Phosphorylation of human lysosomal arylsulfatase B by cAMP-dependent protein kinase. Different sites of phosphorylation between normal and cancer tissues.

@article{Gasa1987PhosphorylationOH,
  title={Phosphorylation of human lysosomal arylsulfatase B by cAMP-dependent protein kinase. Different sites of phosphorylation between normal and cancer tissues.},
  author={Shinsei Gasa and M Balbaa and Mitsuhiro Nakamura and Hironobu Yonemori and Akira Makita},
  journal={The Journal of biological chemistry},
  year={1987},
  volume={262 3},
  pages={1230-8}
}
We previously demonstrated that an acidic variant (B1) of lysosomal arylsulfatase B from transplanted human lung cancer is phosphorylated on its protein and carbohydrate moieties (Gasa, S., and Makita, A. (1983) J. Biol. Chem. 258, 5034-5039). The present study identifies that a cAMP-dependent protein kinase is responsible for phosphorylation of arylsulfatase B. The protein kinase activity toward the sulfatase was considerably higher in the transplanted lung cancer than in normal lung in the… CONTINUE READING
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