BRK protein tyrosine kinase and encoding nucleic acid

Details BRK protein tyrosine kinase and encoding nucleic acid BRK protein tyrosine kinase and encoding nucleic acid

1996-06-10

2000-04-18

Spector, Lorraine

Drug, bio-affecting and body treating compositions

Enzyme or coenzyme containing

Stabilized enzymes or enzymes complexed with nonenzyme

424 941, 435 691, 4353201, 435325, 4352523, 43525411, 530300, 530350, 536 231, 536 232, 536 235, A61K 3843, C12N 1512, C12N 1511, C12N 510

Patent

active

060512210

DESCRIPTION:

BRIEF SUMMARY
FIELD OF THE INVENTION

The present invention relates to a putative signalling molecule. More particularly the invention relates to a novel tyrosine kinase and the use of this tyrosine kinase in the development of diagnostic and therapeutic approaches to cancer, for example breast cancer.


BACKGROUND OF THE INVENTION

Protein tyrosine kinases are enzymes which show the property of catalysing the transfer of phosphate groups from donor molecules (ATP) to the hydroxyl groups of tyrosine residues in polypeptides. Known tyrosine kinases can be classified into two broad groups. Transmembrane tyrosine kinases traverse cellular membranes so that they possess extracellular and intracellular domains. Cytoplasmic tyrosine kinases are located only intracellularly. A general feature of transmembrane (also referred to as receptor) tyrosine kinases is that they possess extracellular ligand-binding domains, hydrophobic transmembrane sequences, and intracellular portions which include the tyrosine kinase domains (for a review see Ullrich & Schlessinger Cell, 61, 203-212 (1990)).
Tyrosine kinases can induce cell proliferation, cell transformation and regulate developmental events (see reviews by Hanks et al, Science, 241, 42-75 (1988) and Cantley et al, Cell 64, 281-302 (1991)). In general, where functional assays have been available (e.g. mitogenesis or transformation), it has been shown that the biological functions of tyrosine kinases are usually dependent on intact enzyme activity and that through autophosphorylation and the phosphorylation of other proteins, they alter the subcellular localisation and activities of various components of the intracellular signalling pathways.
Analysis of the oncogenes of many acutely transforming animal retroviruses has revealed that their products frequently manifest tyrosine kinase activity, as do the products of their cellular proto-oncogene counterparts. Other genes encoding tyrosine kinases have been found to be altered by DNA rearrangements in cancer cells, the result being a presumed acquisition of cellular transforming activity (for example c-abl, c-met). Some cellular proto-oncogenes encoding tyrosine kinases have been cloned independently by virtue of the fact that they encode growth factor receptors, for example the epidermal growth factor receptor. On the other hand, the genes for other growth factor receptors which have tyrosine kinase activities, such as those for platelet-derived growth factor and insulin-like growth factors, have been well characterised, but have never been found to be transduced by retroviruses.
The c-erbB-2/HER2/c-neu gene encodes a transmembrane receptor-like tyrosine kinase which is structurally very similar to the EGF/TGF alpha receptor. The c-erbB-2 gene has been found to be overexpressed in 20 to 30% of human breast tumours, often in association with gene amplification, and this phenotype is now generally accepted as predictive of poor disease free and overall survival (for reviews see Sunderland & McGuire in Regulatory Mechanisms in Breast Cancer, Lippman & Dickson (Eds.), Kluwer Academic Publishers, Boston, pages 3 to 22 (1991) and Gusterson et al., J. Clin. Oncol., 10, 1049-1056 (1992)). Overexpression of the gene in fibroblasts induces transformation (di Fiore et al, Science, 237, 178-182 (1987) and Hudziak et al, Proc. Natl. Acad. Sci. (USA), 84, 7159-7162 (1987)), and ligands which bind to the c-erbB-2 gene product (human and rodent) and activate its tyrosine kinase activity have been identified (Lupu et al, Science, 249, 1552-1555 (1990), Dobashi et al, Proc. Natl. Acad, Sci. (USA), 88, 8582-8586 (1991), Wen et al, Cell, 69, 559-572 (1992) and Holmes et al, Science 256, 1205-1210 (1992)). Some of these ligands increase the rate of proliferation of cells expressing the c-erbB-2 protein. The strong implication of these and other findings is that overexpression of this tyrosine kinase in some breast tumour cells is one of the important steps in their progression towards tumourigenicity, and therefore that c-erbB-2 can function as an oncogene

REFERENCES:
patent: 5480968 (1996-01-01), Kraus et al.
Stephens et al Lance vol. 2(8192): pp. 435-438 Aug. 30, 1997.

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