Author/Authors :
Suzuki، نويسنده , , Kuniaki and Okamoto، نويسنده , , Tohru and Yoshimura، نويسنده , , Yoshitaka and Deyama، نويسنده , , Yoshiaki and Hisada، نويسنده , , Yoh and Matsumoto، نويسنده , , Akira، نويسنده ,
Abstract :
The homogenate of MC3T3-E1 cells hydrolysed phosphotyrosine, but not phosphoserine or phosphothreonine at acidic pH. It dephosphorylated lysozyme and Raytide (a gastrin analogue peptide) phosphorylated by tyrosine kinase, but showed little activity toward histones phosphorylated by cyclic AMP-dependent protein kinase. Dephosphorylation of phosphorylated lysozyme and Raytide were inhibited by zinc and vanadate, but were insensitive to okadaic acid. These data suggest that the osteoblastic cell line MC3T3-E1 has a phosphotyrosyl protein phosphatase-like activity that may participate in cellular regulation involving protein tyrosine phosphorylation.
