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Spleen protein tyrosine kinases TPK‐IIB and CSK display different immunoreactivity and opposite specificities toward c‐ src ‐derived peptides
Author(s) -
Brunati Anna Maria,
Allee Guillaume,
Marin Oriano,
Donella-Deana Arianna,
Cesaro Luca,
Bougeret Cecile,
Fagard Remi,
Benarous Richard,
Fischer Siegmund,
Pinna Lorenzo A.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81212-5
Subject(s) - tyrosine protein kinase csk , proto oncogene tyrosine protein kinase src , sh3 domain , tyrosine , tyrosine kinase , kinase , chemistry , receptor tyrosine kinase , biochemistry , microbiology and biotechnology , biology , signal transduction
Polyclonal antibodies have been raised against two synthetic peptides reproducing the 48–64 and 353–369 sequences of CSK, a protein tyrosine kinase implicated in the down‐regulation of src ‐related protein kinases. Both antibodies specifically recognize recombinant CSK and a CSK‐related 49 kDa protein tyrosine kinase present in spleen but they do not cross‐react with purified TPK‐IIB, a spleen protein tyrosine kinase sharing with CSK catalytic activity toward src kinases and incapability to autophosphorylate. CSK and TPK‐IIB once resolved from each other by heparin‐Sepharose affinity chromatography, display opposite specificities toward synthetic peptides reproducing the sequences around the main phosphoacceptor residues of pp6O c src , namely Tyr‐416 and Tyr‐527. These data support the view that TPK‐IIB and CSK may exert opposite effects on the activity of src ‐related protein tyrosine kinases.