Xenotransplantation of Galactosyl-Transferase Knockout, CD55, CD59, CD39, and Fucosyl-Transferase Transgenic Pig Kidneys Into Baboons

2011 ◽  
Vol 43 (9) ◽  
pp. 3426-3430 ◽  
Author(s):  
S. Le Bas-Bernardet ◽  
X. Tillou ◽  
N. Poirier ◽  
N. Dilek ◽  
M. Chatelais ◽  
...  

Author(s):  
Ichiro Yamamoto ◽  
Toshiaki Tachibana ◽  
Hiroko Maruyama ◽  
Noriyuki Komatsu ◽  
Hiroyuki Kuramoto ◽  
...  

We have paid attention to the alteration of glycosyltransferase in carcinoma cells, because it might be related to the malignancy of the cells. In this connection, localization of β1-4 galactosyl transferase (β1-4 Gal T) in human endometrial carcinoma cells was examined immunocytochemically using two kinds of cell lines, each of which showed different degree of differentiation.An antibody was purified from the rabbit antiserum against the synthetic peptide, IFNRLVFRGMSC (W89) of human β1-4 Gal T coupled with KLH (keyhole limpet hemocyanine) by protein A column and peptide-affinity column chromatography. The anti-W89 serum reacts to the C-terminus of human β 1-4 Gal T and to both membrane-bound and soluble forms of the enzyme. Cell line of well differentiated endometrial adenocarcinoma (I) and that of poorly differentiated endometrial adenocarcinoma (50B) were cultivated respectively in MEM medium containing 15% FCS and 2 mM glutamine for 4 d at 37°C under 5% CO2. The cells were fixed in a mixture of 4% paraformaldehyde and 0.1% glutaraldehyde in 0.1 M Soerensen’s phosphate buffer (pH 7.4) at 4°C for 30 min, washed with PBS, then freezed and thawed. The indirect method of the peroxidase- labeled antibody technique was used for immunocytochemistry of both LM and TEM on the cell lines. The cells were dehydrated in ethanol and embedded in TAAB 812. Ultrathin sections were observed under a TEM, JEM-100S.





Nature ◽  
1992 ◽  
Vol 357 (6379) ◽  
pp. 589-593 ◽  
Author(s):  
David J. Miller ◽  
Mary B. Macek ◽  
Barry D. Shur


2011 ◽  
Vol 12 (1) ◽  
pp. 22 ◽  
Author(s):  
Marion Meixner ◽  
Julia Jungnickel ◽  
Claudia Grothe ◽  
Volkmar Gieselmann ◽  
Matthias Eckhardt


2019 ◽  
Vol 124 ◽  
pp. 263-275 ◽  
Author(s):  
Paola Crociara ◽  
Maria Novella Chieppa ◽  
Elena Vallino Costassa ◽  
Elena Berrone ◽  
Marina Gallo ◽  
...  


1982 ◽  
Vol 60 (7) ◽  
pp. 1054-1059 ◽  
Author(s):  
John A. Webb

An enzyme synthesizing galactinol, UDP-D-galactose:myo-inositol-1-α-D-galactosyl transferase (galactinol synthase), has been isolated and partially purified from mature leaves of Cucurbita pepo. The enzyme showed optimal activity between pH 7.5 and 8.0 and required Mn2+ and the presence throughout isolation, storage, and assay of a sulfhydryl protectant (β-mercaptoethanol). EDTA was completely inhibitory. From a range of metal ions only Mg2+ partially replaced Mn2+, while Co2+, Zn2+, Cu2+, and Ni2+ were inhibitory. The uridine nucleotides and UDP-glucose were from 40 to 80% inhibitory and probably constitute part of the in vivo control system. High concentrations of galactose, melibiose, and xylose were partially inhibitory. The enzyme appeared highly specific for myo-inositol and showed no ability for galactosyl transfer to any other naturally occurring sugar or sugar alcohol. Some reactivity was obtained with the isomeric scyllo-inositol but the product was not identified. A range of other sugar nucleotides were unreactive.



2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Mariana Sponchiado ◽  
Yan‐Shin Liao ◽  
Anna Spate ◽  
Lee Spate ◽  
Raissa Cecil ◽  
...  


The Lancet ◽  
1993 ◽  
Vol 342 (8862) ◽  
pp. 45 ◽  
Keyword(s):  


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