Protein phosphorylation of lysosomal arylsulfatase B in normal and leukemic leukocytes.
An acidic variant form of arylsulfatase B from normal leukocytes and chronic myelogenous leukemia (CML) leukocytes was found to be phosphorylated at its serine and threonine residues through in vivo phosphorylation with 32Pi. However, the predominant phosphorylation site was serine in normal cells, in contrast to threonine in CML cells. A cyclic AMP-dependent protein kinase was responsible for phosphorylation of the sulfatase of CML cells.
Uehara
Y
Y
Gasa
S
S
Makita
A
A
Sakurada
K
K
Miyazaki
T
T
D002803:Chondro-4-Sulfatase / Q000378:metabolism*; D006801:Humans; D007951:Leukemia, Myeloid / Q000201:enzymology*; D007962:Leukocytes / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D010769:Phosphothreonine / Q000378:metabolism; D011494:Protein Kinases / Q000097:blood; D013429:Sulfatases / Q000378:metabolism*
D010769:Phosphothreonine; D010768:Phosphoserine; D011494:Protein Kinases; D013429:Sulfatases; D002803:Chondro-4-Sulfatase