A complete complementary DNA for the oncodevelopmental calcium-binding protein, oncomodulin

• Published in: The Journal of biological chemistry 1987-04, Vol.262 (11), p.5308-5312
• Main Authors: Gillen, M.F., Banville, D., Rutledge, R.G., Narang, S., Seligy, V.L., Whitfield, J.F., MacManus, J.P.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Calcium-Binding Proteins - genetics; Cell Line; DNA - analysis; Fundamental and applied biological sciences. Psychology; Genes. Genome; Humans; Liver Neoplasms, Experimental - genetics; Liver Neoplasms, Experimental - metabolism; Molecular and cellular biology; Molecular genetics; Nucleic Acid Hybridization; Rats; Rats, Inbred BUF; Rats, Inbred Strains
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)61189-5

RNA from a rat liver tumor (Morris hepatoma 5123tc) was used to construct cDNAs together comprising the complete coding sequence of rat oncomodulin mRNA. Information obtained from these cDNAs as well as from primer extension analysis gave a deduced length for the complete oncomodulin mRNA of approximately 680 nucleotides (excluding the poly(A) tail) including a 5′-untranslated region of 97 +/- 2 nucleotides, a 324-nucleotide-coding sequence and a 259-nucleotide 3′-noncoding region. Comparison of the oncomodulin cDNA sequence with those coding for other members of the calcium-binding protein family shows little homology with the exception of a recently reported parvalbumin cDNA where the oncomodulin and parvalbumin nucleotide sequences are 59% identical in the protein-coding region. RNA blot analysis of poly(A+) RNA from normal adult rat liver gave no evidence of oncomodulin expression in this tissue. A single RNA species was detected, however, in RNA extracts from the hepatoma and from rat and human placentas. A probe prepared from one of the rat oncomodulin cDNAs hybridized with a single DNA species in restriction digests of hepatoma and normal DNA from rat and sequences in DNA of humans and other mammals. A 38-nucleotide sequence spanning the 5′-untranslated region and the first seven codons of the oncomodulin cDNA, was far less homologous than was the same region of a parvalbumin cDNA, to a chicken calmodulin cDNA sequence coding for the first calcium-binding domain. The oncomodulin gene appears to have diverged more from that of calmodulin than has the parvalbumin gene.