Abstract: This disclosure demonstrates a novel therapy immunological approach using polyamine-based therapy (PBT) for relieving tumor-induced suppression of the patient's immune system. The demonstration of the pharmacological release from the naturally occurring polyamine-mediated immune suppression offers profound impact on the immunotherapy of cancer together with a variety of diseases caused by the disease-causing vector's ability to evade an immune reaction. This therapeutic approach is equally applicable to disease states whereby immune system suppression by polyamines has been demonstrated including; bacterial infections, parasitic infections including malaria and typanosomiasis, viral infections, peptic ulcers and gastric cancer due to H. Pylori infection together with prevention of pregnancy. With a small molecule drug, used in combination with DFMO, the pharmacological manipulation of polyamine levels for therapeutic benefit in various disease states is possible.

Abstract: This disclosure demonstrates a novel therapy immunological approach using polyamine-based therapy (PBT) for relieving tumor-induced suppression of the patient's immune system. The demonstration of the pharmacological release from the naturally occurring polyamine-mediated immune suppression offers profound impact on the immunotherapy of cancer together with a variety of diseases caused by the disease-causing vector's ability to evade an immune reaction. This therapeutic approach is equally applicable to disease states whereby immune system suppression by polyamines has been demonstrated including; bacterial infections, parasitic infections including malaria and typanosomiasis, viral infections, peptic ulcers and gastric cancer due to H. Pylori infection together with prevention of pregnancy. With a small molecule drug, used in combination with DFMO, the pharmacological manipulation of polyamine levels for therapeutic benefit in various disease states is possible.

Abstract: The invention includes kits and methods for assessing the susceptibility of a mammal such as a human for carcinogenesis. The methods comprise determining whether the mammal comprises a certain allele of the mammal's odc gene. The methods include use of a probe which binds specifically with a portion of one allele of the odc gene and which comprises a fluorescent label and a fluorescence quencher. The methods also include use of such a probe and a polymerase enzyme for amplifying a portion of the odc gene, the polymerase having exonuclease activity whereby the probe can be nucleolytically degraded.

Abstract: The invention includes kits and methods for assessing the susceptibility of a mammal such as a human for carcinogenesis. The methods comprise determining whether the mammal comprises a certain allele of the mammal's odc gene. The methods include use of a probe which binds specifically with a portion of one allele of the odc gene and which comprises a fluorescent label and a fluorescence quencher. The methods also include use of such a probe and a polymerase enzyme for amplifying a portion of the odc gene, the polymerase having exonuclease activity whereby the probe can be nucleolytically degraded.

Abstract: The invention includes kits and methods for assessing the susceptibility of a mammal such as a human for carcinogenesis. The methods comprise determining whether the mammal comprises a certain allele of the mammal's odc gene. The methods include use of a probe which binds specifically with a portion of one allele of the odc gene and which comprises a fluorescent label and a fluorescence quencher. The methods also include use of such a probe and a polymerase enzyme for amplifying a portion of the odc gene, the polymerase having exonuclease activity whereby the probe can be nucleolytically degraded.

Abstract: The invention features a transgenic mammal encoding a chimeric ornithine decarboxylase gene, which transgenic mammal exhibits phenotypic abnormalities. The invention also includes a chimeric transgene comprising ornithine decarboxylase.

Abstract: Monoclonal anti-ornithine decarboxylase antibody is produced by cell hybrids between hypoxanithine phosphoriboxyltransferase deficient myeloma cells and spleen cells derived from an animal previously immunized with ornithine decarboxylase. By means of immunoaffinity chromatography using cyanogen bromide-activated agarose coupled with the antibody, ornithine decarboxylase in animal cell extracts can be highly purified in high yield.