Disease relevance of LOC396192

• The transforming gene of avian sarcoma virus UR2, v-ros, encodes a receptor-like protein tyrosine kinase and differs from its proto-oncogene, c-ros, in its 5' truncation and fusion to viral gag, a three-amino-acid (aa) insertion in the transmembrane (TM) domain, and changes in the carboxyl region [1].

High impact information on LOC396192

• Proto-oncogene c-ros codes for a molecule with structural features common to those of growth factor receptors and displays tissue specific and developmentally regulated expression [2].
• Comparison of the deduced amino acid sequences of c-ros and v-ros shows two differences: v-ros contains a three-amino-acid insertion within the hydrophobic domain presumed to be involved in membrane association, and (ii) the carboxyl 12 amino acids of v-ros are completely different from those of the deduced c-ros sequence [2].
• Finally, nucleotide sequences of c-ros DNA and UR2-associated helper viral genome at regions corresponding to the gag ros recombination site suggest that the junction has been formed by RNA splicing [2].
• The deduced amino acid sequence of c-ros bears striking structural features similar to those of insulin and epidermal growth factor receptors, including the presumed hydrophobic membrane binding domain, amino acids flanking the domain, and the distance between the domain and the catalytic region of the kinase activity [2].
• Heteroduplex mapping and nucleotide sequencing reveal that the v-ros sequences are distributed in nine exons ranging from 65 to 204 nucleotides on cellular ros (c-ros) DNA over a range of 11 kilobases [2].

Biological context of LOC396192

• Our results suggest that c-ros may play a role not only in the initial induction events in the organogenesis, but also in the mature function of those organs [3].
• Primer extension and RNase protection analysis were used to map the transcription initiation site for the c-ros mRNA in kidney and intestine [4].
• Serial deletions of this putative c-ros promoter allowed us to define a minimum c-ros promoter and to identify positive and negative regulatory regions [4].
• Among the cellular proto-oncogenes related to the four ASV transforming genes, c-ros most likely codes for a growth factor receptor-like molecule [5].

Anatomical context of LOC396192

• Confirming our earlier study, we found that kidney is the organ that expresses the highest level of c-ros mRNA, in addition, we found a lower level of expression in gonad, thymus, bursa and brain [6].
• In kidney c-ros was detected in all the epithelial cells of the collecting ducts, in intestine it was detected in the epithelial cells of villi and the underneath crypts [3].
• Our results showed that in addition to kidney and intestine, low levels of c-ros mRNA could also be detected in lung, testis, thymus and bursa [3].
• Those investigators suggested that c-ros may play a role in the development of those organelles [3].

Other interactions of LOC396192

• The predicted amino acid sequence of the chicken c-ros protein differs by 25% from that of its closest known human counterparts within the tyrosine protein kinase catalytic domain, and by 66% downstream of this domain [7].
• Using hybridization probes synthesized from the cDNA clones, a c-ros mRNA transcript of approximately 8.3 kb was detected in chicken kidney RNA, but not in chick embryo fibroblast RNA [7].
• The native c-ros protein has a very low protein tyrosine kinase activity, whereas the ppcros protein is constitutively activated in kinase activity [1].
• To provide information about oncogenes for molecular biological studies of tumors in domestic animals, the proto-oncogenes homologous to the c-myc, c-erbB-2, c-ros-1, c-yes-1, v-myc, v-Ki-ras, and v-Ha-ras oncogenes of genomic DNA in cattle, horses, pigs, dogs, cats, and chickens were investigated by Southern blot hybridization [8].

Analytical, diagnostic and therapeutic context of LOC396192

• Sequence analysis of these clones showed that they were all derived from c-ros mRNA [7].
• In the present study, we have examined the expression profile of c-ros in chicken by RNAase protection and in situ hybridization with riboprobes [3].

References