Physical and biological properties of a novel anti-adhesion material made of thermally cross-linked gelatin film: Investigation of the usefulness as anti-adhesion material

2017 ◽  
Vol 106 (2) ◽  
pp. 689-696 ◽  
Author(s):  
Tsunehito Horii ◽  
Hiroyuki Tsujimoto ◽  
Hiroe Miyamoto ◽  
Koki Yamanaka ◽  
Shota Tanaka ◽  
...  
2020 ◽  
Vol 31 (6) ◽  
pp. 351-360
Author(s):  
Tsunehito Horii ◽  
Hiroyuki Tsujimoto ◽  
Susumu Kageyama ◽  
Tetsuya Yoshida ◽  
Kenichi Kobayashi ◽  
...  

BACKGROUND: To overcome the unfavorable issues associated with conventional anti-adhesive HA/CMC film, we developed an anti-adhesive thermally cross-linked gelatin film. OBJECTIVE: We tried to clarify the re-attachability of the film and the required properties concerning the film thickness, stiffness and anti-adhesion effect. METHODS: To determine the optimal thickness, 5 kinds of the thickness of gelatin film and the conventional film were analyzed by the tensile test, shearing test, buckling test and tissue injury test. Finally, using the optimal film thickness, we tried to clarify the anti-adhesion effect of the reattached film. RESULTS: The tensile and shearing test showed gelatin films ≥30 μm thick had greater tensile strength and a smaller number of film fractures, than the conventional film. The buckling and tissue injury test showed gelatin films ≥60 μm thick had higher buckling strength and worse injury scores than the conventional film. The anti-adhesive effect of re-attached gelatin film using optimal thickness (30–40 μm) found the anti-adhesion score was significantly better than that of the control. CONCLUSIONS: Provided it has an optimal thickness, gelatin film can be reattached with enough physical strength not to tear, safety stiffness not to induce tissue injury, and a sufficient anti-adhesion effect.


2021 ◽  
Vol 22 (7) ◽  
pp. 3648
Author(s):  
Cristina Romo-Valera ◽  
Pedro Guerrero ◽  
Jon Arluzea ◽  
Jaime Etxebarria ◽  
Koro de la Caba ◽  
...  

The vision impairments suffered by millions of people worldwide and the shortage of corneal donors show the need of substitutes that mimic native tissue to promote cell growth and subsequent tissue regeneration. The current study focused on the in vitro assessment of protein-based biomaterials that could be a potential source for corneal scaffolds. Collagen, soy protein isolate (SPI), and gelatin films cross-linked with lactose or citric acid were prepared and physicochemical, transmittance, and degradation measurements were carried out. In vitro cytotoxicity, cell adhesion, and migration studies were performed with human corneal epithelial (HCE) cells and 3T3 fibroblasts for the films’ cytocompatibility assessment. Transmittance values met the cornea’s needs, and the degradation profile revealed a progressive biomaterials’ decomposition in enzymatic and hydrolytic assays. Cell viability at 72 h was above 70% when exposed to SPI and gelatin films. Live/dead assays and scanning electron microscopy (SEM) analysis demonstrated the adhesion of both cell types to the films, with a similar arrangement to that observed in controls. Besides, both cell lines were able to proliferate and migrate over the films. Without ruling out any material, the appropriate optical and biological properties shown by lactose-crosslinked gelatin film highlight its potential for corneal bioengineering.


Author(s):  
David A. Agard ◽  
Yasushi Hiraoka ◽  
John W. Sedat

In an effort to understand the complex relationship between structure and biological function within the nucleus, we have embarked on a program to examine the three-dimensional structure and organization of Drosophila melanogaster embryonic chromosomes. Our overall goal is to determine how DNA and proteins are organized into complex and highly dynamic structures (chromosomes) and how these chromosomes are arranged in three dimensional space within the cell nucleus. Futher, we hope to be able to correlate structual data with such fundamental biological properties as stage in the mitotic cell cycle, developmental state and transcription at specific gene loci.Towards this end, we have been developing methodologies for the three-dimensional analysis of non-crystalline biological specimens using optical and electron microscopy. We feel that the combination of these two complementary techniques allows an unprecedented look at the structural organization of cellular components ranging in size from 100A to 100 microns.


2015 ◽  
Vol 57 ◽  
pp. 177-187 ◽  
Author(s):  
Jennifer N. Byrum ◽  
William Rodgers

Since the inception of the fluid mosaic model, cell membranes have come to be recognized as heterogeneous structures composed of discrete protein and lipid domains of various dimensions and biological functions. The structural and biological properties of membrane domains are represented by CDM (cholesterol-dependent membrane) domains, frequently referred to as membrane ‘rafts’. Biological functions attributed to CDMs include signal transduction. In T-cells, CDMs function in the regulation of the Src family kinase Lck (p56lck) by sequestering Lck from its activator CD45. Despite evidence of discrete CDM domains with specific functions, the mechanism by which they form and are maintained within a fluid and dynamic lipid bilayer is not completely understood. In the present chapter, we discuss recent advances showing that the actomyosin cytoskeleton has an integral role in the formation of CDM domains. Using Lck as a model, we also discuss recent findings regarding cytoskeleton-dependent CDM domain functions in protein regulation.


Planta Medica ◽  
2011 ◽  
Vol 77 (12) ◽  
Author(s):  
N Miceli ◽  
MF Taviano ◽  
A Trovato ◽  
R De Pasquale ◽  
P Maimone ◽  
...  

Planta Medica ◽  
2014 ◽  
Vol 80 (16) ◽  
Author(s):  
D Moreira ◽  
F Candido ◽  
M Siqueira ◽  
C Quaresma ◽  
E Guimarâes ◽  
...  

Planta Medica ◽  
2014 ◽  
Vol 80 (16) ◽  
Author(s):  
CA Aguiar ◽  
AM Ferreira ◽  
R Oliveira ◽  
F Baltazar ◽  
A Cunha

Planta Medica ◽  
2015 ◽  
Vol 81 (16) ◽  
Author(s):  
S Combrinck ◽  
J Linde ◽  
A Ludwiczuk ◽  
S Van Vuuren ◽  
J Van Rooy ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document