Title : Anti-CD2-induced tyrosine phosphorylation of T cell polypeptides is independent of the PMA-induced modification of p56lck.

Pub. Date : 1993 Mar

PMID : 8096437






5 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Anti-CD2-induced tyrosine phosphorylation of T cell polypeptides is independent of the PMA-induced modification of p56lck. Tyrosine CD2 molecule Homo sapiens
2 While polypeptides from resting T cells showed very low levels of endogenous tyrosine phosphorylation, incubation with anti-CD2 for periods as short as 30 sec resulted in the tyrosine phosphorylation of a 75-kDa polypeptide (p75). Tyrosine CD2 molecule Homo sapiens
3 While polypeptides from resting T cells showed very low levels of endogenous tyrosine phosphorylation, incubation with anti-CD2 for periods as short as 30 sec resulted in the tyrosine phosphorylation of a 75-kDa polypeptide (p75). Tyrosine CD2 molecule Homo sapiens
4 Preincubation of T cells with phenylarsine oxide amplified the anti-CD2-induced tyrosine phosphorylation of the p75 and revealed additional phosphotyrosine polypeptides of 120, 100, and 33 kDa. Tyrosine CD2 molecule Homo sapiens
5 Whereas PMA with either anti-CD2 or Con A was required for mitogenesis, only anti-CD2 led to tyrosine phosphorylation, and only PMA induced the lck-shift. Tyrosine CD2 molecule Homo sapiens