599-611 ◽  
Author(s):  
Jeffrey R. Tonniges ◽  
Benjamin Albert ◽  
Edward P. Calomeni ◽  
Shuvro Roy ◽  
Joan Lee ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Collagen Fibril ◽  
Collagen Fibrils ◽  
Collagen Deposition ◽  
Knock Out ◽  
Discoidin Domain Receptor ◽  
Transmission Electron ◽  
Fibril Diameter ◽  
Discoidin Domain Receptor 1

AbstractThe quantity and quality of collagen fibrils in the extracellular matrix (ECM) have a pivotal role in dictating biological processes. Several collagen-binding proteins (CBPs) are known to modulate collagen deposition and fibril diameter. However, limited studies exist on alterations in the fibril ultrastructure by CBPs. In this study, we elucidate how the collagen receptor, discoidin domain receptor 1 (DDR1) regulates the collagen content and ultrastructure in the adventitia of DDR1 knock-out (KO) mice. DDR1 KO mice exhibit increased collagen deposition as observed using Masson’s trichrome. Collagen ultrastructure was evaluated in situ using transmission electron microscopy, scanning electron microscopy, and atomic force microscopy. Although the mean fibril diameter was not significantly different, DDR1 KO mice had a higher percentage of fibrils with larger diameter compared with their wild-type littermates. No significant differences were observed in the length of D-periods. In addition, collagen fibrils from DDR1 KO mice exhibited a small, but statistically significant, increase in the depth of the fibril D-periods. Consistent with these observations, a reduction in the depth of D-periods was observed in collagen fibrils reconstituted with recombinant DDR1-Fc. Our results elucidate how DDR1 modulates collagen fibril ultrastructure in vivo, which may have important consequences in the functional role(s) of the underlying ECM.

scholarly journals Visualization of Collagen–Mineral Arrangement using Atom Probe Tomography

2020 ◽  
Author(s):  
Bryan E.J. Lee ◽  
Brian Langelier ◽  
Kathryn Grandfield
Keyword(s):  
Electron Microscopy ◽  
Atom Probe Tomography ◽  
Collagen Fibril ◽  
Atom Probe ◽  
Rich Phase ◽  
Mineralized Tissues ◽  
Mineralized Collagen Fibril ◽  
Mineralized Collagen

AbstractBone is a complex, hierarchical structure comprised of two distinct phases: the organic, collagen– rich phase and the inorganic mineral–rich phase. This collagen–mineral arrangement has implications for bone function, aging, and disease. However, strategies to extract a single mineralized collagen fibril to investigate the interplay between components with sufficient resolution have been mostly confined to in vitro systems that only approximate the biological environment or transmission electron microscopy studies with lower spatial and chemical resolution. Therefore, there is extensive debate over the location of mineral with respect to collagen in in vivo mineralized tissues as visualization and quantification of the mineral in a living system is difficult or impossible. Herein, we have developed an approach to artificially extract a single mineralized collagen fibril from bone to analyze its composition and structure atom-by-atom with 3D resolution and sub-nanometer accuracy using atom probe tomography. This enables, for the first time, a method to probe fibril-level mineralization and collagen–mineral arrangement from an in vivo system with both the spatial and chemical precision required to comment on collagen– mineral arrangement. Using atom probe tomography, 4D (spatial + chemical) reconstructed volumes of leporine bone were generated with accuracy from correlative scanning electron microscopy. Distinct, winding collagen fibrils were identified with mineralized deposits both encapsulating and incorporated into the collagenous structures. This work demonstrates a novel fibril-level detection method that can be used to probe structural and chemical changes of bone and contribute new insights to the debate on collagen–mineral arrangement in mineralized tissues such as bones, and teeth.

scholarly journals Dermatan Sulfate Epimerase 1-Deficient Mice Have Reduced Content and Changed Distribution of Iduronic Acids in Dermatan Sulfate and an Altered Collagen Structure in Skin

2009 ◽  
Vol 29 (20) ◽  
pp. 5517-5528 ◽  
Author(s):  
Marco Maccarana ◽  
Sebastian Kalamajski ◽  
Mads Kongsgaard ◽  
S. Peter Magnusson ◽  
Åke Oldberg ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Tensile Strength ◽  
Collagen Fibril ◽  
Glucuronic Acid ◽  
Dermatan Sulfate ◽  
Collagen Structure ◽  
Wild Type ◽  
Iduronic Acid ◽  
Skin Collagen ◽  
Deficient Mice

ABSTRACT Dermatan sulfate epimerase 1 (DS-epi1) and DS-epi2 convert glucuronic acid to iduronic acid in chondroitin/dermatan sulfate biosynthesis. Here we report on the generation of DS-epi1-null mice and the resulting alterations in the chondroitin/dermatan polysaccharide chains. The numbers of long blocks of adjacent iduronic acids are greatly decreased in skin decorin and biglycan chondroitin/dermatan sulfate, along with a parallel decrease in iduronic-2-O-sulfated-galactosamine-4-O-sulfated structures. Both iduronic acid blocks and iduronic acids surrounded by glucuronic acids are also decreased in versican-derived chains. DS-epi1-deficient mice are smaller than their wild-type littermates but otherwise have no gross macroscopic alterations. The lack of DS-epi1 affects the chondroitin/dermatan sulfate in many proteoglycans, and the consequences for skin collagen structure were initially analyzed. We found that the skin collagen architecture was altered, and electron microscopy showed that the DS-epi1-null fibrils have a larger diameter than the wild-type fibrils. The altered chondroitin/dermatan sulfate chains carried by decorin in skin are likely to affect collagen fibril formation and reduce the tensile strength of DS-epi1-null skin.

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