Collagen fibrils in the odontoblast layer of the rat incisor by scanning electron microscopy using the maceration method

1994 ◽  
Vol 239 (4) ◽  
pp. 360-370 ◽  
Author(s):  
Shoji Tabata ◽  
Tsuguhiro Nakayama ◽  
Kimitake Funakoshi ◽  
Kinya Yasui ◽  
Kaoru Wada ◽  
...  
1995 ◽  
Vol 104 (6) ◽  
pp. 463-468 ◽  
Author(s):  
Yoshihumi Uno ◽  
Ryusuke Satto

The detailed mechanism of bone resorption in cholesteatoma was investigated by means of eroded ossicles obtained during middle ear surgery for cholesteatoma. In the light microscopic study, multinucleate osteoclasts with ruffled borders were found in contact with the eroded bone, which appeared to be osteoclastic lacunae. Scanning electron microscopy revealed the lacunae to be many absorption bays, 30 to 100 μm in diameter, clustered on the surface of eroded areas. Numerous cone-shaped stubs of digested collagen fiber bundles, consisting of scores of collagen fibrils and degenerated extracellular organic substances, were visible at higher magnification on the bottom of the absorption bay. The pattern of fusion and twining of the disarranged collagen fibrils at the top of the partly digested fiber bundles was clearly rendered by the alkali-water maceration method for scanning electron microscopy. We infer from the morphological evidence that osteoclastic resorption may be one of the major mechanisms of bone destruction in cholesteatoma, and that demineralization and degeneration of extracellular organic substances precede disruption of collagen fibrils at the front of bone resorption.


2016 ◽  
Vol 3 (4) ◽  
pp. e54
Author(s):  
Yehe Liu ◽  
Nelly Andarawis-Puri ◽  
Steven J. Eppell

 A new method is presented to extract collagen fibrils from mammalian tendon tissue. Mammalian tendons are treated with a trypsin-based extraction medium and gently separated with tweezers in an aqueous solution. Collagen fibrils released in the solution are imaged using both dark-field light microscopy and scanning electron microscopy. The method successfully extracts isolated fibrils from rat tail and patellar tendons. To examine whether the method is likely to damage fibrils during extraction, sea cucumber dermis fibril lengths are compared against those obtained using only distilled water. The two methods produce fibrils of similar lengths. This is contrasted with fibrils being shortened when extracted using a tissue homogenizer. Scanning electron microscopy shows the new method preserves D-banding features on fibril surfaces and that fibril diameter does not vary substantially compared with water extracted fibrils. 


1995 ◽  
Vol 72 (5) ◽  
pp. 265-275 ◽  
Author(s):  
Yasutomo IWAI-LIAO ◽  
Yoshikage HIGASHI ◽  
Takeshi SANKOUJI ◽  
Tokio NONAKA ◽  
Hideaki HORI

1983 ◽  
Vol 28 (3) ◽  
pp. 283-285 ◽  
Author(s):  
K. Yamamoto ◽  
T. Nishimoto ◽  
S. Matsuo ◽  
S. Wakisaka ◽  
T. Nakata ◽  
...  

2015 ◽  
Vol 67 (3) ◽  
pp. 741-746 ◽  
Author(s):  
A.P.C. Silva ◽  
J.P.S. Mol ◽  
C.A. Carvalho Junior ◽  
T.A. Paixão ◽  
R.L. Santos

Dermatosparaxis is a genetic disease that affects collagen maturation. This disease is characterized by marked impairment of the resistance of collagen fibers that leads to skin fragility, and it may affect several species. This is the first report of dermatosparaxis in sheep in Brazil. Clinically, two White Dorper lambs had multiple skin lacerations in the neck, dorsum and limbs. Transmission microscopy demonstrated irregular collagen fibers arranged in hieroglyphic shape and scanning electron microscopy demonstrated thin collagen fibrils that were not arranged in bundles as observed in the normal dermis. These findings are consistent with the diagnosis of dermatosparaxis.


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