Altered erythrocyte protein kinase C activity and membrane protein phosphorylation in chronic myelogenous leukemia.
The membrane protein kinase C (PKC) content was found to be higher in erythrocytes form patients suffering from chronic myelogenous leukemia (CML) compared to normal erythrocytes. PKC activity was also higher in the cytosol and after translocation to the membrane, as assessed by histone phosphorylation. The increased PKC activity in CML erythrocytes was associated with abnormal phosphorylation of protein 4.1. Since phosphorylation-dephosphorylation mechanisms are likely candidates for controlling membrane protein associations, the altered PKC activity may be one of the factors responsible for altered thermal sensitivity and mechanical stability of CML erythrocytes.
Kundu
M
M
Department of Chemistry, Bose Institute, Calcutta, India.
Basu
J
J
Fujimagari
M
M
Williamson
P
P
Schlegel
R A
RA
Chakrabarti
P
P
D003598:Cytoskeletal Proteins; D003600:Cytosol / Q000201:enzymology; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D006657:Histones / Q000378:metabolism; D006801:Humans; D015464:Leukemia, Myelogenous, Chronic, BCR-ABL Positive / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D009479:Neuropeptides; D015240:Phorbol 12,13-Dibutyrate / Q000378:metabolism; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*
D003598:Cytoskeletal Proteins; D006657:Histones; D008565:Membrane Proteins; D009479:Neuropeptides; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1; D015240:Phorbol 12,13-Dibutyrate; D011493:Protein Kinase C