Multiplicity of protein serine-threonine phosphatases in PC12 pheochromocytoma and FTO-2B hepatoma cells.

Wadzinski BE, Heasley LE, Johnson GL
J Biol Chem. 1990 265 (35): 21504-8

PMID: 2174876

Protein purification and molecular cloning have defined five classes of protein serine-threonine phosphatase catalytic subunits referred to as types 1, 2A, 2B (calcineurin), 2C, and X. Protein serine-threonine phosphatases 1, 2A, 2B, and X appear to have significant sequence homologies, whereas the 2C enzyme is more divergent. We have used the polymerase chain reaction to define the multiplicity of the closely related types 1, 2A, 2B, and X phosphatase catalytic subunits in two clonal cell lines, rat PC12 pheochromocytoma and rat FTO-2B hepatoma. RNAs for all four related phosphatase types were expressed in both cell lines. In addition to the phosphatase X enzyme, four phosphatase 1, two phosphatase 2A, and three phosphatase 2B isoforms were identified in PC12 and FTO-2B cells. The results indicate a large multiplicity of protein serine-threonine phosphatases within clonal cells of different tissue origin, suggesting that their role in cell regulation will be as divergent as that for the protein serine-threonine kinases.

MeSH Terms (19)

Adrenal Gland Neoplasms Amino Acid Sequence Animals Base Sequence Clone Cells Cloning, Molecular Humans In Vitro Techniques Liver Neoplasms Liver Neoplasms, Experimental Molecular Sequence Data Peptide Fragments Pheochromocytoma Phosphoprotein Phosphatases Polymerase Chain Reaction Protein Phosphatase 1 Protein Phosphatase 2 Rats Tumor Cells, Cultured

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