A HEAT LABILE FACTOR RELATED TO THE DEVELOPMENT OF RETICULUM CELL NEOPLASMS TYPE B FOLLOWING INTRAPERITONEAL INOCULATIONS OF CELL-FREE FILTRATE OF EHRLICH'S ASCITES CARCINOMA

Author(s):  
Andreas O. Myking
Author(s):  
S. Fujinaga ◽  
K. Maruyama ◽  
C.W. Williams ◽  
K. Sekhri ◽  
L. Dmochowski

Yumoto and Dmochowski (Cancer Res.27, 2098 (1967)) reported the presence of mature and immature type C leukemia virus particles in leukemic organs and tissues such as lymph nodes, spleen, thymus, liver, and kidneys of SJL/J strain mice with Hodgki's-like disease or reticulum cell neoplasm (type B). In an attempt to ascertain the possibility that this neoplasia may be of viral origin, experiments with induction and transmission of this neoplasm were carried out using cell-free extracts of leukemic organs from an SJL/J strain mouse with spontaneous disease.It has been possible to induce the disease in low-leukemia BALB/c and C3HZB strain mice and serially transfer the neoplasia by cell-free extracts of leukemic organs of these mice. Histological examination revealed the neoplasia to be of either reticulum cell-type A or type B. Serial transfer is now in its fifth passage. In addition leukemic spleen from another SJL/J strain mouse with spontaneous reticulum cell neoplasm (type A) was set up in tissue culture and is now in its 141st serial passage in vitro. Preliminary results indicate that cell-free material of 39th tissue culture passage can reproduce neoplasia in BALB/c mice.


2013 ◽  
Vol 04 (08) ◽  
pp. 1355-1361 ◽  
Author(s):  
Mohammad M. Abd-Alhaseeb ◽  
Sawsan A. Zaitone ◽  
Soad H. Abou-El-Ela ◽  
Yasser M. Moustafa

1989 ◽  
Vol 35 (6) ◽  
pp. 670-673 ◽  
Author(s):  
Shunji Sugii ◽  
Takao Tsuji

The binding specificities of heat-labile enterotoxins (LTp and LTh) isolated from porcine and human enterotoxigenic Escherichia coli on human erythrocytes were studied by competitive binding assays using different gangliosides as inhibitors. The binding of 125I–labeled LTp to neuraminidase-treated human type A erythrocytes was most effectively inhibited by ganglioside GM1 Ganglioside GM1 was 11 and 105 times more potent than gangliosides GD1b and GM2, respectively. Gangliosides GD1a, GT1b, and GM3 were much less potent. Similar results were also obtained in competitive binding assays with the 125I-labeled B subunit of LTh and neuraminidase-treated human type B erythrocytes, and in those with 3H-labeled ganglioside GM1 and LTp-coupled Sepharose 4B. The binding of 3H-labeled ganglioside GM1 to LTp was not effectively inhibited by galactose-β(1 → 3)N-acetyl-D-galactosamine at the highest concentration used. These findings suggest that the combining sites of LTp and LTh may be specific for at least the galactose-N-acetyl-D-galactosamine-galactose (N-acetyl-neuraminic acid) portion of ganglioside GM1.Key words: binding specificity, heat-labile enterotoxin, enterotoxigenic Escherichia coli, ganglioside.


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