Cationic colloidal gold assisting delivery of macromolecular fluoresceins into target CHO-K1 cells by focused femtosecond laser

2007 ◽  
Author(s):  
Zheng Li ◽  
Zhenxi Zhang ◽  
Xiaochao Qu ◽  
Jing Wang ◽  
Gereon Hüttmann
1986 ◽  
Vol 34 (5) ◽  
pp. 693-696 ◽  
Author(s):  
E Skutelsky ◽  
J Roth

Particles of colloidal gold were coated with poly-L-lysine to prepare cationic colloidal gold. Monodispersed colloidal gold with a particle diameter of 5, 8, or 15 nm and poly-L-lysine with a molecular weight of 350,000 or 1500-8000 were used. The resulting complexes were used to label red blood cell membranes. The labeling was sensitive to neuraminidase treatment or acid hydrolysis, demonstrating that cationic colloidal gold binds preferentially to anionic cell surface constituents. Cationic colloidal gold can be used at physiological pH values and ionic strength, as well as at low pH values, making it a flexible probe for detection of anionic cellular components.


1999 ◽  
Vol 47 (7) ◽  
pp. 881-887 ◽  
Author(s):  
Dong-Hua Yang ◽  
Shinichiro Tsuyama ◽  
Jun Ohmori ◽  
Fusayoshi Murata

Parasitology ◽  
1998 ◽  
Vol 116 (6) ◽  
pp. 511-518 ◽  
Author(s):  
C. T. LIU ◽  
R. F. HOU ◽  
C. C. CHEN

The encapsulation of microfilariae in the haemocoels of mosquitoes combines both humoral and cellular reactions: the microfilariae are first encased in an acellular layer of melanin, followed by a cellular encapsulation by plasmatocytes. In this study, we demonstrated that cellular encapsulation of Brugia pahangi microfilariae in the haemocoel of the mosquito Anopheles quadrimaculatus was terminated by the formation of a basement membrane-like structure on the outermost surface of the cellular capsule. This structure occurred in the early stage of cellular encapsulation and was evident on the exterior surface of the plasmatocyte, when the active haemocytes were attaching to the already melanized microfilariae. The termination structure appears to be laid down by releasing the vesicle inclusions of haemocytes and has similarities in ultrastructure and cationic colloidal gold staining properties with that of mosquito basement membranes.


Author(s):  
Stéphane Roy ◽  
William S. Conway ◽  
Alley E. Watada ◽  
Christopher D. Pooley ◽  
William P. Wergin

The ripening of fleshy fruits involves a softening process that consists of biochemical changes in the cell wall and leads to cell separation. Calcium is an important constituent of the cell wall and plays roles in maintaining the firmness of fruit and in reducing postharvest decay. The modification of cell wall strength is believed to be influenced by calcium that interacts with acidic pectic polymers to form crossbridges. This study examined how the frequency and distribution of anionic binding sites in the cell walls of apple fruit were influenced by calcium infiltration.Mature “Golden Delicious” apple fruits were pressure infiltrated with either H2O or a 4% solution of CaCl2 and the pericarp was sampled and processed according to standard procedures. Cationic poly-Llysine colloidal gold complex was used in a one-step procedure to visualize anionic sites in muro. Observations were performed with light microscopy, following silver intensification, and with transmission electron microscopy.


1993 ◽  
Vol 41 (8) ◽  
pp. 1197-1207 ◽  
Author(s):  
K Saga ◽  
M Takahashi

We localized anionic sites ultrastructurally in human eccrine and apocrine sweat glands with a poly-L-lysine-gold complex (cationic colloidal gold). Anionic sites were labeled by incubating Lowicryl K4M-embedded sections on droplets of cationic colloidal gold. In eccrine sweat glands, colloidal gold particles were restricted to the basolateral membrane of the secretory cells at low pH, whereas the luminal membrane did not react with the gold particles. Chondroitinase ABC digested these anionic sites. This indicates that chondroitin sulfate and/or dermatan sulfate constitutes anionic sites in the basal labyrinth of eccrine sweat glands. In apocrine sweat glands, the luminal membrane of the secretory cells showed strong reaction at low pH, whereas the contraluminal membrane did not show any reaction. Neuraminidase completely digested these anionic sites, which indicated that the anionic charge of the apocrine lumen was due to sialic acid. Differences in distribution and susceptibility to enzymes of anionic sites in cell membranes between eccrine and apocrine sweat glands may reflect functional differences between these glands. Dark cell granules in eccrine secretory cells were negative for the anionic sites when sections were labeled without any pre-treatment. However, pre-incubation of the grids on EGTA or deionized water unmasked the anionic sites on the dark cell granules. The positive staining after EGTA treatment was greatly decreased by reincubation with CaCl2. These results suggested that Ca blocked anionic sites in dark cell granules. Exposed anionic sites were digested with chondroitinase ABC. This indicated that chondroitinase ABC and/or dermatan sulfate composed the anionic sites in dark cell granules.


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