Intermolecular crosslinking and stereospecific molecular packing in type I collagen fibrils of the periodontal ligament

Biochemistry ◽  
1986 ◽  
Vol 25 (17) ◽  
pp. 4907-4913 ◽  
Author(s):  
Mitsuo Yamauchi ◽  
Elton P. Katz ◽  
Gerald L. Mechanic
Keyword(s):  
Periodontal Ligament ◽  
Type I Collagen ◽  
Molecular Packing ◽  
Collagen Fibrils ◽  
Type I ◽  
Intermolecular Crosslinking

Molecular packing in type I collagen fibrils

1987 ◽  
Vol 193 (1) ◽  
pp. 115-125 ◽  
Author(s):  
R.D.B. Fraser ◽  
T.P. MacRae ◽  
A. Miller
Keyword(s):  
Type I Collagen ◽  
Molecular Packing ◽  
Collagen Fibrils ◽  
Type I

scholarly journals Autophagy facilitates type I collagen synthesis in periodontal ligament cells

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Tomomi Nakamura ◽  
Motozo Yamashita ◽  
Kuniko Ikegami ◽  
Mio Suzuki ◽  
Manabu Yanagita ◽  
...  
Keyword(s):  
Periodontal Ligament ◽  
Collagen Synthesis ◽  
Type I Collagen ◽  
Periodontal Diseases ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Physiological Role ◽  
Type I ◽  
Periodontal Tissue ◽  
Pdl Cells

AbstractAutophagy is a lysosomal protein degradation system in which the cell self-digests its intracellular protein components and organelles. Defects in autophagy contribute to the pathogenesis of age-related chronic diseases, such as myocardial infarction and rheumatoid arthritis, through defects in the extracellular matrix (ECM). However, little is known about autophagy in periodontal diseases characterised by the breakdown of periodontal tissue. Tooth-supportive periodontal ligament (PDL) tissue contains PDL cells that produce various ECM proteins such as collagen to maintain homeostasis in periodontal tissue. In this study, we aimed to clarify the physiological role of autophagy in periodontal tissue. We found that autophagy regulated type I collagen synthesis by elimination of misfolded proteins in human PDL (HPDL) cells. Inhibition of autophagy by E-64d and pepstatin A (PSA) or siATG5 treatment suppressed collagen production in HPDL cells at mRNA and protein levels. Immunoelectron microscopy revealed collagen fragments in autolysosomes. Accumulation of misfolded collagen in HPDL cells was confirmed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis. E-64d and PSA treatment suppressed and rapamycin treatment accelerated the hard tissue-forming ability of HPDL cells. Our findings suggest that autophagy is a crucial regulatory process that facilitates type I collagen synthesis and partly regulates osteoblastic differentiation of PDL cells.

scholarly journals Thermal (In)Stability of Type I Collagen Fibrils

2009 ◽  
Vol 102 (4) ◽  
Author(s):  
S. G. Gevorkian ◽  
A. E. Allahverdyan ◽  
D. S. Gevorgyan ◽  
A. L. Simonian
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I

Detection of type I collagen fibrils formation and dissociation by a fluorescence method based on thioflavin T

2016 ◽  
Vol 92 ◽  
pp. 1175-1182 ◽  
Author(s):  
Meilian Zou ◽  
Huan Yang ◽  
Haibo Wang ◽  
Haiyin Wang ◽  
Juntao Zhang ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Fluorescence Method ◽  
Thioflavin T ◽  
Type I

scholarly journals Mechanical Properties of Native and Cross-linked Type I Collagen Fibrils

2008 ◽  
Vol 94 (6) ◽  
pp. 2204-2211 ◽  
Author(s):  
Lanti Yang ◽  
Kees O. van der Werf ◽  
Carel F.C. Fitié ◽  
Martin L. Bennink ◽  
Pieter J. Dijkstra ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I

The ultrastructure of type I collagen at nanoscale: large or small D-spacing distribution?

Nanoscale ◽  
2014 ◽  
Vol 6 (14) ◽  
pp. 8134-8139 ◽  
Author(s):  
Hai-Nan Su ◽  
Li-Yuan Ran ◽  
Zhi-Hua Chen ◽  
Qi-Long Qin ◽  
Mei Shi ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I ◽  
Spacing Distribution ◽  
Large Distribution

The large distribution ofD-spacing values of type I collagen fibrils was due to image drift during measurement, and theD-spacing values were nearly identical both within a single fibril bundle and in different fibril bundles, exhibiting only a narrow distribution of 2.5 nm.

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.

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