scholarly journals Gelation of Sodium-Deoxycholate: Influenced by the Presence of a CorticosteroidBetamethasone-17-Valerate

2017 ◽  
pp. 7-13
Author(s):  
Gokce Evren Homan
Keyword(s):  
2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Naresh Polisetti ◽  
Anke Schmid ◽  
Ursula Schlötzer-Schrehardt ◽  
Philip Maier ◽  
Stefan J. Lang ◽  
...  

AbstractAllogenic transplants of the cornea are prone to rejection, especially in repetitive transplantation and in scarred or highly vascularized recipient sites. Patients with these ailments would particularly benefit from the possibility to use non-immunogenic decellularized tissue scaffolds for transplantation, which may be repopulated by host cells in situ or in vitro. So, the aim of this study was to develop a fast and efficient decellularization method for creating a human corneal extracellular matrix scaffold suitable for repopulation with human cells from the corneal limbus. To decellularize human donor corneas, sodium deoxycholate, deoxyribonuclease I, and dextran were assessed to remove cells and nuclei and to control tissue swelling, respectively. We evaluated the decellularization effects on the ultrastructure, optical, mechanical, and biological properties of the human cornea. Scaffold recellularization was studied using primary human limbal epithelial cells, stromal cells, and melanocytes in vitro and a lamellar transplantation approach ex vivo. Our data strongly suggest that this approach allowed the effective removal of cellular and nuclear material in a very short period of time while preserving extracellular matrix proteins, glycosaminoglycans, tissue structure, and optical transmission properties. In vitro recellularization demonstrated good biocompatibility of the decellularized human cornea and ex vivo transplantation revealed complete epithelialization and stromal repopulation from the host tissue. Thus, the generated decellularized human corneal scaffold could be a promising biological material for anterior corneal reconstruction in the treatment of corneal defects.


2008 ◽  
Vol 68 (5-6) ◽  
pp. 415-419 ◽  
Author(s):  
Wan Aini Wan Ibrahim ◽  
Dadan Hermawan ◽  
Mohamed Noor Hasan ◽  
Hassan Y. Aboul Enein ◽  
M. Marsin Sanagi

1971 ◽  
Vol 17 (7) ◽  
pp. 915-920
Author(s):  
C. Margaret Johnson ◽  
John C. N. Westwood

A comparison of the effect of several different virus disruption procedures on the biological activity and antigenic structure of the Myxovirus influenza A/PR8 virion has shown that sodium deoxycholate was the best disrupting agent. Six virus structural components were detected, of which one was classified as host specific, two were identified as virus specific, and three were found to possess dual specificity. These were classified as host-virus (HV) structural antigens.


2012 ◽  
Vol 20 (7) ◽  
pp. 615-622 ◽  
Author(s):  
Shixiao Jin ◽  
Shanshan Fu ◽  
Jin Han ◽  
Shiying Jin ◽  
Qingyuan Lv ◽  
...  

2003 ◽  
Vol 655 (2) ◽  
pp. 321-330 ◽  
Author(s):  
Y. Sun ◽  
Z.-L. Yang ◽  
L. Zhang ◽  
N.-F. Zhou ◽  
S.-F. Weng ◽  
...  

1985 ◽  
Vol 227 (2) ◽  
pp. 405-412 ◽  
Author(s):  
P W Cheng ◽  
W E Wingert ◽  
M R Little ◽  
R Wei

We have characterized a bovine tracheal mucin beta-6-N-acetylglucosaminyltransferase that catalyses the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to the C-6 of the N-acetylgalactosamine residue of galactosyl-β 1→3-N-acetylgalactosamine. Optimal enzyme activity was obtained between pH 7.5-8.5, at 5mM-MnCl2, and at 0.06-0.08% (v/v) Triton X-100 (or Nonidet P-40), or 0.5-5.0% (v/v) Tween 20. Ba2+, Mg2+ and Ca2+ could partially replace Mn2+, but Co2+, Fe2+, Cd2+ and Zn2+ could not. Sodium dodecyl sulphate, cetylpyridinium chloride, sodium deoxycholate, octyl beta-D-glucoside, digitonin and alkyl alcohols were less effective in enhancing enzyme activity, and dimethyl sulphoxide was ineffective. The apparent Michaelis constants were 1.25 mM for UDP-N-acetylglucosamine, 0.94-3.34 mM for freezing-point-depressing glycoprotein and 0.19 mM for periodate-treated blood-group-A porcine submaxillary mucin. Asialo ovine submaxillary mucin could not serve as the glycosyl acceptor. The structure of the 14C-labelled oligosaccharide obtained by alkaline-borohydride treatment of the product was identified as Gal beta 1→3(Glc-NAc beta 1→6)N-acetylgalactosaminitol by beta-hexosaminidase treatment, gas chromatography-mass spectrometry and 1H-n.m.r. (270 MHz) analysis. The enzyme is important in the regulation of mucin oligosaccharide biosynthesis.


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