Tyrosine phosphorylation in human T lymphoma cells.

A high level of tyrosine protein kinase (TPK) has been recently detected in the murine lymphoma LSTRA. The main substrate for tyrosine phosphorylation in this cell line is a Mr 55 000 protein associated with the insoluble matrix of the cell. These findings prompted the search for TPK activities in human lymphoid cells. Three human T lymphoma cell lines (i.e. Molt. 4, JM, and Ke 37) and control lymphocytes were examined. After in vitro phosphorylation of detergent insoluble extracts from human T lymphoma cells, 2 major phosphotyrosine containing proteins with Mr 55 000 and 35 000 can be detected in all three T lymphoma lines, whereas an additional species with Mr 78 000 is present only in the Ke 37 cell line. Similar size proteins are weakly phosphorylated in normal lymphocytes. Tyrosine phosphorylation in these proteins proceeds actively at 0 degrees C, and is dramatically stimulated by Mn++ ions. Partial proteolysis mappings of the Mr 55 000 phosphoproteins from murine and human lymphomas revealed a strong homology among these molecules. The function of this protein in transformed lymphocytes is discussed.