scholarly journals Highly sensitive single-fibril erosion assay demonstrates mechanochemical switch in native collagen fibrils

2012 ◽  
Vol 12 (2) ◽  
pp. 291-300 ◽  
Author(s):  
Brendan P. Flynn ◽  
Graham E. Tilburey ◽  
Jeffrey W. Ruberti
Keyword(s):  
Collagen Fibrils ◽  
Highly Sensitive ◽  
Native Collagen

scholarly journals Erratum to: Highly sensitive single-fibril erosion assay demonstrates mechanochemical switch in native collagen fibrils

2013 ◽  
Vol 12 (4) ◽  
pp. 847-847
Author(s):  
Brendan P. Flynn ◽  
Graham E. Tilburey ◽  
Jeffrey W. Ruberti
Keyword(s):  
Collagen Fibrils ◽  
Highly Sensitive ◽  
Native Collagen

Banded Structures in the Connective Tissue of Meningioma

1976 ◽  
Vol 34 ◽  
pp. 234-235
Author(s):  
C. N. Sun ◽  
H. J. White
Keyword(s):  
Connective Tissue ◽  
Osmium Tetroxide ◽  
Uranyl Acetate ◽  
Collagen Fibrils ◽  
Lead Citrate ◽  
Connective Tissues ◽  
Native Collagen ◽  
Routine Procedures

Previously, we have reported on extracellular cross-striated banded structures in human connective tissues of a variety of organs (1). Since then, more material has been examined and other techniques applied. Recently, we studied a fibrocytic meningioma of the falx. After the specimen was fixed in 4% buffered glutaraldehyde and post-fixed in 1% buffered osmium tetroxide, other routine procedures were followed for embedding in Epon 812. Sections were stained with uranyl acetate and lead citrate. There were numerous cross striated banded structures in aggregated bundle forms found in the connecfive tissue of the tumor. The banded material has a periodicity of about 450 Å and where it assumes a filamentous arrangement, appears to be about 800 Å in diameter. In comparison with the vicinal native collagen fibrils, the banded material Is sometimes about twice the diameter of native collagen.

scholarly journals Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction

Materials ◽  
2020 ◽  
Vol 13 (2) ◽  
pp. 358 ◽  
Author(s):  
Haiyan Ju ◽  
Xiuying Liu ◽  
Gang Zhang ◽  
Dezheng Liu ◽  
Yongsheng Yang
Keyword(s):  
Type I Collagen ◽  
Structural Characteristics ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Dry Weight ◽  
Collagen Fibrils ◽  
Type I ◽  
X Ray Diffraction ◽  
Aggregation Structure ◽  
Native Collagen

Native collagen fibrils (CF) were successfully extracted from bovine tendons using two different methods: modified acid-solubilized extraction for A-CF and pepsin-aided method for P-CF. The yields of A-CF and P-CF were up to 64.91% (±1.07% SD) and 56.78% (±1.22% SD) (dry weight basis), respectively. The analyses of both amino acid composition and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed that A-CF and P-CF were type I collagen fibrils. Both A-CF and P-CF retained the intact crystallinity and integrity of type I collagen’s natural structure by FTIR spectra, circular dichroism spectroscopy (CD) and X-ray diffraction detection. The aggregation structures of A-CF and P-CF were displayed by UV–Vis. However, A-CF showed more intact aggregation structure than P-CF. Microstructure and D-periodicities of A-CF and P-CF were observed (SEM and TEM). The diameters of A-CF and P-CF are about 386 and 282 nm, respectively. Although both A-CF and P-CF were theoretically concordant with the Schmitt hypothesis, A-CF was of evener thickness and higher integrity in terms of aggregation structure than P-CF. Modified acid-solubilized method provides a potential non-enzyme alternative to extract native collagen fibrils with uniform thickness and integral aggregation structure.

Determination of the elastic modulus of native collagen fibrils via radial indentation

2006 ◽  
Vol 89 (18) ◽  
pp. 181902 ◽  
Author(s):  
August J. Heim ◽  
William G. Matthews ◽  
Thomas J. Koob
Keyword(s):  
Elastic Modulus ◽  
Collagen Fibrils ◽  
Native Collagen

Effect of Glutaraldehyde on Properties of Membranes Prepared from Fish Scale Collagen

2012 ◽  
Vol 1418 ◽  
Author(s):  
Zhefeng Xu ◽  
Toshiyuki Ikoma ◽  
Tomohiko Yoshioka ◽  
Motohiro Tagaya ◽  
Satoshi Motozuka ◽  
...  
Keyword(s):  
Mechanical Property ◽  
Tensile Strength ◽  
Free Amino ◽  
Collagen Fibrils ◽  
Type I ◽  
Fish Scale ◽  
Amino Groups ◽  
High Mechanical Property ◽  
Crosslinking Degree ◽  
Native Collagen

ABSTRACTCollagen fibril membranes (CFMs) with a high mechanical property were fabricated with a lateral face evaporation method, in which type I atelocollagen extracted from tilapia scales was used. The density and thickness of the CFM obtained were 0.51 ± 0.04 mg/cm3 and 50 ± 5 μm. The collagen fibrils in the CFM had a similar periodic stripped pattern of 67 nm with native collagen fibrils. The CFM was crosslinked in gaseous glutaraldehyde for different duration in order to increase the mechanical property. The crosslinking degrees of the CFMs analyzed by free amino groups gradually increased to 70.3 % against the exposure duration until 6 hours, and reached a plateau. The denaturation temperatures of the CFMs with the crosslinking degrees at 20.4 % to 43% were linearly increased from 49°C to 75°C. The tensile strength of the CFMs was slightly improved until the crosslinking degree at 33.3 % and then the tensile strength rapidly increased to be 68 MPa. It was suggested that a percolation phenomenon took place in the CFMs by crosslinking of collagen fibrils with polymerized GA molecules.

scholarly journals Identifying distinct nanoscopic features of native collagen fibrils towards early diagnosis of pelvic organ prolapse

2016 ◽  
Vol 12 (3) ◽  
pp. 667-675 ◽  
Author(s):  
Taeyoung Kim ◽  
Indumathi Sridharan ◽  
Yin Ma ◽  
Bofan Zhu ◽  
Naiwei Chi ◽  
...  
Keyword(s):  
Pelvic Organ Prolapse ◽  
Early Diagnosis ◽  
Pelvic Organ ◽  
Collagen Fibrils ◽  
Native Collagen

Electron Microscopy of Wound Healing in Patients with Hernia

1975 ◽  
Vol 33 ◽  
pp. 352-353
Author(s):  
C.N. Sun ◽  
H.J. White ◽  
R.C. Read
Keyword(s):  
Electron Microscopy ◽  
Wound Healing ◽  
Phosphate Buffer ◽  
Osmium Tetroxide ◽  
Phosphotungstic Acid ◽  
Rectus Sheath ◽  
Uranyl Acetate ◽  
Collagen Fibrils ◽  
Lead Citrate ◽  
Native Collagen

Previously we have reported the defect of collagen fibrils from herniated rectus sheath. This presentation includes additional sections from postsurgical incisions (10 days) from both control and hernia patients. Small pieces of rectus sheath were fixed in 3% glutaraldehyde in phosphate buffer (pH 7.2) and post fixed with buffered 2% osmium tetroxide. The tissues were then dehydrated in serially increasing concentrations of alcohol and embedded in Epon 812. Sections were stained with 2.5% phosphotungstic acid or uranyl acetate and lead citrate.Previously we found that collagen fibrils from "non-herniated" rectus sheath have uniform diameters and 640 Å periodicity with seven or more intraperiodic bands resembling typical native collagen fibrils, while the fibrils from fascia obtained from patients with direct herniation show considerable variation in diameter. These variations are often found in the same individual fibers with a range from 300 Å to 3000 Å.

scholarly journals Supramolecular structure of polymorphic collagen fibrils.

1976 ◽  
Vol 68 (3) ◽  
pp. 521-538 ◽  
Author(s):  
R R Bruns
Keyword(s):  
Electron Microscopy ◽  
Banding Pattern ◽  
Collagen Fibrils ◽  
Graphic Method ◽  
Interaction Sites ◽  
Symmetrical Pattern ◽  
Native Collagen ◽  
Major Period ◽  
Polymorphic Forms ◽  
Specific Band

Reconstituted cartilage collagen fibrils with an oblique banding pattern or with two types of symmetrical patterns, and reconstituted rattail tendon fibrils with a third type of symmetrical pattern were examined by electron microscopy and found to consist of narrow subfibrils having native-type cross-striations. Analysis of the four types of patterns by a graphic method of specific band matching revealed the orientation and axial relation of individual subfibrils and their component molecules. In fibrils with an oblique pattern, subfibrils have the same orientation and a regular 100A axial displacement. Observations on staining characteristics, folded fibrils, and transverse sections of embedded fibrils suggest that the obliquely banded fibrils are ribbonlike or layered structures. In the three types of fibrils with a symmetrical pattern, adjacent subfibrils are oppositely oriented and aligned within a 119-A segment of the 670-A major period. Considered together, the observations suggest that interaction sites on the surface of subfibrils (and perhaps on the surface of native collagen fibrils) occur in various patterns that are manifested accouding to the nature of the environment during fibril formation, and that such patterns can be mapped on the surface of subfibrils by noting the arrangement of subfibrils in polymorphic forms.

Cell growth improvement on the poly (lactic acid) surface with spray deposited separate native collagen fibrils

2019 ◽  
Author(s):  
Yury A. Polikarpov ◽  
Alexey V. Romashkin ◽  
Denis D. Levin ◽  
Nikolay S. Struchkov ◽  
Vladimir A. Petukhov ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Cell Growth ◽  
Collagen Fibrils ◽  
Poly Lactic Acid ◽  
Native Collagen

Native collagen fibrils from echinoderms are molecularly bipolar

1994 ◽  
Vol 235 (1) ◽  
pp. 73-79 ◽  
Author(s):  
F.A. Thurmond ◽  
J.A. Trotter
Keyword(s):  
Collagen Fibrils ◽  
Native Collagen
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