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Ocm2  -  oncomodulin 2

Rattus norvegicus

Synonyms: OM, Ocm, Oncomodulin, Parvalbumin beta, oncmodulin
 
 
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Disease relevance of Ocm

  • 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 [1].
  • Oncomodulin, the parvalbumin-like calcium-binding protein frequently expressed in tumor tissue, was isolated from Morris hepatoma 5123tc and studied using the luminescent lanthanide ions, Eu3+ and Tb3+ [2].
  • It is now possible to detect, by radioimmunoassay and immunofluorescence, the presence of oncomodulin in normal rat kidney cells virally transformed by avian sarcoma virus [3].
  • By comparing the response magnitude and the effectiveness in evoking a response, the rank order for evoking excitation, the primary response, was found to be: OM > CCh > ACh approximately McN, which is consistent with that (OM > CCh > McN) for facilitating lordosis reported by others [4].
 

High impact information on Ocm

 

Biological context of Ocm

 

Anatomical context of Ocm

 

Associations of Ocm with chemical compounds

  • These findings strongly suggest that residues in oncomodulin besides aspartate 59 are important determinants of the observed calcium specificity of the CD calcium-binding domain [14].
  • Site-specific substitution of glutamate for aspartate at position 59 of rat oncomodulin [14].
  • In particular we have followed the replacement of calcium by lutetium in bacterial recombinant oncomodulin and D59E oncomodulin to provide a measure of the protein's preferences for metal ions of different ionic radii [15].
  • Oncomodulin and parvalbumin. A comparison of their interactions with europium ion [16].
  • The result of the Asp----Glu substitution is to make the mutant oncomodulin more similar to rat parvalbumin in terms of its relative CD- and EF-domain affinities for lutetium(III), that is to increase its affinity for metal ions with smaller ionic radii [15].
 

Regulatory relationships of Ocm

 

Other interactions of Ocm

  • In the present report, we substituted selected amino acid residues in the CD site of PV by those present at identical positions in OM [18].
  • The cellular levels of oncomodulin approached the levels of calmodulin in avian sarcoma virus-transformed normal rat kidney cells, suggesting that the total calcium-binding activity of the cell may play a role in expression of the transformed phenotype [3].
  • Ca2+/calmodulin dependent cyclic nucleotide phosphodiesterase, from the bovine heart and brain, purified by monoclonal antibody chromatography were tested with respect to activation by oncomodulin [17].
 

Analytical, diagnostic and therapeutic context of Ocm

  • In organ cultures isolated prior to the efferent innervation of OHCs, OM immunoreactivity failed to develop in OHCs, but alphaPV immunoreactivity remained present in both IHCs and OHCs [11].
  • Using RT-PCR analysis, we found that OM expression begins between postnatal day 2 (P2) and P4, and peaks as early as P10, while alphaPV mRNA begins expression before birth and remains highly expressed into the adult period [11].
  • 1. Lineshape analyses of several 1H NMR resonances generated by the Lu(III) titration of Ca2-oncomodulin indicated that Ca(II)----Ln(III) exchange at the CD site was 15-20 s-1, approximately 100 times faster than exchange at the CD site of parvalbumins [19].
  • Replacement of the aspartate residue at position 59 of rat oncomodulin by glutamate by oligonucleotide-directed mutagenesis has afforded a protein which more closely resembles rat parvalbumin, at least judged by its interaction with the luminescent lanthanide ion Eu3+ [14].
  • However, when examined by differential scanning calorimetry, the apo-form of the rat beta-PV (i.e. oncomodulin) actually displays greater thermal stability than the alpha-PV [20].

References

  1. A complete complementary DNA for the oncodevelopmental calcium-binding protein, oncomodulin. Gillen, M.F., Banville, D., Rutledge, R.G., Narang, S., Seligy, V.L., Whitfield, J.F., MacManus, J.P. J. Biol. Chem. (1987) [Pubmed]
  2. Lanthanide-binding properties of rat oncomodulin. Henzl, M.T., Hapak, R.C., Birnbaum, E.R. Biochim. Biophys. Acta (1986) [Pubmed]
  3. Occurrence of the tumor-specific, calcium-binding protein, oncomodulin, in virally transformed normal rat kidney cells. Durkin, J.P., Brewer, L.M., MacManus, J.P. Cancer Res. (1983) [Pubmed]
  4. In vitro electro-pharmacological and autoradiographic analyses of muscarinic receptor subtypes in rat hypothalamic ventromedial nucleus: implications for cholinergic regulation of lordosis. Kow, L.M., Tsai, Y.F., Weiland, N.G., McEwen, B.S., Pfaff, D.W. Brain Res. (1995) [Pubmed]
  5. Oncomodulin is a macrophage-derived signal for axon regeneration in retinal ganglion cells. Yin, Y., Henzl, M.T., Lorber, B., Nakazawa, T., Thomas, T.T., Jiang, F., Langer, R., Benowitz, L.I. Nat. Neurosci. (2006) [Pubmed]
  6. Retroviral long terminal repeat is the promoter of the gene encoding the tumor-associated calcium-binding protein oncomodulin in the rat. Banville, D., Boie, Y. J. Mol. Biol. (1989) [Pubmed]
  7. The complete amino acid sequence of oncomodulin--a parvalbumin-like calcium-binding protein from Morris hepatoma 5123tc. MacManus, J.P., Watson, D.C., Yaguchi, M. Eur. J. Biochem. (1983) [Pubmed]
  8. Remodeling of the AB site of rat parvalbumin and oncomodulin into a canonical EF-hand. Cox, J.A., Durussel, I., Scott, D.J., Berchtold, M.W. Eur. J. Biochem. (1999) [Pubmed]
  9. Calmodulin-like effect of oncomodulin on cell proliferation. Blum, J.K., Berchtold, M.W. J. Cell. Physiol. (1994) [Pubmed]
  10. Interactions between residues in the oncomodulin CD domain influence Ca2+ ion-binding affinity. Treviño, C.L., Boschi, J.M., Henzl, M.T. J. Biol. Chem. (1991) [Pubmed]
  11. Expression of alpha and beta parvalbumin is differentially regulated in the rat organ of corti during development. Yang, D., Thalmann, I., Thalmann, R., Simmons, D.D. J. Neurobiol. (2004) [Pubmed]
  12. The concentrations of calcium buffering proteins in mammalian cochlear hair cells. Hackney, C.M., Mahendrasingam, S., Penn, A., Fettiplace, R. J. Neurosci. (2005) [Pubmed]
  13. Expression of the tumor-specific and calcium-binding protein oncomodulin during chemical transformation of rat fibroblasts. Sommer, E.W., Heizmann, C.W. Cancer Res. (1989) [Pubmed]
  14. Site-specific substitution of glutamate for aspartate at position 59 of rat oncomodulin. Hapak, R.C., Lammers, P.J., Palmisano, W.A., Birnbaum, E.R., Henzl, M.T. J. Biol. Chem. (1989) [Pubmed]
  15. Site-specific mutants of oncomodulin. 1H NMR and optical stopped-flow studies of the effect on the metal binding properties of an Asp59----Glu59 substitution in the calcium-specific site. Golden, L.F., Corson, D.C., Sykes, B.D., Banville, D., MacManus, J.P. J. Biol. Chem. (1989) [Pubmed]
  16. Oncomodulin and parvalbumin. A comparison of their interactions with europium ion. Henzl, M.T., Birnbaum, E.R. J. Biol. Chem. (1988) [Pubmed]
  17. The differential stimulation of brain and heart cyclic-AMP phosphodiesterase by oncomodulin. Mutus, B., Karuppiah, N., Sharma, R.K., MacManus, J.P. Biochem. Biophys. Res. Commun. (1985) [Pubmed]
  18. Site-specific replacement of amino acid residues in the CD site of rat parvalbumin changes the metal specificity of this Ca2+/Mg(2+)-mixed site toward a Ca(2+)-specific site. Pauls, T.L., Durussel, I., Clark, I.D., Szabo, A.G., Berchtold, M.W., Cox, J.A. Eur. J. Biochem. (1996) [Pubmed]
  19. Oncomodulin. 1H NMR and optical stopped-flow spectroscopic studies of its solution conformation and metal-binding properties. Williams, T.C., Corson, D.C., Sykes, B.D., MacManus, J.P. J. Biol. Chem. (1987) [Pubmed]
  20. Conformational stabilities of the rat alpha- and beta-parvalbumins. Henzl, M.T., Graham, J.S. FEBS Lett. (1999) [Pubmed]
 
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