Catalytic activity corresponding to the SYK kinase was first detected in extracts from bovine thymus based on the phosphorylation on tyrosine of a synthetic peptide substrate. Purification of this activity by conventional column chromatographic approaches led to the isolation of an enzyme with a molecular mass of 40 kDa that was originally referred to as p40 (Zioncheck et al. 1986). Shortly thereafter, the same catalytic fragment was identified and purified from porcine spleen and given the name CPTK40 (Kobayashi et al. 1990). The fact that these two kinases were actually catalytic fragments was recognized when antibodies generated against p40 revealed a larger precursor of 72 kDa, the proteolytic cleavage of which yielded the activated 40 kDa fragment (Zioncheck et al. 1988). The full-length protein was originally referred to as PTK72. Similarly, the screening of a porcine cDNA...
- Costello PS, Turner M, Walters AE, Cunningham CN, Bauer N, Downward J, et al. Critical role for the tyrosine kinase Syk in signalling through the high affinity IgE receptor of mast cells. Oncogene. 1996;12:2595–605.Google Scholar
- Taube JH, Herschkowitz JI, Komurov K, Zhou AY, Gupta S, Yang J, et al. Core epithelial-to-mesenchymal transition interactome gene-expression signature is associated with claudin low and metaplastic breast cancer subtypes. Proc Natl Acad Sci USA. 2010;107:15449–54.PubMedPubMedCentralCrossRefGoogle Scholar