Chicken cells

Mege RM, Matsuzaki F, Gallin WF, Golber , Cunningham BA, Edelman GM Construction of epithelioid sheets by transfection of mouse sarcoma cells with cDNAs for chicken cell adhesion molecules. Proc Natl Acad Sci USA 1988 85 7274-7278. 

Although the DNA-binding properties of several procaryotic topoisomerases have been well characterized, little information is currently available concerning eucaryotic enzymes. Some eucaryotic topoisomerases may be intimately associated with other nuclear proteins HeLa topoisomerases I and II have been found to be associated with chromatin (Javaherian and Liu, 1983 Liu et al., 1983b). HeLa topoisomerase I has been shown to bind to the nonhistone protein HMG17, which also stimulates DNA catenation by the enzyme (Javaherian and Liu, 1983 Tse et al., 1984). It has been suggested that type II topoisomerase is an important component of the chromosomal scaffold in interphase nuclei and mitotic chromosomes from chicken cell lines (Earnshaw et al., 1985). In addition, an ATP-dependent topoisomerase has been found associated with several other enzymes of DNA metabolism in a complex (termed the replitase complex) isolated from the nuclei of Chinese hamster embryo fibroblast cells (Noguchi et al., 1983). 

AlumetSjJ., Hakanson, R. Sundler, F. (1978) Distribution, ontogeny and ultrastructure of pancreatic polypeptide (PP) cells in pancreas and gut of the chicken. Cell Tissue Res. 194,377 386. 

Hirai, H. Varmus, H.E. (1990). Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse and chicken cells. Proc. Natl Acad. Scl USA, 87, 8592-6. 

Further investigations of ascorbate inhibition of virus replication have been carried out using retroviruses as models. Bissell et al. (1980), working with the avian retrovirus of chickens, found that while cell-free virus was resistant to ascorbate inactivation upon short-term treatment in vitro, exposure of virus-infected cultures to the vitamin resulted in reduction of virus replication and lowered infec-tivity of newly replicated virus. A subsequent study found that ascorbate interfered with the replication and cell-transforming potential of Rous sarcoma virus by stabilizing the differentiated state of chicken cells (Schwarz, 1991). In a lymphocytic cell line latently infected with human T-cell leukemia virus (HTLV-1), ascorbate was shown to interfere with virus production triggered by chemical inducers added to the culture medium (Blakeslee et al., 1985). 

Normal chicken cells, carrying the chicken-helper factor, express a surface glycoprotein which is antigenically cross-reactive with determinants of the major envelope glycoprotein of avian myeloblastosis virus. ... 

Fig. 8.3. Agglutination reactions of mixtures of chicken erythrocytes (oval and nucleated) and human erythrocytes (disc-shaped) the chicken cells were eoated with bovine IgG (BGG) and the human cells with hen ovalbumin. The following rabbit F(ab >2 fragments were present in the mixtures A, antiovalbumin B, anti-BGG C, mixture of antiovalbumin and anti-BGG D, hybrid preparation of antiovalbumin and anti-BGG. From reference 94.

Anti-poly G poly C reacts with total RNA extracted from chicken cells, mouse ascites cells, hamster tumor, rabbit kidney, sheep liver and human tumor (Table 7). Since no precipitation occurs with tRNA extracted from the same cells, these reactions must occur with ribosomal RNA. Preincubation of the RNA (mouse ascites cells) with pancreatic RNAase abolishes the reaction completely. Secondary structure plays a role in this immunoreaction since heating the RNA with 1% formaldehyde for 10 min at 100°C, followed by rapid cooling, also abolishes precipitation with the antibody. Lack of activity of tRNA (leukemic chicken myeloblasts) is not modified by this treatment (Nahon-Merlin et al., 1971). 

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